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Journal articles on the topic 'N-terminal domains'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Zouharova, Monika, Petr Herman, Kateřina Hofbauerová, Jiri Vondrasek, and Kristyna Bousova. "TRPM6 N-Terminal CaM- and S100A1-Binding Domains." International Journal of Molecular Sciences 20, no. 18 (2019): 4430. http://dx.doi.org/10.3390/ijms20184430.

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Transient receptor potential (TRPs) channels are crucial downstream targets of calcium signalling cascades. They can be modulated either by calcium itself and/or by calcium-binding proteins (CBPs). Intracellular messengers usually interact with binding domains present at the most variable TRP regions—N- and C-cytoplasmic termini. Calmodulin (CaM) is a calcium-dependent cytosolic protein serving as a modulator of most transmembrane receptors. Although CaM-binding domains are widespread within intracellular parts of TRPs, no such binding domain has been characterised at the TRP melastatin member

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2

Nieuwesteeg, M. A., L. A. Walsh, M. A. Fox, and S. Damjanovski. "Domain specific overexpression of TIMP-2 and TIMP-3 reveals MMP-independent functions of TIMPs during Xenopus laevis development." Biochemistry and Cell Biology 90, no. 4 (2012): 585–95. http://dx.doi.org/10.1139/o2012-014.

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Extracellular matrix remodelling mediates many processes including cell migration and differentiation and is regulated through the enzymatic action of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). TIMPs are secreted proteins, consisting of structurally and functionally distinct N- and C-terminal domains. TIMP N-terminal domains inhibit MMP activity, whereas their C-terminal domains may have cell signalling activity. The in vivo role of TIMP N- and C-terminal domains in regulating developmental events has not previously been demonstrated. Here we investig

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3

van den Ent, Fusinita M. I., Arnold Vos, and Ronald H. A. Plasterk. "Dissecting the Role of the N-Terminal Domain of Human Immunodeficiency Virus Integrase bytrans-Complementation Analysis." Journal of Virology 73, no. 4 (1999): 3176–83. http://dx.doi.org/10.1128/jvi.73.4.3176-3183.1999.

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ABSTRACT The human immunodeficiency virus (HIV) integrase protein (IN) catalyzes two reactions required to integrate HIV DNA into the human genome: 3′ processing of the viral DNA ends and integration. IN has three domains, the N-terminal zinc-binding domain, the catalytic core, and the C-terminal SH3 domain. Previously, it was shown that IN proteins mutated in different domains could complement each other. We now report that this does not require any overlap between the two complementing proteins; an N-terminal domain, provided intrans, can restore IN activity of a mutant lacking this domain.

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4

Wickström, Claes, and Ingemar Carlstedt. "N-terminal Cleavage of the Salivary MUC5B Mucin." Journal of Biological Chemistry 276, no. 50 (2001): 47116–21. http://dx.doi.org/10.1074/jbc.m106593200.

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Sequence similarities between the oligomeric mucins (MUC2, MUC5AC, MUC5B) and the von Willebrand factor suggest that they may be assembled in a similar way. After oligomerization, a fragment corresponding to the D1 and D2 domains is released from the von Willebrand factor. This cleavage does not appear to occur in pig submaxillary mucin, the only mammalian mucin in which this cleavage has been examined thus far, but whether other oligomeric mucins undergo N terminus proteolysis is not known. Antibodies recognizing the D1, D2, D3, and the first Cys domains in MUC5B were established and used to

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5

Tikhonova, I. G., I. I. Baskin, V. A. Palyulin, and N. S. Zefirov. "Molecular Modeling of N-Terminal Domains of NMDA-Receptor. Study of Ligand Binding to N-Terminal Domains." Doklady Biochemistry and Biophysics 397, no. 1-6 (2004): 242–50. http://dx.doi.org/10.1023/b:dobi.0000039474.86331.7a.

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6

Tanaka, M., W. M. Clouston, and W. Herr. "The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription." Molecular and Cellular Biology 14, no. 9 (1994): 6046–55. http://dx.doi.org/10.1128/mcb.14.9.6046.

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The B-cell POU homeodomain protein Oct-2 contains two transcriptional activation domains, one N terminal and the other C terminal of the central DNA-binding POU domain. The synergistic action of these two activation domains makes Oct-2 a more potent activator of mRNA promoters than the related broadly expressed octamer motif-binding protein Oct-1, which contains an N-terminal but not a C-terminal Oct-2-like activation domain. Both Oct-2 mRNA promoter activation domains were delineated by truncation analysis: the N-terminal Q domain is a 66-amino-acid region rich in glutamines, and the C-termin

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7

Tanaka, M., W. M. Clouston, and W. Herr. "The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription." Molecular and Cellular Biology 14, no. 9 (1994): 6046–55. http://dx.doi.org/10.1128/mcb.14.9.6046-6055.1994.

