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Journal articles on the topic 'Partner proteins'

Author: Grafiati
Published: 2 February 2023

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1

Sahin, Umut, Omar Ferhi, Marion Jeanne, Shirine Benhenda, Caroline Berthier, Florence Jollivet, Michiko Niwa-Kawakita, et al. "Oxidative stress–induced assembly of PML nuclear bodies controls sumoylation of partner proteins." Journal of Cell Biology 204, no. 6 (March 17, 2014): 931–45. http://dx.doi.org/10.1083/jcb.201305148.

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The promyelocytic leukemia (PML) protein organizes PML nuclear bodies (NBs), which are stress-responsive domains where many partner proteins accumulate. Here, we clarify the basis for NB formation and identify stress-induced partner sumoylation as the primary NB function. NB nucleation does not rely primarily on intermolecular interactions between the PML SUMO-interacting motif (SIM) and SUMO, but instead results from oxidation-mediated PML multimerization. Oxidized PML spherical meshes recruit UBC9, which enhances PML sumoylation, allow partner recruitment through SIM interactions, and ultimately enhance partner sumoylation. Intermolecular SUMO–SIM interactions then enforce partner sequestration within the NB inner core. Accordingly, oxidative stress enhances NB formation and global sumoylation in vivo. Some NB-associated sumoylated partners also become polyubiquitinated by RNF4, precipitating their proteasomal degradation. As several partners are protein-modifying enzymes, NBs could act as sensors that facilitate and confer oxidative stress sensitivity not only to sumoylation but also to other post-translational modifications, thereby explaining alterations of stress response upon PML or NB loss.
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2

Di, Han, Husni Elbahesh, and Margo A. Brinton. "Characteristics of Human OAS1 Isoform Proteins." Viruses 12, no. 2 (January 29, 2020): 152. http://dx.doi.org/10.3390/v12020152.

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The human OAS1 (hOAS1) gene produces multiple possible isoforms due to alternative splicing events and sequence variation among individuals, some of which affect splicing. The unique C-terminal sequences of the hOAS1 isoforms could differentially affect synthetase activity, protein stability, protein partner interactions and/or cellular localization. Recombinant p41, p42, p44, p46, p48, p49 and p52 hOAS1 isoform proteins expressed in bacteria were each able to synthesize trimer and higher order 2′-5′ linked oligoadenylates in vitro in response to poly(I:C). The p42, p44, p46, p48 and p52 isoform proteins were each able to induce RNase-mediated rRNA cleavage in response to poly(I:C) when overexpressed in HEK293 cells. The expressed levels of the p42 and p46 isoform proteins were higher than those of the other isoforms, suggesting increased stability in mammalian cells. In a yeast two-hybrid screen, Fibrillin1 (FBN1) was identified as a binding partner for hOAS1 p42 isoform, and Supervillin (SVIL) as a binding partner for the p44 isoform. The p44-SVIL interaction was supported by co-immunoprecipitation data from mammalian cells. The data suggest that the unique C-terminal regions of hOAS1 isoforms may mediate the recruitment of different partners, alternative functional capacities and/or different cellular localization.
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Krishna, Priti. "Plant Hsp90 and Its Partner Proteins." Journal of Plant Biochemistry and Biotechnology 9, no. 2 (July 2000): 53–56. http://dx.doi.org/10.1007/bf03263085.

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4

Rassow, J. "Partner proteins determine multiple functions of Hsp70." Trends in Cell Biology 5, no. 5 (May 1995): 207–12. http://dx.doi.org/10.1016/s0962-8924(00)89001-7.

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Rassow, Joachim, Wolfgang Voos, and Nikolaus Pfanner. "Partner proteins determine multiple functions of Hsp70." Trends in Cell Biology 5, no. 5 (May 1995): 207–12. http://dx.doi.org/10.1016/0962-8924(95)80013-7.

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6

Stower, Hannah. "Proteins partner up in a vigorous relationship." Nature Reviews Genetics 14, no. 12 (October 29, 2013): 822. http://dx.doi.org/10.1038/nrg3617.

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7

Pancsa, Rita, Fruzsina Zsolyomi, and Peter Tompa. "Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings." International Journal of Molecular Sciences 19, no. 11 (October 25, 2018): 3315. http://dx.doi.org/10.3390/ijms19113315.

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Although improved strategies for the detection and analysis of evolutionary couplings (ECs) between protein residues already enable the prediction of protein structures and interactions, they are mostly restricted to conserved and well-folded proteins. Whereas intrinsically disordered proteins (IDPs) are central to cellular interaction networks, due to the lack of strict structural constraints, they undergo faster evolutionary changes than folded domains. This makes the reliable identification and alignment of IDP homologs difficult, which led to IDPs being omitted in most large-scale residue co-variation analyses. By preforming a dedicated analysis of phylogenetically widespread bacterial IDP–partner interactions, here we demonstrate that partner binding imposes constraints on IDP sequences that manifest in detectable interprotein ECs. These ECs were not detected for interactions mediated by short motifs, rather for those with larger IDP–partner interfaces. Most identified coupled residue pairs reside close (<10 Å) to each other on the interface, with a third of them forming multiple direct atomic contacts. EC-carrying interfaces of IDPs are enriched in negatively charged residues, and the EC residues of both IDPs and partners preferentially reside in helices. Our analysis brings hope that IDP–partner interactions difficult to study could soon be successfully dissected through residue co-variation analysis.
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8

Cerveira, Nuno, Susana Bizarro, and Manuel R. Teixeira. "MLL-SEPTIN gene fusions in hematological malignancies." Biological Chemistry 392, no. 8-9 (August 1, 2011): 713–24. http://dx.doi.org/10.1515/bc.2011.072.

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AbstractThe mixed lineage leukemia (MLL) locus is involved in more than 60 different rearrangements with a remarkably diverse group of fusion partners in approximately 10% of human leukemias.MLLrearrangements include chromosomal translocations, gene internal duplications, chromosome 11q deletions or inversions andMLLgene insertions into other chromosomes, or vice versa. MLL fusion partners can be classified into four distinct categories: nuclear proteins, cytoplasmatic proteins, histone acetyltransferases and septins. Five different septin genes (SEPT2,SEPT5,SEPT6,SEPT9, andSEPT11) have been identified asMLLfusion partners, giving rise to chimeric fusion proteins in which the N terminus of MLL is fused, in frame, to almost the entire open reading frame of the septin partner gene. The rearranged alleles result from heterogeneous breaks in distinct introns of bothMLLand its septin fusion partner, originating distinct gene fusion variants.MLL-SEPTIN rearrangements have been repeatedly identified inde novoand therapy related myeloid neoplasia in both children and adults, and some clinicopathogenetic associations are being uncovered. The fundamental roles of septins in cytokinesis, membrane remodeling and compartmentalization can provide some clues on how abnormalities in the septin cytoskeleton and MLL deregulation could be involved in the pathogenesis of hematological malignancies.
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9

Siahaan, Riana Friska, and Erli Mutiara. "TURNING DISASTER INTO BUSINESS OPPORTUNITY THROUGH PROCESSING OF POTATO STICK IN SIOSAR VILLAGE KARO DISTRICT." Journal of Community Research and Service 1, no. 2 (March 29, 2018): 59. http://dx.doi.org/10.24114/jcrs.v1i2.9338.

