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Artículos de revistas sobre el tema "Protein N-terminal modifications"

Autor: Grafiati

Publicado: 21 de diciembre de 2024

Última modificación: 28 de julio de 2025

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1

Lai, Zon W., Agnese Petrera, and Oliver Schilling. "Protein amino-terminal modifications and proteomic approaches for N-terminal profiling." Current Opinion in Chemical Biology 24 (February 2015): 71–79. http://dx.doi.org/10.1016/j.cbpa.2014.10.026.

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2

Voronina, A. I., Yu V. Miroshnichenko, and V. S. Skvortsov. "Bioinformatic identification of proteins with altered PTM levels in a mouse line established to study the mechanisms of the development of fibromuscular dysplasia." Biomeditsinskaya Khimiya 70, no. 4 (2024): 248–55. http://dx.doi.org/10.18097/pbmc20247004248.

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Data from a mass spectrometry experiment of a mouse line developed to study the mechanisms of fibromuscular dysplasia and deposited by d'Escamard et al. in ProteomeXchange (PXD051750) have been analyzed. Identification of peptides with post-translational modifications (PTMs) was repeated using more stringent conditions than in the original work. The following modifications were considered during analysis of changes in the PTM levels in experimental and control groups of mice: acetylation of lysine residue and N-terminal protein peptide, ubiquitination of lysine residue, phosphorylation of seri

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3

Yu, Guann-Yi, Ki-Jeong Lee, Lu Gao, and Michael M. C. Lai. "Palmitoylation and Polymerization of Hepatitis C Virus NS4B Protein." Journal of Virology 80, no. 12 (2006): 6013–23. http://dx.doi.org/10.1128/jvi.00053-06.

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ABSTRACT Hepatitis C Virus (HCV) NS4B protein induces a specialized membrane structure which may serve as the replication platform for HCV RNA replication. In the present study, we demonstrated that NS4B has lipid modifications (palmitoylation) on two cysteine residues (cysteines 257 and 261) at the C-terminal end. Site-specific mutagenesis of these cysteine residues on individual NS4B proteins and on an HCV subgenomic replicon showed that the lipid modifications, particularly of Cys261, are important for protein-protein interaction in the formation of the HCV RNA replication complex. We furth

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4

Meinnel, Thierry, and Carmela Giglione. "Tools for analyzing and predicting N-terminal protein modifications." PROTEOMICS 8, no. 4 (2008): 626–49. http://dx.doi.org/10.1002/pmic.200700592.

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5

Dissmeyer, Nico. "Conditional Protein Function via N-Degron Pathway–Mediated Proteostasis in Stress Physiology." Annual Review of Plant Biology 70, no. 1 (2019): 83–117. http://dx.doi.org/10.1146/annurev-arplant-050718-095937.

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The N-degron pathway, formerly the N-end rule pathway, regulates functions of regulatory proteins. It impacts protein half-life and therefore directs the actual presence of target proteins in the cell. The current concept holds that the N-degron pathway depends on the identity of the amino (N)-terminal amino acid and many other factors, such as the follow-up sequence at the N terminus, conformation, flexibility, and protein localization. It is evolutionarily conserved throughout the kingdoms. One possible entry point for substrates of the N-degron pathway is oxidation of N-terminal Cys residue

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6

Lee, Seon Hwa, and Tomoyuki Oe. "Oxidative stress-mediated N-terminal protein modifications and MS-based approaches for N-terminal proteomics." Drug Metabolism and Pharmacokinetics 31, no. 1 (2016): 27–34. http://dx.doi.org/10.1016/j.dmpk.2015.12.002.

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7

Rose, K., P. O. Regamey, R. Anderegg, T. N. C. Wells, and A. E. I. Proudfoot. "Human interleukin-5 expressed in Escherichia coli has N-terminal modifications." Biochemical Journal 286, no. 3 (1992): 825–28. http://dx.doi.org/10.1042/bj2860825.

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Recombinant human interleukin-5 exists as four major isoforms all possessing N-terminal methionine. Peptide mapping and subsequent analysis by fast-atom-bombardment mass spectrometry (f.a.b.-m.s.) have shown that N-terminal modifications are the cause of the charge heterogeneity. In order of decreasing abundance, these are unmodified methionine, retention of N-terminal formyl group, oxidation of N-terminal methionine to sulphoxide and carbamoylation of the N-terminus. These results were confirmed by analysis of the reduced and alkylated intact protein by electrospray-ionization mass spectromet

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8

Van Damme, Petra. "Charting the N-Terminal Acetylome: A Comprehensive Map of Human NatA Substrates." International Journal of Molecular Sciences 22, no. 19 (2021): 10692. http://dx.doi.org/10.3390/ijms221910692.