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The B-cell POU homeodomain protein Oct-2 contains two transcriptional activation domains, one N terminal and the other C terminal of the central DNA-binding POU domain. The synergistic action of these two activation domains makes Oct-2 a more potent activator of mRNA promoters than the related broadly expressed octamer motif-binding protein Oct-1, which contains an N-terminal but not a C-terminal Oct-2-like activation domain. Both Oct-2 mRNA promoter activation domains were delineated by truncation analysis: the N-terminal Q domain is a 66-amino-acid region rich in glutamines, and the C-termin

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8

Surtees, Jennifer A., and Barbara E. Funnell. "P1 ParB Domain Structure Includes Two Independent Multimerization Domains." Journal of Bacteriology 181, no. 19 (1999): 5898–908. http://dx.doi.org/10.1128/jb.181.19.5898-5908.1999.

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ABSTRACT ParB is one of two P1-encoded proteins that are required for active partition of the P1 prophage in Escherichia coli. To probe the native domain structure of ParB, we performed limited proteolytic digestions of full-length ParB, as well as of several N-terminal and C-terminal deletion fragments of ParB. The C-terminal 140 amino acids of ParB form a very trypsin-resistant domain. In contrast, the N terminus is more susceptible to proteolysis, suggesting that it forms a less stably folded domain or domains. Because native ParB is a dimer in solution, we analyzed the ability of ParB frag

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9

Miller, Gregory J., Stanley D. Dunn, and Eric H. Ball. "Interaction of the N- and C-terminal Domains of Vinculin." Journal of Biological Chemistry 276, no. 15 (2000): 11729–34. http://dx.doi.org/10.1074/jbc.m008646200.

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The vinculin head to tail intramolecular self-association controls its binding sites for other components of focal adhesions. To study this interaction, the head and tail domains were expressed, purified, and assayed for various characteristics of complex formation. Analytical centrifugation demonstrated a strong interaction in solution and formation of a complex more asymmetric than either of the individual domains. A survey of binding conditions using a solid-phase binding assay revealed characteristics of both electrostatic and hydrophobic forces involved in the binding. In addition, circul

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10

Rubenstein, Eric M., Rhonda R. McCartney, and Martin C. Schmidt. "Regulatory Domains of Snf1-Activating Kinases Determine Pathway Specificity." Eukaryotic Cell 5, no. 4 (2006): 620–27. http://dx.doi.org/10.1128/ec.5.4.620-627.2006.

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ABSTRACT In Saccharomyces cerevisiae, the Snf1 kinase can be activated by any one of three upstream kinases, Sak1, Tos3, or Elm1. All three Snf1-activating kinases contain serine/threonine kinase domains near their N termini and large C-terminal domains with little sequence conservation and previously unknown function. Deletion of the C-terminal domains of Sak1 and Tos3 greatly reduces their ability to activate the Snf1 pathway. In contrast, deletion of the Elm1 C-terminal domain has no effect on Snf1 signaling but abrogates the ability of Elm1 to participate in the morphogenetic-checkpoint si

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11

Nieuwesteeg, M. A., J. A. Willson, M. Cepeda, M. A. Fox, and S. Damjanovski. "Functional Characterization of Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) N- and C-Terminal Domains duringXenopus laevisDevelopment." Scientific World Journal 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/467907.

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Extracellular matrix (ECM) remodeling is essential for facilitating developmental processes. ECM remodeling, accomplished by matrix metalloproteinases (MMPs), is regulated by endogenous tissue inhibitors of metalloproteinases (TIMPs). While the TIMP N-terminal domain is involved in inhibition of MMP activity, the C-terminal domain exhibits cell-signaling activity, which is TIMP and cell type dependent. We have previously examined the distinct roles of theXenopus laevisTIMP-2 and -3 C-terminal domains during development and here examined the unique roles of TIMP-1 N- and C-terminal domains in e

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12

Morgan, B. A., B. A. Mittman, and M. M. Smith. "The highly conserved N-terminal domains of histones H3 and H4 are required for normal cell cycle progression." Molecular and Cellular Biology 11, no. 8 (1991): 4111–20. http://dx.doi.org/10.1128/mcb.11.8.4111.