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AbstractThe purpose of this activity is to empower the potential owned by the partner community. The activities are conducted from July to November 2017. Activity partners are Ati Rohati and home industries Wahyuni. Location of activity in Suka Meriah Village Siosar Kec. Brand Kab. Karo. This village is an area where the relocation of people affected by eruption of Mount Sinabung. Located 110 km from Unimed. Methods of implementation of activities are education, production training, business management training, machine use and mentoring. Output t of this activity is 1) Potato Sticker Machine and 2) Potato Stick. Specifications of potato sticks are: 1) Have nutritional content: Carbohydrates, Proteins, fats, iron, and fiber; 2) Durable and hygienic. Results of activities obtained are partners have knowledge of potato stick processing, actively participating partners, skilled partners using potato sticker printing machine. Partner production is getting better and partner income is also increasing.Keywords: Stick, Potato, Disaster, Karo
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10

Berthelsen, J. "Prep1, a novel functional partner of Pbx proteins." EMBO Journal 17, no. 5 (March 2, 1998): 1423–33. http://dx.doi.org/10.1093/emboj/17.5.1423.

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11

Shore, Gordon C., and Mai Nguyen. "Bcl-2 Proteins and Apoptosis: Choose Your Partner." Cell 135, no. 6 (December 2008): 1004–6. http://dx.doi.org/10.1016/j.cell.2008.11.029.

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12

Ansari, Aseem Z., and Kimberly J. Peterson-Kaufman. "A Partner Evokes Latent Differences between Hox Proteins." Cell 147, no. 6 (December 2011): 1220–21. http://dx.doi.org/10.1016/j.cell.2011.11.046.

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13

Fili, Natalia, Yukti Hari-Gupta, Bjork Aston, Ália dos Santos, Rosemarie E. Gough, Bana Alamad, Lin Wang, Marisa L. Martin-Fernandez, and Christopher P. Toseland. "Competition between two high- and low-affinity protein-binding sites in myosin VI controls its cellular function." Journal of Biological Chemistry 295, no. 2 (November 19, 2019): 337–47. http://dx.doi.org/10.1074/jbc.ra119.010142.

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Myosin VI is involved in many cellular processes ranging from endocytosis to transcription. This multifunctional potential is achieved through alternative isoform splicing and through interactions of myosin VI with a diverse network of binding partners. However, the interplay between these two modes of regulation remains unexplored. To this end, we compared two different binding partners and their interactions with myosin VI by exploring the kinetic properties of recombinant proteins and their distribution in mammalian cells using fluorescence imaging. We found that selectivity for these binding partners is achieved through a high-affinity motif and a low-affinity motif within myosin VI. These two motifs allow competition among partners for myosin VI. Exploring how this competition affects the activity of nuclear myosin VI, we demonstrate the impact of a concentration-driven interaction with the low-affinity binding partner DAB2, finding that this interaction blocks the ability of nuclear myosin VI to bind DNA and its transcriptional activity in vitro. We conclude that loss of DAB2, a tumor suppressor, may enhance myosin VI–mediated transcription. We propose that the frequent loss of specific myosin VI partner proteins during the onset of cancer leads to a higher level of nuclear myosin VI activity.
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14

Bockaert, J., G. Roussignol, C. Bécamel, S. Gavarini, L. Joubert, A. Dumuis, L. Fagni, and P. Marin. "GPCR-interacting proteins (GIPs): nature and functions." Biochemical Society Transactions 32, no. 5 (October 26, 2004): 851–55. http://dx.doi.org/10.1042/bst0320851.

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The simplistic idea that seven transmembrane receptors are single monomeric proteins that interact with heterotrimeric G-proteins after agonist binding is definitively out of date. Indeed, GPCRs (G-protein-coupled receptors) are part of multiprotein networks organized around scaffolding proteins. These GIPs (GPCR-interacting proteins) are either transmembrane or cytosolic proteins. Proteomic approaches can be used to get global pictures of these ‘receptosomes’. This approach allowed us to identify direct but also indirect binding partners of serotonin receptors. GIPs are involved in a wide range of functions including control of the targeting, trafficking and signalling of GPCRs. One of them, Shank, which is a secondary and tertiary partner of metabotropic and ionotropic glutamate receptors, respectively, can induce the formation of a whole functional glutamate ‘receptosome’ and the structure to which it is associated, the dendritic spine.
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15

LoCascio, Costanza, Robert Kupp, Shiv Singh, Emily Szeto, Vincent Loo, Femina Rauf, Alanna Derogatis, Joshua Labaer, Nader Sanai, and Shwetal Mehta. "CSIG-11. ROLE OF OLIG2 PARTNER PROTEINS IN GLIOBLASTOMA." Neuro-Oncology 18, suppl_6 (November 1, 2016): vi43. http://dx.doi.org/10.1093/neuonc/now212.172.

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16

Degenhardt, Yan Yan, and Saul J. Silverstein. "Gps2, a Protein Partner for Human Papillomavirus E6 Proteins." Journal of Virology 75, no. 1 (January 1, 2001): 151–60. http://dx.doi.org/10.1128/jvi.75.1.151-160.2001.

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ABSTRACT We have used the yeast two-hybrid system to screen a cDNA library prepared from normal human epidermal keratinocytes and identified protein partners for human papilloma virus (HPV) E6 proteins. A clone that encoded Gps2 interacted with E6 proteins from HPVs of high and low oncogenic risk. The specificity of these reactions was verified and the regions of E6 that were required for interaction were mapped. Steady-state and pulse-chase analyses of cells cotransfected with DNAs expressing E6 from either HPV6 or HPV18 and Gps2 demonstrated that the E6 proteins induced the degradation of Gps2 in vivo but not in vitro. Gps2 exhibited transcriptional activation activity, and high-risk E6 suppressed this activity.
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17

Gruez, Arnaud, and Guy Branlant. "Structural diversity in the recognition between reduced thioredoxin and its oxidized enzyme partners." BioMolecular Concepts 3, no. 2 (April 1, 2012): 141–50. http://dx.doi.org/10.1515/bmc.2011.056.