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N-terminal acetylation (Nt-acetylation) catalyzed by conserved N-terminal acetyltransferases or NATs embodies a modification with one of the highest stoichiometries reported for eukaryotic protein modifications to date. Comprising the catalytic N-alpha acetyltransferase (NAA) subunit NAA10 plus the ribosome anchoring regulatory subunit NAA15, NatA represents the major acetyltransferase complex with up to 50% of all mammalian proteins representing potential substrates. Largely in consequence of the essential nature of NatA and its high enzymatic activity, its experimentally confirmed mammalian

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9

Ouidir, Tassadit, Frédérique Jarnier, Pascal Cosette, Thierry Jouenne, and Julie Hardouin. "Characterization of N-terminal protein modifications in Pseudomonas aeruginosa PA14." Journal of Proteomics 114 (January 2015): 214–25. http://dx.doi.org/10.1016/j.jprot.2014.11.006.

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10

Giglione, Carmela, Sonia Fieulaine, and Thierry Meinnel. "N-terminal protein modifications: Bringing back into play the ribosome." Biochimie 114 (July 2015): 134–46. http://dx.doi.org/10.1016/j.biochi.2014.11.008.

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11

Millar, A. Harvey, Joshua L. Heazlewood, Carmela Giglione, Michael J. Holdsworth, Andreas Bachmair, and Waltraud X. Schulze. "The Scope, Functions, and Dynamics of Posttranslational Protein Modifications." Annual Review of Plant Biology 70, no. 1 (2019): 119–51. http://dx.doi.org/10.1146/annurev-arplant-050718-100211.

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Assessing posttranslational modification (PTM) patterns within protein molecules and reading their functional implications present grand challenges for plant biology. We combine four perspectives on PTMs and their roles by considering five classes of PTMs as examples of the broader context of PTMs. These include modifications of the N terminus, glycosylation, phosphorylation, oxidation, and N-terminal and protein modifiers linked to protein degradation. We consider the spatial distribution of PTMs, the subcellular distribution of modifying enzymes, and their targets throughout the cell, and we

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12

Brettrager, Segura, and van Waardenburg. "Tyrosyl-DNA Phosphodiesterase I N-Terminal Domain Modifications and Interactions Regulate Cellular Function." Genes 10, no. 11 (2019): 897. http://dx.doi.org/10.3390/genes10110897.

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The conserved eukaryotic DNA repair enzyme Tyrosyl-DNA phosphodiesterase I (Tdp1) removes a diverse array of adducts from the end of DNA strand breaks. Tdp1 specifically catalyzes the hydrolysis of phosphodiester linked DNA-adducts. These DNA lesions range from damaged nucleotides to peptide-DNA adducts to protein-DNA covalent complexes and are products of endogenously or exogenously induced insults or simply failed reaction products. These adducts include DNA inserted ribonucleotides and non-conventional nucleotides, as well as covalent reaction intermediates of DNA topoisomerases with DNA an

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13

Paskevicius, Tautvydas, Rabih Abou Farraj, Marek Michalak, and Luis B. Agellon. "Calnexin, More than Just a Molecular Chaperone." Cells 12, no. 3 (2023): 403. http://dx.doi.org/10.3390/cells12030403.

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Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in the folding and quality control of membrane-associated and secreted proteins, a function that is attributed to its ER- localized domain with a structure that bears a strong resemblance to another luminal ER chaperone and Ca2+-binding protein known as calreticulin. Studies have discovered that the cytosolic C-terminal domain of calnexin u

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14

Nassiri Toosi, Zahra, Xinya Su, Ruth Austin та ін. "Combinatorial phosphorylation modulates the structure and function of the G protein γ subunit in yeast". Science Signaling 14, № 688 (2021): eabd2464. http://dx.doi.org/10.1126/scisignal.abd2464.

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Intrinsically disordered regions (IDRs) in proteins are often targets of combinatorial posttranslational modifications, which serve to regulate protein structure and function. Emerging evidence suggests that the N-terminal tails of G protein γ subunits, which are essential components of heterotrimeric G proteins, are intrinsically disordered, phosphorylation-dependent determinants of G protein signaling. Here, we found that the yeast Gγ subunit Ste18 underwent combinatorial, multisite phosphorylation events within its N-terminal IDR. G protein–coupled receptor (GPCR) activation and osmotic str

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15

Engle, Sarah M., Justin J. Crowder, Sheldon G. Watts, Christopher J. Indovina, Samuel Z. Coffey, and Eric M. Rubenstein. "Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon." PeerJ 5 (August 22, 2017): e3728. http://dx.doi.org/10.7717/peerj.3728.