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The N-terminal domains of the histones H3 and H4 are highly conserved throughout evolution. Mutant alleles deleted for these N-terminal domains were constructed in vitro and examined for function in vivo in Saccharomyces cerevisiae. Cells containing a single deletion allele of either histone H3 or histone H4 were viable. Deletion of the N-terminal domain of histone H4 caused cells to become sterile and temperature sensitive for growth. The normal cell cycle progression of these cells was also altered, as revealed by a major delay in progression through the G2 + M periods. Deletion of the N-ter

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13

Morgan, B. A., B. A. Mittman, and M. M. Smith. "The highly conserved N-terminal domains of histones H3 and H4 are required for normal cell cycle progression." Molecular and Cellular Biology 11, no. 8 (1991): 4111–20. http://dx.doi.org/10.1128/mcb.11.8.4111-4120.1991.

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The N-terminal domains of the histones H3 and H4 are highly conserved throughout evolution. Mutant alleles deleted for these N-terminal domains were constructed in vitro and examined for function in vivo in Saccharomyces cerevisiae. Cells containing a single deletion allele of either histone H3 or histone H4 were viable. Deletion of the N-terminal domain of histone H4 caused cells to become sterile and temperature sensitive for growth. The normal cell cycle progression of these cells was also altered, as revealed by a major delay in progression through the G2 + M periods. Deletion of the N-ter

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14

Watzel, Jonas, Sepas Sarawi, Elke Duchardt-Ferner, Helge B. Bode, and Jens Wöhnert. "NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii." Biomolecular NMR Assignments 15, no. 1 (2021): 229–34. http://dx.doi.org/10.1007/s12104-021-10010-1.

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AbstractNon-ribosomal peptide synthetases (NRPSs) are large multienzyme machineries. They synthesize numerous important natural products starting from amino acids. For peptide synthesis functionally specialized NRPS modules interact in a defined manner. Individual modules are either located on a single or on multiple different polypeptide chains. The “peptide-antimicrobial-Xenorhabdus” (PAX) peptide producing NRPS PaxS from Xenorhabdus bacteria consists of the three proteins PaxA, PaxB and PaxC. Different docking domains (DDs) located at the N-termini of PaxB and PaxC and at the C-termini of P

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15

Liebschner, Dorothee, Krzysztof Brzezinski, Miroslawa Dauter, et al. "Dimeric structure of the N-terminal domain of PriB protein fromThermoanaerobacter tengcongensissolvedab initio." Acta Crystallographica Section D Biological Crystallography 68, no. 12 (2012): 1680–89. http://dx.doi.org/10.1107/s0907444912041637.

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PriB is one of the components of the bacterial primosome, which catalyzes the reactivation of stalled replication forks at sites of DNA damage. The N-terminal domain of the PriB protein from the thermophilic bacteriumThermoanaerobacter tengcongensis(TtePriB) was expressed and its crystal structure was solved at the atomic resolution of 1.09 Å by direct methods. The protein chain, which encompasses the first 104 residues of the full 220-residue protein, adopts the characteristic oligonucleotide/oligosaccharide-binding (OB) structure consisting of a five-stranded β-barrel filled with hydrophobic

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16

Abe, Yoshito, Takaaki Jo, Yusaku Matsuda, Chika Matsunaga, Tsutomu Katayama, and Tadashi Ueda. "Structure and Function of DnaA N-terminal Domains." Journal of Biological Chemistry 282, no. 24 (2007): 17816–27. http://dx.doi.org/10.1074/jbc.m701841200.

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17

Dutta, Anindita, Ahmet Bakan, and Ivet Bahar. "Druggability of Ionotropic Glutamate Receptor N-Terminal Domains." Biophysical Journal 104, no. 2 (2013): 226a. http://dx.doi.org/10.1016/j.bpj.2012.11.1274.

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18

Dos Santos, Patricia C., Archer D. Smith, Jeverson Frazzon, Valerie L. Cash, Michael K. Johnson, and Dennis R. Dean. "Iron-Sulfur Cluster Assembly." Journal of Biological Chemistry 279, no. 19 (2004): 19705–11. http://dx.doi.org/10.1074/jbc.m400278200.

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The NifU protein is a homodimer that is proposed to provide a molecular scaffold for the assembly of [Fe-S] clusters uniquely destined for the maturation of the nitrogenase catalytic components. There are three domains contained within NifU, with the N-terminal domain exhibiting a high degree of primary sequence similarity to a related family of [Fe-S] cluster biosynthetic scaffolds designated IscU. The C-terminal domain of NifU exhibits sequence similarity to a second family of proposed [Fe-S] cluster biosynthetic scaffolds designated Nfu. Genetic experiments described here involving amino ac

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19

Hu, Zonglin, and Joe Lutkenhaus. "Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ." Journal of Bacteriology 182, no. 14 (2000): 3965–71. http://dx.doi.org/10.1128/jb.182.14.3965-3971.2000.