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AbstractThioredoxins (Trx) are ubiquitous proteins that are conserved in all living organisms from archaea to humans. These small proteins display various cellular roles, including functioning as reductases in redox processes. All Trxs share a similar, characteristic three-dimensional fold with the Cys-Pro-Gly-Cys motif that contains both the catalytic and the resolving cysteine (Cys) on the surface of the protein. Reaction of reduced Trx with its oxidized protein partners leads to formation of a transient interdisulfide intermediate. However, the short lifetime of this species hinders the characterization of the stabilizing interactions that occur between the partners. In this short review, the three-dimensional structures of four artificial covalent Trx-protein partner complexes are analyzed. The data show that interprotein stabilization is mainly due to hydrophobic contacts and main-chain hydrogen bonds but that no common recognition motif between Trx and its protein partners can be identified. In two cases, formation of the Trx-partner complex is accompanied by a significant conformational change of the protein target, although in no case does the conformation of Trx change significantly. The absence of a common recognition motif supports the idea that it is difficult to predict with confidence putative oxidized protein substrates of Trx using only soft docking and molecular simulation methods. Instead, biochemical methods including proteomic approaches remain the primary tools to identify novel protein substrates of Trx. The generality and relevance of methods used to identify which of the two Cys of the disulfide-oxidized protein partner forms the transient interdisulfide intermediate with Trx are also discussed.
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Fuxreiter, Monika. "Classifying the Binding Modes of Disordered Proteins." International Journal of Molecular Sciences 21, no. 22 (November 16, 2020): 8615. http://dx.doi.org/10.3390/ijms21228615.

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Disordered proteins often act as interaction hubs in cellular pathways, via the specific recognition of a distinguished set of partners. While disordered regions can adopt a well-defined conformation upon binding, the coupled folding to binding model does not explain how interaction versatility is achieved. Here, I present a classification scheme for the binding modes of disordered protein regions, based on their conformational heterogeneity in the bound state. Binding modes are defined as (i) disorder-to-order transitions leading to a well-defined bound state, (ii) disordered binding leading to a disordered bound state and (iii) fuzzy binding when the degree of disorder in the bound state may vary with the partner or cellular conditions. Fuzzy binding includes polymorphic bound structures, conditional folding and dynamic binding. This classification scheme describes the structural continuum of complexes involving disordered regions as well as their context-dependent interaction behaviors.
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Grogan, Christina, Marissa Bennett, and David J. Lampe. "An evaluation of fusion partner proteins for paratransgenesis in Asaia bogorensis." PLOS ONE 17, no. 9 (September 1, 2022): e0273568. http://dx.doi.org/10.1371/journal.pone.0273568.

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Mosquitoes transmit many pathogens responsible for human diseases, such as malaria which is caused by parasites in the genus Plasmodium. Current strategies to control vector-transmitted diseases are increasingly undermined by mosquito and pathogen resistance, so additional methods of control are required. Paratransgenesis is a method whereby symbiotic bacteria are genetically modified to affect the mosquito’s phenotype by engineering them to deliver effector molecules into the midgut to kill parasites. One paratransgenesis candidate is Asaia bogorensis, a Gram-negative bacterium colonizing the midgut, ovaries, and salivary glands of Anopheles sp. mosquitoes. Previously, engineered Asaia strains using native signals to drive the release of the antimicrobial peptide, scorpine, fused to alkaline phosphatase were successful in significantly suppressing the number of oocysts formed after a blood meal containing P. berghei. However, these strains saw high fitness costs associated with the production of the recombinant protein. Here, we report evaluation of five different partner proteins fused to scorpine that were evaluated for effects on the growth and fitness of the transgenic bacteria. Three of the new partner proteins resulted in significant levels of protein released from the Asaia bacterium while also significantly reducing the prevalence of mosquitoes infected with P. berghei. Two partners performed as well as the previously tested Asaia strain that used alkaline phosphatase in the fitness analyses, but neither exceeded it. It may be that there is a maximum level of fitness and parasite inhibition that can be achieved with scorpine being driven constitutively, and that use of a Plasmodium specific effector molecule in place of scorpine would help to mitigate the stress on the symbionts.
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20

Garbett, Damien, Cécile Sauvanet, Raghuvir Viswanatha, and Anthony Bretscher. "The tails of apical scaffolding proteins EBP50 and E3KARP regulate their localization and dynamics." Molecular Biology of the Cell 24, no. 21 (November 2013): 3381–92. http://dx.doi.org/10.1091/mbc.e13-06-0330.

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The closely related apical scaffolding proteins ERM-binding phosphoprotein of 50 kDa (EBP50) and NHE3 kinase A regulatory protein (E3KARP) both consist of two postsynaptic density 95/disks large/zona occludens-1 (PDZ) domains and a tail ending in an ezrin-binding domain. Scaffolding proteins are thought to provide stable linkages between components of multiprotein complexes, yet in several types of epithelial cells, EBP50, but not E3KARP, shows rapid exchange from microvilli compared with its binding partners. The difference in dynamics is determined by the proteins’ tail regions. Exchange rates of EBP50 and E3KARP correlated strongly with their abilities to precipitate ezrin in vivo. The EBP50 tail alone is highly dynamic, but in the context of the full-length protein, the dynamics is lost when the PDZ domains are unable to bind ligand. Proteomic analysis of the effects of EBP50 dynamics on binding-partner preferences identified a novel PDZ1 binding partner, the I-BAR protein insulin receptor substrate p53 (IRSp53). Additionally, the tails promote different microvillar localizations for EBP50 and E3KARP, which localized along the full length and to the base of microvilli, respectively. Thus the tails define the localization and dynamics of these scaffolding proteins, and the high dynamics of EBP50 is regulated by the occupancy of its PDZ domains.
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Noyer, Lucile, Loic Lemonnier, Pascal Mariot, and Dimitra Gkika. "Partners in Crime: Towards New Ways of Targeting Calcium Channels." International Journal of Molecular Sciences 20, no. 24 (December 16, 2019): 6344. http://dx.doi.org/10.3390/ijms20246344.

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The characterization of calcium channel interactome in the last decades opened a new way of perceiving ion channel function and regulation. Partner proteins of ion channels can now be considered as major components of the calcium homeostatic mechanisms, while the reinforcement or disruption of their interaction with the channel units now represents an attractive target in research and therapeutics. In this review we will focus on the targeting of calcium channel partner proteins in order to act on the channel activity, and on its consequences for cell and organism physiology. Given the recent advances in the partner proteins’ identification, characterization, as well as in the resolution of their interaction domain structures, we will develop the latest findings on the interacting proteins of the following channels: voltage-dependent calcium channels, transient receptor potential and ORAI channels, and inositol 1,4,5-trisphosphate receptor.
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22

Albakri, Maram B., Yuwei Jiang, and Patrick Lajoie. "Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in Saccharomyces cerevisiae." F1000Research 7 (August 10, 2018): 1242. http://dx.doi.org/10.12688/f1000research.15829.1.