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Conserved homologues of the Hrd1 ubiquitin ligase target for degradation proteins that persistently or aberrantly engage the endoplasmic reticulum translocon, including mammalian apolipoprotein B (apoB; the major protein component of low-density lipoproteins) and the artificial yeast protein Deg1-Sec62. A complete understanding of the molecular mechanism by which translocon-associated proteins are recognized and degraded may inform the development of therapeutic strategies for cholesterol-related pathologies. Both apoB and Deg1-Sec62 are extensively post-translationally modified. Mass spectrom

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16

Yao, Shixiang, and Chibuike C. Udenigwe. "Peptidomics of potato protein hydrolysates: implications of post-translational modifications in food peptide structure and behaviour." Royal Society Open Science 5, no. 7 (2018): 172425. http://dx.doi.org/10.1098/rsos.172425.

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Post-translational modifications (PTMs) often occur in proteins and play a regulatory role in protein function. There is an increasing interest in the bioactivity of food protein-derived peptides, but the occurrence of PTMs and their influence on food peptide structure and behaviour remain largely unknown. In this study, the shotgun-based peptidomics strategy was used to identify the occurrence of PTMs in peptides generated from potato protein hydrolysis using digestive proteases. Diverse PTMs were found in the potato peptides, including acetylation of lysine, N-terminal of proteins and peptid

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17

Umelo-Njaka, Elizabeth, Wade H. Bingle, Faten Borchani, et al. "Caulobacter crescentus Synthesizes an S-Layer-Editing Metalloprotease Possessing a Domain Sharing Sequence Similarity with Its Paracrystalline S-Layer Protein." Journal of Bacteriology 184, no. 10 (2002): 2709–18. http://dx.doi.org/10.1128/jb.184.10.2709-2718.2002.

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ABSTRACT Strains of Caulobacter crescentus elaborate an S-layer, a two-dimensional protein latticework which covers the cell surface. The S-layer protein (RsaA) is secreted by a type I mechanism (relying on a C-terminal signal) and is unusual among type I secreted proteins because high levels of protein are produced continuously. In efforts to adapt the S-layer for display of foreign peptides and proteins, we noted a proteolytic activity that affected S-layer monomers with foreign inserts. The cleavage was precise, resulting in fragments with an unambiguous N-terminal sequence. We developed an

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18

Schwarz-Ben Meir, N., T. Glaser, and N. S. Kosower. "Band 3 protein degradation by calpain is enhanced in erythrocytes of old people." Biochemical Journal 275, no. 1 (1991): 47–52. http://dx.doi.org/10.1042/bj2750047.

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Band 3 protein is a major erythrocyte transmembrane glycoprotein. We compared the degradation of band 3 protein by calpain I (a cytoplasmic, micromolar-Ca2(+)-requiring thiol proteinase) in the cells from old individuals (greater than 70 years old) to that in the cells from young ones (20-30 years old). In the young, little degradation of band 3 protein occurred in calpain-treated erythrocyte ghosts. In the old, significant band 3 protein degradation was found in erythrocyte ghosts treated similarly. The difference between young and old in the susceptibility of band 3 protein to calpain was re

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19

Wieczorek, Andrew, Clara K. Chan, Suzana Kovacic, Cindy Li, Thomas Dierks, and Nancy R. Forde. "Genetically modified human type II collagen for N- and C-terminal covalent tagging." Canadian Journal of Chemistry 96, no. 2 (2018): 204–11. http://dx.doi.org/10.1139/cjc-2017-0335.

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Collagen is the predominant structural protein in vertebrates, where it contributes to connective tissues and the ECM; it is also widely used in biomaterials and tissue engineering. Dysfunction of this protein and its processing can lead to a wide variety of developmental disorders and connective tissue diseases. Recombinantly engineering the protein is challenging due to post-translational modifications generally required for its stability and secretion from cells. Introducing end labels into the protein is problematic, because the N- and C-termini of the physiologically relevant tropocollage

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20

Cornish, Jasmine, Darerca Owen, and Helen R. Mott. "RLIP76: A Structural and Functional Triumvirate." Cancers 13, no. 9 (2021): 2206. http://dx.doi.org/10.3390/cancers13092206.