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ABSTRACT In Escherichia coli FtsZ assembles into a Z ring at midcell while assembly at polar sites is prevented by themin system. MinC, a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. In this study we found that MinC consists of two functional domains connected by a short linker. When fused to MalE the N-terminal domain is able to inhibit cell division and prevent FtsZ assembly in vitro. The C-terminal domain interacts with MinD, and expression in wild-type cells as a MalE fusion disrupts minfunction, resulting in a min

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20

Vyas, Payal, and David T. Brown. "N- and C-terminal Domains Determine Differential Nucleosomal Binding Geometry and Affinity of Linker Histone Isotypes H10 and H1c." Journal of Biological Chemistry 287, no. 15 (2012): 11778–87. http://dx.doi.org/10.1074/jbc.m111.312819.

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Eukaryotic linker or H1 histones modulate DNA compaction and gene expression in vivo. In mammals, these proteins exist as multiple isotypes with distinct properties, suggesting a functional significance to the heterogeneity. Linker histones typically have a tripartite structure composed of a conserved central globular domain flanked by a highly variable short N-terminal domain and a longer highly basic C-terminal domain. We hypothesized that the variable terminal domains of individual subtypes contribute to their functional heterogeneity by influencing chromatin binding interactions. We develo

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Herrera, Raul, Charles Anderson, Krishan Kumar, et al. "Reversible Conformational Change in the Plasmodium falciparum Circumsporozoite Protein Masks Its Adhesion Domains." Infection and Immunity 83, no. 10 (2015): 3771–80. http://dx.doi.org/10.1128/iai.02676-14.

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The extended rod-likePlasmodium falciparumcircumsporozoite protein (CSP) is comprised of three primary domains: a charged N terminus that binds heparan sulfate proteoglycans, a central NANP repeat domain, and a C terminus containing a thrombospondin-like type I repeat (TSR) domain. Only the last two domains are incorporated in RTS,S, the leading malaria vaccine in phase 3 trials that, to date, protects about 50% of vaccinated children against clinical disease. A seroepidemiological study indicated that the N-terminal domain might improve the efficacy of a new CSP vaccine. Using a panel of CSP-

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22

Rahier, Renaud, Alexandre Noiriel та Abdelkarim Abousalham. "Functional Characterization of the N-Terminal C2 Domain fromArabidopsis thalianaPhospholipase Dαand Dβ". BioMed Research International 2016 (2016): 1–15. http://dx.doi.org/10.1155/2016/2721719.

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Most of plant phospholipases D (PLD) exhibit a C2-lipid binding domain of around 130 amino acid residues at their N-terminal region, involved in their Ca2+-dependent membrane binding. In this study, we expressed and partially purified catalytically active PLDαfromArabidopsis thaliana(AtPLDα) in the yeastPichia pastoris. The N-terminal amino acid sequence of the recombinant AtPLDαwas found to be NVEETIGV and thus to lack the first 35 amino acid belonging to the C2 domain, as found in other recombinant or plant purified PLDs. To investigate the impact of such a cleavage on the functionality of C

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Himmler, A., D. Drechsel, M. W. Kirschner, and D. W. Martin. "Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains." Molecular and Cellular Biology 9, no. 4 (1989): 1381–88. http://dx.doi.org/10.1128/mcb.9.4.1381.

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Tau proteins consist of a family of proteins, heterogeneous in size, which associate with microtubules in vivo and are induced during neurite outgrowth. In humans, tau is one of the major components of the pathognomonic neurofibrillary tangles in Alzheimer's disease brain. Screening of a cDNA library prepared from bovine brain led to the isolation of several cDNA clones encoding tau proteins with different N termini and differing by insertions or deletions, suggesting differential splicing of the tau transcripts. One of the N-terminal domains and the repeated C-terminal domain of the encoded t

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Himmler, A., D. Drechsel, M. W. Kirschner, and D. W. Martin. "Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains." Molecular and Cellular Biology 9, no. 4 (1989): 1381–88. http://dx.doi.org/10.1128/mcb.9.4.1381-1388.1989.