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Development of fluorescent proteins (FPs) enabled researchers to visualize protein localization and trafficking in living cells and organisms. The extended palette of available FPs allows simultaneous detection of multiples fluorescent fusion proteins. Importantly, FPs are originally derived from different organisms from jelly fish to corals and each FP display its own biophysical properties. Among these properties, the tendency of FPs to oligomerize inherently affects the behavior of its fusion partner. Here we employed the budding yeast Saccharomyces cerevisiae to determine the impact of the latest generation of red FPs on their binding partner. We used a yeast assay based on the aggregation and toxicity of misfolded polyQ expansion proteins linked to Huntington’s disease. Since polyQ aggregation and toxicity are highly dependent on the sequences flanking the polyQ region, polyQ expansions provide an ideal tool to assess the impact of FPs on their fusion partners. We found that unlike yemRFP and yFusionRed, the synthetically engineered ymScarlet displayed severe polyQ toxicity and aggregation similar to what is observed for green FP variants. Our data indicate that ymScarlet might have significant advantages over the previous generation of red FPs for use in fluorescent fusions in yeast.
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23

Legaree, Blaine A., and Anthony J. Clarke. "Interaction of Penicillin-Binding Protein 2 with Soluble Lytic Transglycosylase B1 in Pseudomonas aeruginosa." Journal of Bacteriology 190, no. 20 (August 15, 2008): 6922–26. http://dx.doi.org/10.1128/jb.00934-08.

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ABSTRACT Soluble lytic transglycosylase B1 from Pseudomonas aeruginosa was coupled to Sepharose and used to immobilize interaction partners from membrane protein extracts. Penicillin-binding protein 2 (PBP2) was identified as a binding partner, suggesting that the two proteins function together in the biosynthesis of peptidoglycan. By use of an engineered truncated derivative, the N-terminal module of PBP2 was found to confer the binding properties.
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24

Athukorala, Sarangi N. P., Erwin Huebner, and Michele D. Piercey-Normore. "Identification and comparison of the 3 early stages of resynthesis for the lichen Cladonia rangiferina." Canadian Journal of Microbiology 60, no. 1 (January 2014): 41–52. http://dx.doi.org/10.1139/cjm-2013-0313.

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A lichen is an association between a biotrophic fungal partner and a green algal and (or) cyanobacterial partner, which may be considered a “controlled” parasitic interaction. While controlled parasitism implies benefit to both interacting partners, a parasitism that is not controlled implies that one partner benefits to the detriment of the other partner. The objective of this study was to compare morphological development of the interaction between Cladonia rangiferina with its compatible algal partner (Asterochloris glomerata/irregularis) and incompatible algae (Coccomyxa peltigerae and Chloroidium ellipsoideum) at 3 early resynthesis stages. The fungus was co-inoculated with each alga separately and the stages of development were compared using quantitative measures. The first 3 stages of development of the lichen thallus were identified in the compatible interaction as the “pre-contact” stage (1 day post co-inoculation (PCI)), “contact” stage (8 days PCI), and “growth together” stage (21 days PCI). Compatible interactions showed significantly shorter internode length, significantly more new lateral hyphal branches, significantly greater appressorial frequency, and no reduction in cell diameter of the algal cells, compared with incompatible interactions. At 21 days PCI, a parasitic interaction was observed between Cladonia rangiferina and Chloroidium ellipsoideum. These findings support the importance of recognition between compatible partners for successful lichenization. This study also revealed a strategy that may explain the success of this species in northern habitats. Identification of the resynthesis stages of Cladonia rangiferina is required before expression of the proteins involved in recognition and defense can be understood.
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Kobe, Bostjan, Thomas Ve, and Simon J. Williams. "Fusion-protein-assisted protein crystallization." Acta Crystallographica Section F Structural Biology Communications 71, no. 7 (June 27, 2015): 861–69. http://dx.doi.org/10.1107/s2053230x15011061.

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Fusion proteins can be used directly in protein crystallization to assist crystallization in at least two different ways. In one approach, the `heterologous fusion-protein approach', the fusion partner can provide additional surface area to promote crystal contact formation. In another approach, the `fusion of interacting proteins approach', protein assemblies can be stabilized by covalently linking the interacting partners. The linker connecting the proteins plays different roles in the two applications: in the first approach a rigid linker is required to reduce conformational heterogeneity; in the second, conversely, a flexible linker is required that allows the native interaction between the fused proteins. The two approaches can also be combined. The recent applications of fusion-protein technology in protein crystallization from the work of our own and other laboratories are briefly reviewed.
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Castro, Inês, Michal Eisenberg-Bord, Elisa Persiani, Justin Rochford, Maya Schuldiner, and Maria Bohnert. "Promethin Is a Conserved Seipin Partner Protein." Cells 8, no. 3 (March 21, 2019): 268. http://dx.doi.org/10.3390/cells8030268.

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Seipin (BSCL2/SPG17) is a key factor in lipid droplet (LD) biology, and its dysfunction results in severe pathologies, including the fat storage disease Berardinelli-Seip congenital lipodystrophy type 2, as well as several neurological seipinopathies. Despite its importance for human health, the molecular role of seipin is still enigmatic. Seipin is evolutionarily conserved from yeast to humans. In yeast, seipin was recently found to cooperate with the lipid droplet organization (LDO) proteins, Ldo16 and Ldo45, two structurally-related proteins involved in LD function and identity that display remote homology to the human protein promethin/TMEM159. In this study, we show that promethin is indeed an LD-associated protein that forms a complex with seipin, and its localization to the LD surface can be modulated by seipin expression levels. We thus identify promethin as a novel seipin partner protein.
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van Deventer, Sjoerd J., Vera-Marie E. Dunlock, and Annemiek B. van Spriel. "Molecular interactions shaping the tetraspanin web." Biochemical Society Transactions 45, no. 3 (June 15, 2017): 741–50. http://dx.doi.org/10.1042/bst20160284.

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To facilitate the myriad of different (signaling) processes that take place at the plasma membrane, cells depend on a high degree of membrane protein organization. Important mediators of this organization are tetraspanin proteins. Tetraspanins interact laterally among themselves and with partner proteins to control the spatial organization of membrane proteins in large networks called the tetraspanin web. The molecular interactions underlying the formation of the tetraspanin web were hitherto mainly described based on their resistance to different detergents, a classification which does not necessarily correlate with functionality in the living cell. To look at these interactions from a more physiological point of view, this review discusses tetraspanin interactions based on their function in the tetraspanin web: (1) intramolecular interactions supporting tetraspanin structure, (2) tetraspanin–tetraspanin interactions supporting web formation, (3) tetraspanin–partner interactions adding functional partners to the web and (4) cytosolic tetraspanin interactions regulating intracellular signaling. The recent publication of the first full-length tetraspanin crystal structure sheds new light on both the intra- and intermolecular tetraspanin interactions that shape the tetraspanin web. Furthermore, recent molecular dynamic modeling studies indicate that the binding strength between tetraspanins and between tetraspanins and their partners is the complex sum of both promiscuous and specific interactions. A deeper insight into this complex mixture of interactions is essential to our fundamental understanding of the tetraspanin web and its dynamics which constitute a basic building block of the cell surface.
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28

Chen, Xin, Melissa J. Rubock, and Malcolm Whitman. "A transcriptional partner for MAD proteins in TGF-β signalling." Nature 383, no. 6602 (October 1996): 691–96. http://dx.doi.org/10.1038/383691a0.