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RLIP76/RalBP1 is an ATP-dependent transporter of glutathione conjugates, which is overexpressed in various human cancers, but its diverse functions in normal cells, which include endocytosis, stress response and mitochondrial dynamics, are still not fully understood. The protein can be divided into three distinct regions, each with its own structural properties. At the centre of the protein are two well-defined domains, a GTPase activating protein domain targeting Rho family small G proteins and a small coiled-coil that binds to the Ras family small GTPases RalA and RalB. In engaging with Rho

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21

Ogino, Tomoaki, Hiroyuki Fukuda, Shinobu Imajoh-Ohmi, Michinori Kohara, and Akio Nomoto. "Membrane Binding Properties and Terminal Residues of the Mature Hepatitis C Virus Capsid Protein in Insect Cells." Journal of Virology 78, no. 21 (2004): 11766–77. http://dx.doi.org/10.1128/jvi.78.21.11766-11777.2004.

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ABSTRACT The immature core protein (p23, residues 1 to 191) of hepatitis C virus undergoes posttranslational modifications including intramembranous proteolysis within its C-terminal signal sequence by signal peptide peptidase to generate the mature form (p21). In this study, we analyzed the cleavage site and other amino acid modifications that occur on the core protein. To produce the posttranslationally modified core protein, we used a baculovirus-insect cell expression model system. As previously reported, p23 is processed to form p21 in insect as well as in mammalian cells. p21 was found t

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22

Starheim, Kristian K., Darina Gromyko, Rune Evjenth та ін. "Knockdown of Human Nα-Terminal Acetyltransferase Complex C Leads to p53-Dependent Apoptosis and Aberrant Human Arl8b Localization". Molecular and Cellular Biology 29, № 13 (2009): 3569–81. http://dx.doi.org/10.1128/mcb.01909-08.

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ABSTRACT Protein Nα-terminal acetylation is one of the most common protein modifications in eukaryotic cells. In yeast, three major complexes, NatA, NatB, and NatC, catalyze nearly all N-terminal acetylation, acetylating specific subsets of protein N termini. In human cells, only the NatA and NatB complexes have been described. We here identify and characterize the human NatC (hNatC) complex, containing the catalytic subunit hMak3 and the auxiliary subunits hMak10 and hMak31. This complex associates with ribosomes, and hMak3 acetylates Met-Leu protein N termini in vitro, suggesting a model in

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23

Webber, Matthew J., Eric A. Appel, Brittany Vinciguerra, et al. "Supramolecular PEGylation of biopharmaceuticals." Proceedings of the National Academy of Sciences 113, no. 50 (2016): 14189–94. http://dx.doi.org/10.1073/pnas.1616639113.

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The covalent modification of therapeutic biomolecules has been broadly explored, leading to a number of clinically approved modified protein drugs. These modifications are typically intended to address challenges arising in biopharmaceutical practice by promoting improved stability and shelf life of therapeutic proteins in formulation, or modifying pharmacokinetics in the body. Toward these objectives, covalent modification with poly(ethylene glycol) (PEG) has been a common direction. Here, a platform approach to biopharmaceutical modification is described that relies on noncovalent, supramole

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24

Bennick, A. "Structural and Genetic Aspects of Proline-rich Proteins." Journal of Dental Research 66, no. 2 (1987): 457–61. http://dx.doi.org/10.1177/00220345870660021201.

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Considerable advances have been made in the genetics of salivary proline-rich proteins (PRP). The genes for acidic, basic, and glycosylated PRP have been cloned. They code for precursor proteins that all have an acidic N-terminal followed by proline-rich repeat sequences. Structural studies on secreted proteins have demonstrated that not only acidic but also some basic PRPs have this general structure. It is possible that mRNA for different PRP may have originated from a single gene by differential mRNA splicing, but post-translational cleavages of the primary translation product apparently al

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25

Franco, Aitor, Jorge Cuéllar, José Ángel Fernández-Higuero та ін. "Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-Based Disaggregase". International Journal of Molecular Sciences 22, № 23 (2021): 12983. http://dx.doi.org/10.3390/ijms222312983.

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The aggregation of α-synuclein is the hallmark of a collective of neurodegenerative disorders known as synucleinopathies. The tendency to aggregate of this protein, the toxicity of its aggregation intermediates and the ability of the cellular protein quality control system to clear these intermediates seems to be regulated, among other factors, by post-translational modifications (PTMs). Among these modifications, we consider herein proteolysis at both the N- and C-terminal regions of α-synuclein as a factor that could modulate disassembly of toxic amyloids by the human disaggregase, a combina

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26

Ji, Chengjie, Zhengping Wang, and Liang Li. "Protein mass measurement combined with mass spectrometric sequencing of protein digests for detection and characterization of protein modifications1." Canadian Journal of Chemistry 84, no. 7 (2006): 986–97. http://dx.doi.org/10.1139/v06-114.