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Tau proteins consist of a family of proteins, heterogeneous in size, which associate with microtubules in vivo and are induced during neurite outgrowth. In humans, tau is one of the major components of the pathognomonic neurofibrillary tangles in Alzheimer's disease brain. Screening of a cDNA library prepared from bovine brain led to the isolation of several cDNA clones encoding tau proteins with different N termini and differing by insertions or deletions, suggesting differential splicing of the tau transcripts. One of the N-terminal domains and the repeated C-terminal domain of the encoded t

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Tetel, Marc J., Paloma H. Giangrande, Susan A. Leonhardt, Donald P. McDonnell, and Dean P. Edwards. "Hormone-Dependent Interaction between the Amino- and Carboxyl-Terminal Domains of Progesterone Receptor in Vitro and in Vivo." Molecular Endocrinology 13, no. 6 (1999): 910–24. http://dx.doi.org/10.1210/mend.13.6.0300.

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Abstract Full transcriptional activation by steroid hormone receptors requires functional synergy between two transcriptional activation domains (AF) located in the amino (AF-1) and carboxyl (AF-2) terminal regions. One possible mechanism for achieving this functional synergy is a physical intramolecular association between amino (N-) and carboxyl (C-) domains of the receptor. Human progesterone receptor (PR) is expressed in two forms that have distinct functional activities: full-length PR-B and the amino-terminally truncated PR-A. PR-B is generally a stronger activator than PR-A, whereas und

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26

BLUME, Astrid, Wenke WEIDEMANN, Ulrich STELZL, et al. "Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase." Biochemical Journal 384, no. 3 (2004): 599–607. http://dx.doi.org/10.1042/bj20040917.

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UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a bifunctional enzyme, which initiates and regulates sialic acid biosynthesis. Sialic acids are important compounds of mammalian glycoconjugates, mediating several biological processes, such as cell–cell or cell–matrix interactions. In order to characterize the function of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, a number of deletion mutants were generated, lacking either parts of the N-terminal epimerase or the C-terminal kinase domain. N-terminal deletion of only 39 amino acids results in a complete loss

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27

Wang, Ling, Céline Fabret, Kyoko Kanamaru, et al. "Dissection of the Functional and Structural Domains of Phosphorelay Histidine Kinase A of Bacillus subtilis." Journal of Bacteriology 183, no. 9 (2001): 2795–802. http://dx.doi.org/10.1128/jb.183.9.2795-2802.2001.

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ABSTRACT The initiation of sporulation in Bacillus subtilisresults primarily from phosphoryl group input into the phosphorelay by histidine kinases, the major kinase being kinase A. Kinase A is active as a homodimer, the protomer of which consists of an approximately 400-amino-acid N-terminal putative signal-sensing region and a 200-amino-acid C-terminal autokinase. On the basis of sequence similarity, the N-terminal region may be subdivided into three PAS domains: A, B, and C, located from the N- to the C-terminal end. Proteolysis experiments and two-hybrid analyses indicated that dimerizatio

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28

Fursenko, D. V., P. G. Georgiev, and A. N. Bonchuk. "Study of the N-Terminal Domain Homodimerization in Human Proteins with Zinc Finger Clusters." Doklady Biochemistry and Biophysics 499, no. 1 (2021): 257–59. http://dx.doi.org/10.1134/s1607672921040050.

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Abstract CTCF belongs to a large family of transcription factors with clusters of C2H2-type zinc finger domains (C2H2 proteins) and is a main architectural protein in mammals. Human CTCF has a homodimerizing unstructured domain at the N-terminus which is involved in long-distance interactions. To test the presence of similar N-terminal domains in other human C2H2 proteins, a yeast two-hybrid system was used. In total, the ability of unstructured N-terminal domains to homodimerize was investigated for six human C2H2 proteins with an expression profile similar to CTCF. The data indicate the lack

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Heintz, Udo, Anton Meinhart, and Andreas Winkler. "Multi-PAS domain-mediated protein oligomerization of PpsR fromRhodobacter sphaeroides." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (2014): 863–76. http://dx.doi.org/10.1107/s1399004713033634.

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Per–ARNT–Sim (PAS) domains are essential modules of many multi-domain signalling proteins that mediate protein interaction and/or sense environmental stimuli. Frequently, multiple PAS domains are present within single polypeptide chains, where their interplay is required for protein function. Although many isolated PAS domain structures have been reported over the last decades, only a few structures of multi-PAS proteins are known. Therefore, the molecular mechanism of multi-PAS domain-mediated protein oligomerization and function is poorly understood. The transcription factor PpsR fromRhodoba

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Hallin, Erik I., Sigurbjörn Markússon, Lev Böttger, Andrew E. Torda, Clive R. Bramham, and Petri Kursula. "Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc." PLOS ONE 16, no. 5 (2021): e0251459. http://dx.doi.org/10.1371/journal.pone.0251459.