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29

Caillet-Boudin, M. L. "Complementary peptide sequences in partner proteins of the adenovirus capsid." Journal of Molecular Biology 208, no. 1 (July 1989): 195–98. http://dx.doi.org/10.1016/0022-2836(89)90095-8.

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30

Petty, Howard R., Randall G. Worth, and Robert F. Todd. "Interactions of Integrins with Their Partner Proteins in Leukocyte Membranes." Immunologic Research 25, no. 1 (2002): 75–96. http://dx.doi.org/10.1385/ir:25:1:75.

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31

Kim, Tae Im, Pyo Yun Cho, Shunyu Li, Sung-Tae Hong, Min-Ho Choi, and Sung-Jong Hong. "Partner proteins that interact with Clonorchis sinensis WD40-repeat protein." Parasitology Research 101, no. 5 (July 6, 2007): 1233–38. http://dx.doi.org/10.1007/s00436-007-0625-5.

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Zaman, Shadia, Karen Sukhodolets, Patricia Wang, Jun Qin, David Levens, Sunita K. Agarwal, and Stephen J. Marx. "FBP1 Is an Interacting Partner of Menin." International Journal of Endocrinology 2014 (2014): 1–6. http://dx.doi.org/10.1155/2014/535401.

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Multiple endocrine neoplasia type 1 (MEN1) is a syndrome characterized by tumors in multiple endocrine tissues such as the parathyroid glands, the pituitary gland, and the enteropancreatic neuroendocrine tissues. MEN1 is usually caused by mutations in theMEN1gene that codes for the protein menin. Menin interacts with proteins that regulate transcription, DNA repair and processing, and maintenance of cytoskeletal structure. We describe the identification of FBP1 as an interacting partner of menin in a large-scale pull-down assay that also immunoprecipitated RBBP5, ASH2, and LEDGF, which are members of complex proteins associated with SET1 (COMPASS), a protein complex that methylates histone H3. This interaction was confirmed by coimmunoprecipitation and Flag-pull-down assays. Furthermore, menin localized to the FUSE site on theMYCpromoter, a site that is transactivated by FBP1. This investigation therefore places menin in a pathway that regulatesMYCgene expression and has important implications for the biological function of menin.
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33

Zibouche, Malik, Françoise Illien, and Jesus Ayala-Sanmartin. "Annexin A2 expression and partners during epithelial cell differentiation." Biochemistry and Cell Biology 97, no. 5 (October 2019): 612–20. http://dx.doi.org/10.1139/bcb-2018-0393.

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The members of the annexin family of calcium- and phospholipid-binding proteins participate in different cellular processes. Annexin A2 binds to S100A10, forming a functional heterotetrameric protein that has been involved in many cellular functions, such as exocytosis, endocytosis, cell junction formation, and actin cytoskeleton dynamics. Herein, we studied annexin A2 cellular movements and looked for its partners during epithelial cell differentiation. By using immunofluorescence, mass spectrometry (MS), and western blot analyses after S100A10 affinity column separation, we identified several annexin A2–S100A10 partner candidates. The association of putative annexin A2–S100A10 partner candidates obtained by MS after column affinity was validated by immunofluorescence and sucrose density gradient separation. The results show that three proteins are clearly associated with annexin A2: E-cadherin, actin, and caveolin 1. Overall, the data show that annexin A2 can associate with molecular complexes containing actin, caveolin 1, and flotillin 2 before epithelial differentiation and with complexes containing E-cadherin, actin, and caveolin 1, but not flotillin 2 after cell differentiation. The results indicate that actin, caveolin 1, and E-cadherin are the principal protein partners of annexin A2 in epithelial cells and that the serine phosphorylation of the N-terminal domain does not play an essential role during epithelial cell differentiation.
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Kophengnavong, Thiphaphone, Jennifer E. Michnowicz, and T. Keith Blackwell. "Establishment of Distinct MyoD, E2A, and Twist DNA Binding Specificities by Different Basic Region-DNA Conformations." Molecular and Cellular Biology 20, no. 1 (January 1, 2000): 261–72. http://dx.doi.org/10.1128/mcb.20.1.261-272.2000.

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ABSTRACT Basic helix-loop-helix (bHLH) proteins perform a wide variety of biological functions. Most bHLH proteins recognize the consensus DNA sequence CAN NTG (the E-box consensus sequence is underlined) but acquire further functional specificity by preferring distinct internal and flanking bases. In addition, induction of myogenesis by MyoD-related bHLH proteins depends on myogenic basic region (BR) and BR-HLH junction residues that are not essential for binding to a muscle-specific site, implying that their BRs may be involved in other critical interactions. We have investigated whether the myogenic residues influence DNA sequence recognition and how MyoD, Twist, and their E2A partner proteins prefer distinct CAN NTG sites. In MyoD, the myogenic BR residues establish specificity for particular CAN NTG sites indirectly, by influencing the conformation through which the BR helix binds DNA. An analysis of DNA binding by BR and junction mutants suggests that an appropriate BR-DNA conformation is necessary but not sufficient for myogenesis, supporting the model that additional interactions with this region are important. The sequence specificities of E2A and Twist proteins require the corresponding BR residues. In addition, mechanisms that position the BR allow E2A to prefer distinct half-sites as a heterodimer with MyoD or Twist, indicating that the E2A BR can be directed toward different targets by dimerization with different partners. Our findings indicate that E2A and its partner bHLH proteins bind to CAN NTG sites by adopting particular preferred BR-DNA conformations, from which they derive differences in sequence recognition that can be important for functional specificity.
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35

Kamachi, Yusuke, Kathryn S. E. Cheah, and Hisato Kondoh. "Mechanism of Regulatory Target Selection by the SOX High-Mobility-Group Domain Proteins as Revealed by Comparison of SOX1/2/3 and SOX9." Molecular and Cellular Biology 19, no. 1 (January 1, 1999): 107–20. http://dx.doi.org/10.1128/mcb.19.1.107.