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A method for the characterization of modifications of low molecular weight proteins (<20 kDa) extracted from a microorganism based on the use of multiple separation tools and mass spectrometric techniques is described. In this method, intact proteins from cell extracts are first separated and fractionated by liquid chromatography (LC). Individual fractions are then analyzed by matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) to provide intact protein mass information. The fractions are further characterized by using trypsin digestion and LC electrospray ionization

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27

Sharma, Ajit K., Abhilasha Mansukh, Ashok Varma, Nikhil Gadewal та Sanjay Gupta. "Molecular Modeling of Differentially Phosphorylated Serine 10 and Acetylated lysine 9/14 of Histone H3 Regulates their Interactions with 14-3-3ζ, MSK1, and MKP1". Bioinformatics and Biology Insights 7 (січень 2013): BBI.S12449. http://dx.doi.org/10.4137/bbi.s12449.

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Histone modifications occur in precise patterns, with several modifications known to affect the binding of proteins. These interactions affect the chromatin structure, gene regulation, and cell cycle events. The dual modifications on the H3 tail, serine10 phosphorylation, and lysine14 acetylation (H3Ser10PLys14Ac) are reported to be crucial for interaction with 14-3-3ζ. However, the mechanism by which H3Ser10P along with neighboring site-specific acetylation(s) is targeted by its regulatory proteins, including kinase and phosphatase, is not fully understood. We carried out molecular modeling s

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28

Azevedo, Cristina, and Adolfo Saiardi. "The new world of inorganic polyphosphates." Biochemical Society Transactions 44, no. 1 (2016): 13–17. http://dx.doi.org/10.1042/bst20150210.

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Post-translational modifications (PTMs) add regulatory features to proteins that help establish the complex functional networks that make up higher organisms. Advances in analytical detection methods have led to the identification of more than 200 types of PTMs. However, some modifications are unstable under the present detection methods, anticipating the existence of further modifications and a much more complex map of PTMs. An example is the recently discovered protein modification polyphosphorylation. Polyphosphorylation is mediated by inorganic polyphosphate (polyP) and represents the cova

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29

Abdul, Shiraazkhan, Frank W. G. Leebeek, Dingeman C. Rijken та Shirley Uitte de Willige. "Natural heterogeneity of α2-antiplasmin: functional and clinical consequences". Blood 127, № 5 (2016): 538–45. http://dx.doi.org/10.1182/blood-2015-09-670117.

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AbstractHuman α2-antiplasmin (α2AP, also called α2-plasmin inhibitor) is the main physiological inhibitor of the fibrinolytic enzyme plasmin. α2AP inhibits plasmin on the fibrin clot or in the circulation by forming plasmin-antiplasmin complexes. Severely reduced α2AP levels in hereditary α2AP deficiency may lead to bleeding symptoms, whereas increased α2AP levels have been associated with increased thrombotic risk. α2AP is a very heterogeneous protein. In the circulation, α2AP undergoes both amino terminal (N-terminal) and carboxyl terminal (C-terminal) proteolytic modifications that signific

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30

Zlatkine, P., B. Mehul, and A. I. Magee. "Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif." Journal of Cell Science 110, no. 5 (1997): 673–79. http://dx.doi.org/10.1242/jcs.110.5.673.

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Several members of the Src family of protein tyrosine kinases have a N-terminal dual acylation motif which specifies their myristoylation and S-acylation. These lipid modifications are necessary for correct intracellular localisation to the plasma membrane and to detergent-resistant glycolipid-enriched membrane domains (GEMs). Using chimaeras of the Lck dual acylation motif with two normally cytosolic proteins (chloramphenicol acetyl transferase and galectin-3), we show here that this motif is sufficient to encode correct lipid modification and to target these chimaeras to the plasma membrane,

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31

Feng, Jinlin, Jianxin Hu, Yan Li, Ruiqi Li, Hao Yu, and Ligeng Ma. "The N-Terminal Acetyltransferase Naa50 Regulates Arabidopsis Growth and Osmotic Stress Response." Plant and Cell Physiology 61, no. 9 (2020): 1565–75. http://dx.doi.org/10.1093/pcp/pcaa081.