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Synaptic plasticity is vital for brain function and memory formation. One of the key proteins in long-term synaptic plasticity and memory is the activity-regulated cytoskeleton-associated protein (Arc). Mammalian Arc forms virus-like capsid structures in a process requiring the N-terminal domain and contains two C-terminal lobes that are structural homologues to retroviral capsids. Drosophila has two isoforms of Arc, dArc1 and dArc2, with low sequence similarity to mammalian Arc, but lacking a large N-terminal domain. Both dArc isoforms are related to the Ty3/gypsy retrotransposon capsid, cons

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KOBAYASHI, Shigeki, Takeshi YAMAMOTO, Jerome PARNESS, and Noriaki IKEMOTO. "Antibody probe study of Ca2+ channel regulation by interdomain interaction within the ryanodine receptor." Biochemical Journal 380, no. 2 (2004): 561–69. http://dx.doi.org/10.1042/bj20040112.

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N-terminal and central domains of ryanodine receptor 1 (RyR1), where many reported malignant hyperthermia (MH) mutations are localized, represent putative channel regulatory domains. Recent domain peptide (DP) probe studies led us to the hypothesis that these domains interact to stabilize the closed state of channel (zipping), while weakening of domain–domain interactions (unzipping) by mutation de-stabilizes the channel, making it leaky to Ca2+ or sensitive to the agonists of RyR1. As shown previously, DP1 (N-terminal domain peptide) and DP4 (central domain peptide) produced MH-like channel a

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32

Journet, Laure, Alain Rigal, Claude Lazdunski, and Hélène Bénédetti. "Role of TolR N-Terminal, Central, and C-Terminal Domains in Dimerization and Interaction with TolA and TolQ." Journal of Bacteriology 181, no. 15 (1999): 4476–84. http://dx.doi.org/10.1128/jb.181.15.4476-4484.1999.

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ABSTRACT The Tol-PAL system of Escherichia coli is a multiprotein system involved in maintaining the cell envelope integrity and is necessary for the import of some colicins and phage DNA into the bacterium. It is organized into two complexes, one near the outer membrane between TolB and PAL and one in the cytoplasmic membrane between TolA, TolQ, and TolR. In the cytoplasmic membrane, all of the Tol proteins have been shown to interact with each other. Cross-linking experiments have shown that the TolA transmembrane domain interacts with TolQ and TolR. Suppressor mutant analyses have localized

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Singh, Rahul, Sonali Deshmukh, Ashwani Kumar, Venuka Durani Goyal, and Ravindra D. Makde. "Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase." Acta Crystallographica Section F Structural Biology Communications 76, no. 10 (2020): 488–94. http://dx.doi.org/10.1107/s2053230x20011875.

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LonA peptidase is a major component of the protein quality-control mechanism in both prokaryotes and the organelles of eukaryotes. Proteins homologous to the N-terminal domain of LonA peptidase, but lacking its other domains, are conserved in several phyla of prokaryotes, including the Xanthomonadales order. However, the function of these homologous proteins (LonNTD-like proteins) is not known. Here, the crystal structure of the LonNTD-like protein from Xanthomonas campestris (XCC3289; UniProt Q8P5P7) is reported at 2.8 Å resolution. The structure was solved by molecular replacement and contai

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Willett, Julia L. E., Grant C. Gucinski, Jackson P. Fatherree, David A. Low, and Christopher S. Hayes. "Contact-dependent growth inhibition toxins exploit multiple independent cell-entry pathways." Proceedings of the National Academy of Sciences 112, no. 36 (2015): 11341–46. http://dx.doi.org/10.1073/pnas.1512124112.

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Contact-dependent growth inhibition (CDI) systems function to deliver toxins into neighboring bacterial cells. CDI+ bacteria export filamentous CdiA effector proteins, which extend from the inhibitor-cell surface to interact with receptors on neighboring target bacteria. Upon binding its receptor, CdiA delivers a toxin derived from its C-terminal region. CdiA C-terminal (CdiA-CT) sequences are highly variable between bacteria, reflecting the multitude of CDI toxin activities. Here, we show that several CdiA-CT regions are composed of two domains, each with a distinct function during CDI. The C

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Funk, M., B. Poensgen, W. Graulich, V. Jerome, and R. Müller. "A novel, transformation-relevant activation domain in Fos proteins." Molecular and Cellular Biology 17, no. 2 (1997): 537–44. http://dx.doi.org/10.1128/mcb.17.2.537.