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ABSTRACT SOX proteins bind similar DNA motifs through their high-mobility-group (HMG) domains, but their action is highly specific with respect to target genes and cell type. We investigated the mechanism of target selection by comparing SOX1/2/3, which activate δ-crystallin minimal enhancer DC5, with SOX9, which activates Col2a1 minimal enhancer COL2C2. These enhancers depend on both the SOX binding site and the binding site of a putative partner factor. The DC5 site was equally bound and bent by the HMG domains of SOX1/2 and SOX9. The activation domains of these SOX proteins mapped at the distal portions of the C-terminal domains were not cell specific and were independent of the partner factor. Chimeric proteins produced between SOX1 and SOX9 showed that to activate the DC5 enhancer, the C-terminal domain must be that of SOX1, although the HMG domains were replaceable. The SOX2-VP16 fusion protein, in which the activation domain of SOX2 was replaced by that of VP16, activated the DC5 enhancer still in a partner factor-dependent manner. The results argue that the proximal portion of the C-terminal domain of SOX1/2 specifically interacts with the partner factor, and this interaction determines the specificity of the SOX1/2 action. Essentially the same results were obtained in the converse experiments in which COL2C2 activation by SOX9 was analyzed, except that specificity of SOX9-partner factor interaction also involved the SOX9 HMG domain. The highly selective SOX-partner factor interactions presumably stabilize the DNA binding of the SOX proteins and provide the mechanism for regulatory target selection.
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Albakri, Maram B., Yuwei Jiang, Julie Genereaux, and Patrick Lajoie. "Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in Saccharomyces cerevisiae." F1000Research 7 (November 26, 2018): 1242. http://dx.doi.org/10.12688/f1000research.15829.2.

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Development of fluorescent proteins (FPs) enabled researchers to visualize protein localization and trafficking in living cells and organisms. The extended palette of available FPs allows simultaneous detection of multiple fluorescent fusion proteins. Importantly, FPs are originally derived from different organisms from jelly fish to corals and each FP displays its own biophysical properties. Among these properties, the tendency of FPs to oligomerize inherently affects the behavior of its fusion partner. Here we employed the budding yeast Saccharomyces cerevisiae to determine the impact of the latest generation of red FPs on their binding partner. We used a yeast assay based on the aggregation and toxicity of misfolded polyQ expansion proteins linked to Huntington’s disease. Since polyQ aggregation and toxicity are highly dependent on the sequences flanking the polyQ region, polyQ expansions provide an ideal tool to assess the impact of FPs on their fusion partners. We found that unlike what is observed for green FP variants, yemRFP and yFusionRed-tagged polyQ expansions show reduced toxicity. However, polyQ expansions tagged with the bright synthetically engineered ymScarlet displayed severe polyQ toxicity. Our data indicate that ymScarlet might have significant advantages over the previous generation of red FPs for use in fluorescent fusions in yeast.
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Hsu, Che-Yu, Kuan-Ting Lee, Tzu-Yu Sun, Chun-I. Sze, Shenq-Shyang Huang, Li-Jin Hsu, and Nan-Shan Chang. "WWOX and Its Binding Proteins in Neurodegeneration." Cells 10, no. 7 (July 14, 2021): 1781. http://dx.doi.org/10.3390/cells10071781.

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WW domain-containing oxidoreductase (WWOX) is known as one of the risk factors for Alzheimer’s disease (AD), a neurodegenerative disease. WWOX binds Tau via its C-terminal SDR domain and interacts with Tau phosphorylating enzymes ERK, JNK, and GSK-3β, and thereby limits AD progression. Loss of WWOX in newborns leads to severe neural diseases and early death. Gradual loss of WWOX protein in the hippocampus and cortex starting from middle age may slowly induce aggregation of a protein cascade that ultimately causes accumulation of extracellular amyloid beta plaques and intracellular tau tangles, along with reduction in inhibitory GABAergic interneurons, in AD patients over 70 years old. Age-related increases in pS14-WWOX accumulation in the brain promotes neuronal degeneration. Suppression of Ser14 phosphorylation by a small peptide Zfra leads to enhanced protein degradation, reduction in NF-κB-mediated inflammation, and restoration of memory loss in triple transgenic mice for AD. Intriguingly, tumor suppressors p53 and WWOX may counteract each other in vivo, which leads to upregulation of AD-related protein aggregation in the brain and lung. WWOX has numerous binding proteins. We reported that the stronger the binding between WWOX and its partners, the better the suppression of cancer growth and reduction in inflammation. In this regard, the stronger complex formation between WWOX and partners may provide a better blockade of AD progression. In this review, we describe whether and how WWOX and partner proteins control inflammatory response and protein aggregation and thereby limit AD progression.
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Lin, Min, and Michael L. Cleary. "MLL Translocation Partners AF4, AF5q31, and ENL Associate in a Higher Order Protein Complex with CDK9 and Cyclin T1." Blood 106, no. 11 (November 16, 2005): 99. http://dx.doi.org/10.1182/blood.v106.11.99.99.

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Abstract The Mixed Lineage Leukemia (MLL) gene is frequently involved in chromosomal translocations that cause acute leukemia. More than 40 different genes have been identified as MLL translocation partners, with the expression of corresponding MLL fusion proteins. The MLL protein has histone methyltransferase activity and is required for embryonic development and hematopoiesis. Several proteins have been demonstrated to associate with MLL in a macromolecular complex, which is believed to have chromatin remodeling function. However, the C-terminal SET domain of MLL, which carries the histone methyltransferase activity, is lost in all MLL fusion proteins, thus making the biochemical functions of the fusion proteins unclear. Moreover, the promiscuity of MLL translocation partners, most of them with no known functions, further complicates an understanding of MLL leukemogenic mechanisms. In this study, we purified a protein complex containing AF4, the most common MLL translocation partner, using a combination of conventional column chromatography and immunoaffinity techniques. The AF4 protein complex contains AF5q31 and ENL, two other MLL translocation partners, as well as CDK9 and Cyclin T1, a heterodimer that regulates transcriptional elongation. Gel filtration confirmed that these five proteins co-fractionate with an estimated overall size of 0.8 MDa. All protein-protein interactions were further confirmed by immunoprecipitation-western blotting from K562 cell nuclear extract. To investigate whether these protein-protein interactions are retained in corresponding MLL fusion proteins, immunoprecipitation-western blotting assays were carried out in human leukemia cell lines harboring MLL chromosomal translocations. We found that MLL-AF4, MLL-AF5q31, MLL-ENL and MLL-AF9 each associate with wild type AF4 complex components, including CDK9 and Cyclin T1. In contrast, MLL-AF6 does not associate with any of the AF4 complex components. We propose that the four nuclear MLL translocation partner proteins (AF4, AF5q31, ENL/AF9), whose translocations are found in over 75% of MLL leukemias, associate in a higher order protein complex with CDK9 and Cyclin T1 and thus function in part to regulate transcriptional elongation. The association of CDK9 and Cyclin T1 with the four MLL fusion proteins suggests a common leukemogenic mechanism that may involve transcriptional elongation, which we are currently investigating. Conversely, MLL-cytosolic fusions, e.g. MLL-AF6, appear to function independently of association with the AF4 protein complex, possibly through a homo-dimerization pathway.
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Eguchi, Mariko, Minenori Eguchi-Ishimae, and Mel Greaves. "The small oligomerization domain of gephyrin converts MLL to an oncogene." Blood 103, no. 10 (May 15, 2004): 3876–82. http://dx.doi.org/10.1182/blood-2003-11-3817.