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Abstract N-terminal acetylation (Nt-acetylation) is one of the most common protein modifications in eukaryotes. The function of Naa50, the catalytic subunit of the evolutionarily conserved N-terminal acetyltransferase (Nat) E complex, has not been reported in Arabidopsis. In this study, we found that a loss of Naa50 resulted in a pleiotropic phenotype that included dwarfism and sterility, premature leaf senescence and a shortened primary root. Further analysis revealed that root cell patterning and various root cell properties were severely impaired in naa50 mutant plants. Moreover, defects in

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Nevitt, Chris, John G. Tooley, and Christine E. Schaner Tooley. "N-terminal acetylation and methylation differentially affect the function of MYL9." Biochemical Journal 475, no. 20 (2018): 3201–19. http://dx.doi.org/10.1042/bcj20180638.

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Deciphering the histone code has illustrated that acetylation or methylation on the same residue can have analogous or opposing roles. However, little is known about the interplay between these post-translational modifications (PTMs) on the same nonhistone residues. We have recently discovered that N-terminal acetyltransferases (NATs) and N-terminal methyltransferases (NRMTs) can have overlapping substrates and identified myosin regulatory light chain 9 (MYL9) as the first confirmed protein to occur in either α-amino-methylated (Nα-methyl) or α-amino-acetylated (Nα-acetyl) states in vivo. Here

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Crandall, I., and I. W. Sherman. "Plasmodium falciparum (human malaria)-induced modifications in human erythrocyte band 3 protein." Parasitology 102, no. 3 (1991): 335–40. http://dx.doi.org/10.1017/s0031182000064271.

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A monoclonal antibody, 1C4, was produced which recognizes a 65 kDa protein that is localized to the plasma membrane of human erythrocytes infected with Plasmodium falciparum. By immunofluorescence the antigen was visualized as dots on the surface of the infected cell. The 65 kDa protein was present in 4 strains of diverse geographical origin, and in erythrocytes infected with a knobless strain. The 65 kDa protein was insoluble in non-ionic detergents, but was partly soluble in SDS and some high (1 M) śalt solutions. The 65 kDa protein is recognized by antibodies specific for the cytoplasmic do

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34

Beranger, F., H. Paterson, S. Powers, J. de Gunzburg, and J. F. Hancock. "The effector domain of Rab6, plus a highly hydrophobic C terminus, is required for Golgi apparatus localization." Molecular and Cellular Biology 14, no. 1 (1994): 744–58. http://dx.doi.org/10.1128/mcb.14.1.744-758.1994.

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C-terminal lipid modifications are essential for the interaction of Ras-related proteins with membranes. While all Ras proteins are farnesylated and some palmitoylated, the majority of other Ras-related proteins are geranylgeranylated. One such protein, Rab6, is associated with the Golgi apparatus and has a C-terminal CXC motif that is geranylgeranylated on both cysteines. We show here that farnesylation alone cannot substitute for geranylgeranylation in targeting Rab6 to the Golgi apparatus and that whereas Ras proteins that are farnesylated and palmitoylated are targeted to the plasma membra

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35

Beranger, F., H. Paterson, S. Powers, J. de Gunzburg, and J. F. Hancock. "The effector domain of Rab6, plus a highly hydrophobic C terminus, is required for Golgi apparatus localization." Molecular and Cellular Biology 14, no. 1 (1994): 744–58. http://dx.doi.org/10.1128/mcb.14.1.744.

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C-terminal lipid modifications are essential for the interaction of Ras-related proteins with membranes. While all Ras proteins are farnesylated and some palmitoylated, the majority of other Ras-related proteins are geranylgeranylated. One such protein, Rab6, is associated with the Golgi apparatus and has a C-terminal CXC motif that is geranylgeranylated on both cysteines. We show here that farnesylation alone cannot substitute for geranylgeranylation in targeting Rab6 to the Golgi apparatus and that whereas Ras proteins that are farnesylated and palmitoylated are targeted to the plasma membra

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36

Shuvo, Sabbir R., Uliana Kovaltchouk, Abdullah Zubaer, et al. "Functional characterization of an N-terminally-truncated mitochondrial porin expressed in Neurospora crassa." Canadian Journal of Microbiology 63, no. 8 (2017): 730–38. http://dx.doi.org/10.1139/cjm-2016-0764.