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We have previously demonstrated that transformation by Fos is critically dependent on an intact DNA-binding domain (bZip) and a functional N-terminal transactivation motif (N-TM). We now show that a novel motif (C-terminal transactivation motif [C-TM]) near the C terminus also plays an important role in both transformation and the activation of AP1-dependent transcription and that the hydrophobic amino acids in the C-TM are functionally essential. The C-TM is the most crucial element in the C-terminal transactivation domain in Fos, as indicated by its relative strength and context-independent

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Liu, Kaixian, Xiuqi Chen, and Christian M. Kaiser. "Energetic dependencies dictate folding mechanism in a complex protein." Proceedings of the National Academy of Sciences 116, no. 51 (2019): 25641–48. http://dx.doi.org/10.1073/pnas.1914366116.

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Large proteins with multiple domains are thought to fold cotranslationally to minimize interdomain misfolding. Once folded, domains interact with each other through the formation of extensive interfaces that are important for protein stability and function. However, multidomain protein folding and the energetics of domain interactions remain poorly understood. In elongation factor G (EF-G), a highly conserved protein composed of 5 domains, the 2 N-terminal domains form a stably structured unit cotranslationally. Using single-molecule optical tweezers, we have defined the steps leading to fully

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Kashimoto, Takashige, Jun Katahira, Willian R. Cornejo, et al. "Identification of Functional Domains ofBordetella Dermonecrotizing Toxin." Infection and Immunity 67, no. 8 (1999): 3727–32. http://dx.doi.org/10.1128/iai.67.8.3727-3732.1999.

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ABSTRACT Bordetella dermonecrotizing toxin (DNT) stimulates the assembly of actin stress fibers and focal adhesions by deamidating Gln63 of the small GTPase Rho. To clarify the functional and structural organization of DNT, we cloned and sequenced the DNT gene and examined the functions of various DNT mutants. Our analyses of the nucleotide and amino acid sequences revealed that the start codon of the DNT gene is a GTG triplet located 39 bp upstream of the reported putative initiation ATG codon; consequently, DNT contains an additional 13 amino acids at its N-terminal end. All of the N-termina

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Dix, Samuel R., Ruyue Sun, Matthew J. Harris, et al. "TssA from Aeromonas hydrophila: expression, purification and crystallographic studies." Acta Crystallographica Section F Structural Biology Communications 74, no. 9 (2018): 578–82. http://dx.doi.org/10.1107/s2053230x18010439.

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TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ring-forming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crysta

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NAGATA, Kyoko, Kazumasa OHASHI, Neng YANG, and Kensaku MIZUNO. "The N-terminal LIM domain negatively regulates the kinase activity ofLIM-kinase 1." Biochemical Journal 343, no. 1 (1999): 99–105. http://dx.doi.org/10.1042/bj3430099.

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LIM-kinase 1 (LIMK1, where LIM is an acronym of the three gene products Lin-11, Isl-1 and Mec-3) is a serine/threonine kinase that phosphorylates cofilin and regulates actin cytoskeletal reorganization. LIMK1 contains two LIM domains and a PDZ (an acronym of the three proteins PSD-95, Dlg and ZO-1) domain in the N-terminal half and a kinase domain in the C-terminal half. In this study we examined the role of the extra-catalytic region in the regulation of kinase activity of LIMK1. Limited proteolysis of LIMK1 resulted in the production of the 35-40-kDa kinase core fragments with 3.5-5.5-fold i

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Guardado-Calvo, Pablo, Eva M. Muñoz, Antonio L. Llamas-Saiz, et al. "Crystallographic Structure of Porcine Adenovirus Type 4 Fiber Head and Galectin Domains." Journal of Virology 84, no. 20 (2010): 10558–68. http://dx.doi.org/10.1128/jvi.00997-10.

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ABSTRACT Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locat

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Taft-Benz, Sharon A., and Roel M. Schaaper. "The C-Terminal Domain of DnaQ Contains the Polymerase Binding Site." Journal of Bacteriology 181, no. 9 (1999): 2963–65. http://dx.doi.org/10.1128/jb.181.9.2963-2965.1999.

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ABSTRACT The Escherichia coli dnaQ gene encodes the 3′→5′ exonucleolytic proofreading (ɛ) subunit of DNA polymerase III (Pol III). Genetic analysis of dnaQ mutants has suggested that ɛ might consist of two domains, an N-terminal domain containing the exonuclease and a C-terminal domain essential for binding the polymerase (α) subunit. We have created truncated forms ofdnaQ resulting in ɛ subunits that contain either the N-terminal or the C-terminal domain. Using the yeast two-hybrid system, we analyzed the interactions of the single-domain ɛ subunits with the α and θ subunits of the Pol III co

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Dhalluin, Anne, Ingrid Bourgeois, Martine Pestel-Caron, et al. "Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity." Microbiology 151, no. 7 (2005): 2343–51. http://dx.doi.org/10.1099/mic.0.27878-0.