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Abstract The MLL (mixed lineage leukemia) gene forms chimeric fusions with a diverse set of partner genes as a consequence of chromosome translocations in leukemia. In several fusion partners, a transcriptional activation domain appears to be essential for conferring leukemogenic capacity on MLL protein. Other fusion partners, however, lack such domains. Here we show that gephyrin (GPHN), a neuronal receptor assembly protein and rare fusion partner of MLL in leukemia, has the capacity as an MLL-GPHN chimera to transform hematopoietic progenitors, despite lack of transcriptional activity. A small 15–amino acid tubulin-binding domain of GPHN is necessary and sufficient for this activity in vitro and in vivo. This domain also confers oligomerization capacity on MLL protein, suggesting that such activity may contribute critically to leukemogenesis. The transduction of MLL-GPHN into hematopoietic progenitor cells caused myeloid and lymphoid lineage leukemias in mice, suggesting that MLL-GPHN can target multipotent progenitor cells. Our results, and other recent data, provide a mechanism for oncogenic conversion of MLL by fusion partners encoding cytoplasmic proteins.
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Slany, Robert K., Dorothee Mueller, Christian Bach, Deniz Zeisig, Maria-Paz Garcia-Cuellar, Sara Monroe, Arun Sreekumar, et al. "Purification of an MLL Partner Associated Complex (MPAC) Suggests a Common Role for MLL Fusion Partners in Transcriptional Elongation." Blood 108, no. 11 (November 16, 2006): 770. http://dx.doi.org/10.1182/blood.v108.11.770.770.

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Abstract Chromosomal translocations at 11q23 are characteristic for a subset of particularly aggressive acute lymphoid and myeloid leukemias. This event fuses the mixed lineage leukemia (MLL) gene to a puzzling variety of seemingly unrelated fusion partners to create novel transcription factors with potent oncogenic activity. Despite the molecular heterogeneity, MLL−associated leukemias show similar clinical presentations and an almost identical gene expression pattern regardless of the translocation partner. We and others previously identified interactions between individual MLL translocation partners suggesting that these might share a common mechanism for transformation. To characterize these interactions in more detail we generated a HEK293−derived producer line expressing a FLAG−tagged derivative of the frequent fusion partner ENL. Double affinity purification of nuclear extracts on FLAG and ENL antibody resins reproducibly yielded a macromolecular complex of 10 proteins we term MPAC, for MLL Partner Associated Complex, which in addition to ENL includes the MLL fusion partners AF4, AF9 and AF5q31, and two components involved in transcriptional elongation: pTEFb and DOT1L. The pTEFb dimer consists of cyclin T1/2 and CDK9 and is responsible for serine−2 phosphorylation of the C−terminal repeat domain of elongating RNA Polymerase II. DOT1L is the only known histone methyltransferase that catalyzes dimethylation of H3K79, a modification introduced during elongation of actively transcribed transcription units. Surprisingly, PC3 and RING1b, members of the polycomb repressive complex I were also identified in the MPAC complex. Further examination demonstrated a direct interaction of ENL with DOT1L through C−terminal interaction domains by yeast 2−hybrid, pulldown and colocalization experiments. Knock−down of ENL diminished global H3K79 dimethylation and also impaired various promoters in transient reporter assays suggesting the MPAC complex is involved in transcriptional regulation mediated by DOT1L, even in the absence of MLL fusion proteins. In summary, our results indicate that the most common MLL fusion partners are associated in an hitherto undescribed complex involved in transcriptional elongation.
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Aznabayeva, Rabiga Baurzhanovna, Aigerim Makashkyzy Turgimbayeva, Ulan Zein, and Sailau Kasenovich Abeldenov. "Peptide sequences for protein–protein sliding clamp interactions." Bulletin of the Karaganda University. “Biology, medicine, geography Series” 106, no. 2 (June 30, 2022): 18–25. http://dx.doi.org/10.31489/2022bmg2/18-25.

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Today antibiotic resistance to pathogenic microorganisms is becoming an increasingly dangerous problem all over the world. At the same time, the need for the development of new antibacterial targets is growing. Since the discovery of sliding clamps in bacteria, a large number of studies have been carried out during which its unique properties, such as the ability to bind to DNA and increase the activity and efficiency of repair and replication proteins, have been discovered, which underlines its important role in maintaining bacteria resistance to DNA damage. At the moment, the number of partner proteins with which the sliding clamp isable to create functional complexes continues to grow, and therefore the β-clamp is the object of close attention of scientists as a potential solution for finding new antibiotics. This review article presents some studies highlighting its structure, structure and mechanism of functioning, as well as its ability to form complexes with many partner proteins using a unique PIP β-clamp binding motif, which is conservative and similar for all partner proteins.
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42

EVANS, Gareth J. O., and Alan MORGAN. "Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I." Biochemical Journal 364, no. 2 (June 1, 2002): 343–47. http://dx.doi.org/10.1042/bj20020123.

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The secretory vesicle cysteine string proteins (CSPs) are members of the DnaJ family of chaperones, and function at late stages of Ca2+-regulated exocytosis by an unknown mechanism. To determine novel binding partners of CSPs, we employed a pull-down strategy from purified rat brain membrane or cytosolic proteins using recombinant hexahistidine-tagged (His6-)CSP. Western blotting of the CSP-binding proteins identified synaptotagmin I to be a putative binding partner. Furthermore, pull-down assays using cAMP-dependent protein kinase (PKA)-phosphorylated CSP recovered significantly less synaptotagmin. Complexes containing CSP and synaptotagmin were immunoprecipitated from rat brain membranes, further suggesting that these proteins interact in vivo. Binding assays in vitro using recombinant proteins confirmed a direct interaction between the two proteins and demonstrated that the PKA-phosphorylated form of CSP binds synaptotagmin with approximately an order of magnitude lower affinity than the non-phosphorylated form. Genetic studies have implicated each of these proteins in the Ca2+-dependency of exocytosis and, since CSP does not bind Ca2+, this novel interaction might explain the Ca2+-dependent actions of CSP.
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43

Sklan, Ella H., Kirk Staschke, Tina M. Oakes, Menashe Elazar, Mark Winters, Benjamin Aroeti, Tsafi Danieli, and Jeffrey S. Glenn. "A Rab-GAP TBC Domain Protein Binds Hepatitis C Virus NS5A and Mediates Viral Replication." Journal of Virology 81, no. 20 (August 8, 2007): 11096–105. http://dx.doi.org/10.1128/jvi.01249-07.