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Mitochondrial porin, which forms voltage-dependent anion-selective channels (VDAC) in the outer membrane, can be folded into a 19-β-stranded barrel. The N terminus of the protein is external to the barrel and contains α-helical structure. Targeted modifications of the N-terminal region have been assessed in artificial membranes, leading to different models for gating in vitro. However, the in vivo requirements for gating and the N-terminal segment of porin are less well-understood. Using Neurospora crassa porin as a model, the effects of a partial deletion of the N-terminal segment were invest

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Suzuki, Takashi, Masaaki Ito, Toru Ezure, et al. "N-Terminal protein modifications in an insect cell-free protein synthesis system and their identification by mass spectrometry." PROTEOMICS 6, no. 16 (2006): 4486–95. http://dx.doi.org/10.1002/pmic.200600126.

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Shang, Tao, Chee Mun Fang, Chin Eng Ong, and Yan Pan. "Heterologous Expression of Recombinant Human Cytochrome P450 (CYP) in Escherichia coli: N-Terminal Modification, Expression, Isolation, Purification, and Reconstitution." BioTech 12, no. 1 (2023): 17. http://dx.doi.org/10.3390/biotech12010017.

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Cytochrome P450 (CYP) enzymes play important roles in metabolising endogenous and xenobiotic substances. Characterisations of human CYP proteins have been advanced with the rapid development of molecular technology that allows heterologous expression of human CYPs. Among several hosts, bacteria systems such as Escherichia coli (E. coli) have been widely used thanks to their ease of use, high level of protein yields, and affordable maintenance costs. However, the levels of expression in E. coli reported in the literature sometimes differ significantly. This paper aims to review several contribu

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Pauly, P. C., and C. Klein. "Lack of glycosyl-phosphatidylinositol anchoring leads to precursor retention by a unique mechanism in Dictyostelium discoideum." Biochemical Journal 306, no. 3 (1995): 643–50. http://dx.doi.org/10.1042/bj3060643.

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Gp80, a cell-adhesion molecule in Dictyostelium discoideum, is modified by N- and O-linked oligosaccharides, and a glycosylphosphatidylinositol (GPI) anchor. To identify sequences important for the addition of these modifications to gp80, we created a hybrid protein in which the C-terminal 136 amino acids of yeast invertase were replaced by the C-terminal 110 amino acids of gp80. When expressed in D. discoideum, this protein (Inv-gp80) was not GPI-anchored and was retained in a pre-Golgi compartment. Inv-gp80 did, however, display characteristics of a transmembrane protein, suggesting a novel

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Soshnikova, N. V., A. A. Sheynov, Eu V. Tatarskiy, and S. G. Georgieva. "The DPF Domain As a Unique Structural Unit Participating in Transcriptional Activation, Cell Differentiation, and Malignant Transformation." Acta Naturae 12, no. 4 (2020): 57–65. http://dx.doi.org/10.32607/actanaturae.11092.

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The DPF (double PHD finger) domain consists of two PHD fingers organized in tandem. The two PHD-finger domains within a DPF form a single structure that interacts with the modification of the N-terminal histone fragment in a way different from that for single PHD fingers. Several histone modifications interacting with the DPF domain have already been identified. They include acetylation of H3K14 and H3K9, as well as crotonylation of H3K14. These modifications are found predominantly in transcriptionally active chromatin. Proteins containing DPF belong to two classes of protein complexes, which

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Yao, Xuejing, Guiping Qi, Yaocheng Qu, et al. "Structural Characterization of RC28-E, a Recombinant Fusion Protein With Dual Targets on VEGF and FGF2." Natural Product Communications 17, no. 3 (2022): 1934578X2210869. http://dx.doi.org/10.1177/1934578x221086989.

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Vascular endothelial growth factor (VEGF) and fibroblast growthfactor (FGF) play important roles in angiogenesis-related diseases. RC28-E is a soluble fusion protein composed of the human VEGF receptor 1 (VEGFR1) extracellular domain 2 (ECD 2), VEGFR2 ECD 3, FGFR1 ECDs 2 and 3, and the Fc regions of human immunoglobulin G1. By targeting both VEGF and FGF2, RC28-E may represent a useful antiangiogenetic agent, but structural and functional characterizations of this fusion protein are needed. Liquid chromatography–tandem mass spectrometry, size exclusion high-performance liquid chromatography, c

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Heissenberger, Clemens, Lisa Liendl, Fabian Nagelreiter, et al. "Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein synthesis and normal growth." Nucleic Acids Research 47, no. 22 (2019): 11807–25. http://dx.doi.org/10.1093/nar/gkz1043.