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A gene encoding a putative peptidoglycan hydrolase was identified by sequence similarity searching in the Clostridium difficile 630 genome sequence, and the corresponding protein, named Acd (autolysin of C. difficile) was expressed in Escherichia coli. The deduced amino acid sequence of Acd shows a modular structure with two main domains: an N-terminal domain exhibiting repeated sequences and a C-terminal catalytic domain. The C-terminal domain exhibits sequence similarity with the glucosaminidase domains of Staphylococcus aureus Atl and Bacillus subtilis LytD autolysins. Purified recombinant

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Tian, M., and G. S. Martin. "The role of the Src homology domains in morphological transformation by v-src." Molecular Biology of the Cell 8, no. 7 (1997): 1183–93. http://dx.doi.org/10.1091/mbc.8.7.1183.

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The Src homology (SH2 and SH3) domains of v-Src are required for transformation of Rat-2 cells and for wild-type (morphr) transformation of chicken embryo fibroblasts (CEFs). We report herein that the N-terminal domains of v-Src, when expressed in trans, cannot complement the transformation defect of a deletion mutant lacking the "unique," SH3, and SH2 regions. However, the same regions of Src can promote transformation when translocated to the C terminus of v-Src, although the transformation of CEFs is somewhat slower. We conclude that the SH3 and SH2 domains must be present in cis to the cat

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Pittman, Jon K., Coimbatore S. Sreevidya, Toshiro Shigaki, Hanayo Ueoka-Nakanishi, and Kendal D. Hirschi. "Distinct N-Terminal Regulatory Domains of Ca2+/H+ Antiporters." Plant Physiology 130, no. 2 (2002): 1054–62. http://dx.doi.org/10.1104/pp.008193.

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Chestukhina, G. G., S. A. Tyurin, L. I. Kostina, et al. "Subdomain organization ofBacillus thuringiensis entomocidal proteins' N-terminal domains." Journal of Protein Chemistry 9, no. 4 (1990): 501–7. http://dx.doi.org/10.1007/bf01024627.

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Sirrieh, Rita E., David M. MacLean, and Vasanthi Jayaraman. "Arrangement of the N-Terminal Domains in NMDA Receptors." Biophysical Journal 104, no. 2 (2013): 272a—273a. http://dx.doi.org/10.1016/j.bpj.2012.11.1529.

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Makarov, Valentin V., Ekaterina N. Rybakova, Alexander V. Efimov, et al. "Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1." Journal of General Virology 90, no. 12 (2009): 3022–32. http://dx.doi.org/10.1099/vir.0.013862-0.

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Three ‘triple gene block’ proteins known as TGBp1, TGBp2 and TGBp3 are required for cell-to-cell movement of plant viruses belonging to a number of genera including Hordeivirus. Hordeiviral TGBp1 interacts with viral genomic RNAs to form ribonucleoprotein (RNP) complexes competent for translocation between cells through plasmodesmata and over long distances via the phloem. Binding of hordeivirus TGBp1 to RNA involves two protein regions, the C-terminal NTPase/helicase domain and the N-terminal extension region. This study demonstrated that the extension region of hordeivirus TGBp1 consists of

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Hutchinson, Oliver Clyde, Wendy Smith, Nicola G. Jones, Anasuya Chattopadhyay, Susan C. Welburn, and Mark Carrington. "VSG structure: similar N-terminal domains can form functional VSGs with different types of C-terminal domain." Molecular and Biochemical Parasitology 130, no. 2 (2003): 127–31. http://dx.doi.org/10.1016/s0166-6851(03)00144-0.

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Yu, G., J. Swiston, and D. Young. "Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins." Journal of Cell Science 107, no. 6 (1994): 1671–78. http://dx.doi.org/10.1242/jcs.107.6.1671.

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We previously reported the identification of human CAP, a protein that is related to the Saccharomyces cerevisiae and Schizosaccharomyces pombe adenylyl cyclase-associated CAP proteins. The two yeast CAP proteins have similar functions: the N-terminal domains are required for the normal function of adenylyl cyclase, while loss of the C-terminal domains result in morphological and nutritional defects that are unrelated to the cAMP pathways. We have amplified and cloned cDNAs from a human glioblastoma library that encode a second CAP-related protein, CAP2. The human CAP and CAP2 proteins are 64%

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Papoff, Giuliana, Nadia Trivieri, Sonia Marsilio, et al. "N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction." PLOS ONE 10, no. 2 (2015): e0116251. http://dx.doi.org/10.1371/journal.pone.0116251.

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