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ABSTRACT Hepatitis C virus (HCV) is an important cause of liver disease worldwide. Current therapies are inadequate for most patients. Using a two-hybrid screen, we isolated a novel cellular binding partner interacting with the N terminus of HCV nonstructural protein NS5A. This partner contains a TBC Rab-GAP (GTPase-activating protein) homology domain found in all known Rab-activating proteins. As the first described interaction between such a Rab-GAP and a viral protein, this finding suggests a new mechanism whereby viruses may subvert host cell machinery for mediating the endocytosis, trafficking, and sorting of their own proteins. Moreover, depleting the expression of this partner severely impairs HCV RNA replication with no obvious effect on cell viability. These results suggest that pharmacologic disruption of this NS5A-interacting partner can be contemplated as a potential new antiviral strategy against a pathogen affecting nearly 3% of the world's population.
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Toto, Angelo, Francesca Malagrinò, Lorenzo Visconti, Francesca Troilo, Livia Pagano, Maurizio Brunori, Per Jemth, and Stefano Gianni. "Templated folding of intrinsically disordered proteins." Journal of Biological Chemistry 295, no. 19 (April 6, 2020): 6586–93. http://dx.doi.org/10.1074/jbc.rev120.012413.

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Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered, while being functional, has revolutionized our understanding of proteins and raised new and interesting questions. Many intrinsically disordered proteins (IDPs) have been determined to undergo a disorder-to-order transition when recognizing their physiological partners, suggesting that their mechanisms of folding are intrinsically different from those observed in globular proteins. However, IDPs also follow some of the classic paradigms established for globular proteins, pointing to important similarities in their behavior. In this review, we compare and contrast the folding mechanisms of globular proteins with the emerging features of binding-induced folding of intrinsically disordered proteins. Specifically, whereas disorder-to-order transitions of intrinsically disordered proteins appear to follow rules of globular protein folding, such as the cooperative nature of the reaction, their folding pathways are remarkably more malleable, due to the heterogeneous nature of their folding nuclei, as probed by analysis of linear free-energy relationship plots. These insights have led to a new model for the disorder-to-order transition in IDPs termed “templated folding,” whereby the binding partner dictates distinct structural transitions en route to product, while ensuring a cooperative folding.
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El Ghazi, Issam, Bruce L. Martin, and Ian M. Armitage. "New Proteins Found Interacting with Brain Metallothionein-3 Are Linked to Secretion." International Journal of Alzheimer's Disease 2011 (2011): 1–9. http://dx.doi.org/10.4061/2011/208634.

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Metallothionein 3 (MT-3), also known as growth inhibitory factor (GIF), exhibits a neuroinhibitory activity. Our lab and others have previously shown that this biological activity involves interacting protein partners in the brain. However, nothing specific is yet known about which of these interactions is responsible for the GIF activity. In this paper, we are reporting upon new proteins found interacting with MT-3 as determined through immunoaffinity chromatography and mass spectrometry. These new partner proteins—Exo84p, 14-3-3 Zeta,αandβEnolase, Aldolase C, Malate dehydrogenase, ATP synthase, and Pyruvate kinase—along with those previously identified have now been classified into three functional groups: transport and signaling, chaperoning and scaffolding, and glycolytic metabolism. When viewed together, these interactions support a proposed model for the regulation of the GIF activity of MT-3.
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CONESA, Magali, Annik PRAT, John S. MORT, Jacques MARVALDI, Jean-Claude LISSITZKY, and Nabil G. SEIDAH. "Down-regulation of alphav/beta3 integrin via misrouting to lysosomes by overexpression of a beta3Lamp1 fusion protein." Biochemical Journal 370, no. 2 (March 1, 2003): 703–11. http://dx.doi.org/10.1042/bj20021301.

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We present a general strategy for the dominant negative reduction in the levels of type-1 membrane-bound heterodimeric proteins within the secretory pathway through fusion of the soluble ectodomain of one of the partners to the transmembrane-cytosolic tail of the lysosomal protein Lamp1. Thus, in human embryonic kidney (HEK)-293 cells, overexpression of an integrin β3Lamp1 chimera resulted in a drastic reduction of its endogenous partner, the integrin αv subunit. The mechanism involves the formation in the endoplasmic reticulum of a αv/β3Lamp1 complex that is subsequently sorted towards a lysosomal/endosomal degradation pathway. The specificity of this approach is afforded by the invariance in the levels of the endogenous integrins α5 and β1 as compared with control cells. Conversely overexpression of integrin β3 in HEK-293 cells led to an increased level of αvβ3 at the cell surface. Functionally β3Lamp1 and β3 overexpressors exhibit decreased and increased adhesion to vitronectin, respectively, as well as diminished cellular aggregation. The application of this technology should enable the analysis of the functional importance of homodimers or heterodimers in the cell types of choice and the identification of novel partner proteins by proteomic approaches.
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Waskiewicz, Andrew Jan, Holly A. Rikhof, Rafael E. Hernandez, and Cecilia B. Moens. "Zebrafish Meis functions to stabilize Pbx proteins and regulate hindbrain patterning." Development 128, no. 21 (November 1, 2001): 4139–51. http://dx.doi.org/10.1242/dev.128.21.4139.

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Homeodomain-containing Hox proteins regulate segmental identity in Drosophila in concert with two partners known as Extradenticle (Exd) and Homothorax (Hth). These partners are themselves DNA-binding, homeodomain proteins, and probably function by revealing the intrinsic specificity of Hox proteins. Vertebrate orthologs of Exd and Hth, known as Pbx and Meis (named for a myeloid ecotropic leukemia virus integration site), respectively, are encoded by multigene families and are present in multimeric complexes together with vertebrate Hox proteins. Previous results have demonstrated that the zygotically encoded Pbx4/Lazarus (Lzr) protein is required for segmentation of the zebrafish hindbrain and proper expression and function of Hox genes. We demonstrate that Meis functions in the same pathway as Pbx in zebrafish hindbrain development, as expression of a dominant-negative mutant Meis results in phenotypes that are remarkably similar to that of lzr mutants. Surprisingly, expression of Meis protein partially rescues the lzr– phenotype. Lzr protein levels are increased in embryos overexpressing Meis and are reduced for lzr mutants that cannot bind to Meis. This implies a mechanism whereby Meis rescues lzr mutants by stabilizing maternally encoded Lzr. Our results define two functions of Meis during zebrafish hindbrain segmentation: that of a DNA-binding partner of Pbx proteins, and that of a post-transcriptional regulator of Pbx protein levels.
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Hira, D., M. Nojiri, K. Yamaguchi, and S. Suzuki. "X-ray structures of redox partner proteins forHyphomicrobiumCu-containing nitrite reductase." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (August 23, 2008): C291. http://dx.doi.org/10.1107/s0108767308090685.

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49

Ogbureke, Kalu U. E., and Larry W. Fisher. "Renal expression of SIBLING proteins and their partner matrix metalloproteinases (MMPs)." Kidney International 68, no. 1 (July 2005): 155–66. http://dx.doi.org/10.1111/j.1523-1755.2005.00389.x.

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50

Chen, Xin, Melissa J. Rubock, and Malcolm Whitman. "Erratum: A transcriptional partner for MAD proteins in TGF-β signalling." Nature 384, no. 6610 (December 1996): 648. http://dx.doi.org/10.1038/384648b0.

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