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Abstract Modifications of ribosomal RNA expand the nucleotide repertoire and thereby contribute to ribosome heterogeneity and translational regulation of gene expression. One particular m5C modification of 25S ribosomal RNA, which is introduced by Rcm1p, was previously shown to modulate stress responses and lifespan in yeast and other small organisms. Here, we report that NSUN5 is the functional orthologue of Rcm1p, introducing m5C3782 into human and m5C3438 into mouse 28S ribosomal RNA. Haploinsufficiency of the NSUN5 gene in fibroblasts from William Beuren syndrome patients causes partial lo

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Malo, Mackenzie E., and Larry Fliegel. "Physiological role and regulation of the Na+/H+ exchanger." Canadian Journal of Physiology and Pharmacology 84, no. 11 (2006): 1081–95. http://dx.doi.org/10.1139/y06-065.

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In mammalian eukaryotic cells, the Na+/H+ exchanger is a family of membrane proteins that regulates ions fluxes across membranes. Plasma membrane isoforms of this protein extrude 1 intracellular proton in exchange for 1 extracellular sodium. The family of Na+/H+ exchangers (NHEs) consists of 9 known isoforms, NHE1–NHE9. The NHE1 isoform was the first discovered, is the best characterized, and exists on the plasma membrane of all mammalian cells. It contains an N-terminal 500 amino acid membrane domain that transports ions, plus a 315 amino acid C-terminal, the intracellular regulatory domain.

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Wu, Si, Roslyn N. Brown, Samuel H. Payne, et al. "Top-Down Characterization of the Post-Translationally Modified Intact Periplasmic Proteome from the Bacterium Novosphingobium aromaticivorans." International Journal of Proteomics 2013 (March 10, 2013): 1–10. http://dx.doi.org/10.1155/2013/279590.

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The periplasm of Gram-negative bacteria is a dynamic and physiologically important subcellular compartment where the constant exposure to potential environmental insults amplifies the need for proper protein folding and modifications. Top-down proteomics analysis of the periplasmic fraction at the intact protein level provides unrestricted characterization and annotation of the periplasmic proteome, including the post-translational modifications (PTMs) on these proteins. Here, we used single-dimension ultra-high pressure liquid chromatography coupled with the Fourier transform mass spectrometr

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Bleve, Gianluca, Giuseppe Zacheo, Maria Stella Cappello, Franco Dellaglio, and Francesco Grieco. "Subcellular localization and functional expression of the glycerol uptake protein 1 (GUP1) of Saccharomyces cerevisiae tagged with green fluorescent protein." Biochemical Journal 390, no. 1 (2005): 145–55. http://dx.doi.org/10.1042/bj20042045.

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GFP (green fluorescent protein) from Aequorea victoria was used as an in vivo reporter protein when fused to the N- and C-termini of the glycerol uptake protein 1 (Gup1p) of Saccharomyces cerevisiae. The subcellular localization and functional expression of biologically active Gup1–GFP chimaeras was monitored by confocal laser scanning and electron microscopy, thus supplying the first study of GUP1 dynamics in live yeast cells. The Gup1p tagged with GFP is a functional glycerol transporter localized at the plasma membrane and endoplasmic reticulum levels of induced cells. The factors involved

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Reed, Brian D., Michael J. Meyer, Valentin Abramzon, et al. "Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device." Science 378, no. 6616 (2022): 186–92. http://dx.doi.org/10.1126/science.abo7651.

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Studies of the proteome would benefit greatly from methods to directly sequence and digitally quantify proteins and detect posttranslational modifications with single-molecule sensitivity. Here, we demonstrate single-molecule protein sequencing using a dynamic approach in which single peptides are probed in real time by a mixture of dye-labeled N-terminal amino acid recognizers and simultaneously cleaved by aminopeptidases. We annotate amino acids and identify the peptide sequence by measuring fluorescence intensity, lifetime, and binding kinetics on an integrated semiconductor chip. Our resul

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Sluzala, Zachary B., Angelina Hamati, and Patrice E. Fort. "Key Role of Phosphorylation in Small Heat Shock Protein Regulation via Oligomeric Disaggregation and Functional Activation." Cells 14, no. 2 (2025): 127. https://doi.org/10.3390/cells14020127.

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Heat shock proteins (HSPs) are essential molecular chaperones that protect cells by aiding in protein folding and preventing aggregation under stress conditions. Small heat shock proteins (sHSPs), which include members from HSPB1 to HSPB10, are particularly important for cellular stress responses. These proteins share a conserved α-crystallin domain (ACD) critical for their chaperone function, with flexible N- and C-terminal extensions that facilitate oligomer formation. Phosphorylation, a key post-translational modification (PTM), plays a dynamic role in regulating sHSP structure, oligomeric

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Kumar, Raj, and Iain J. McEwan. "Allosteric Modulators of Steroid Hormone Receptors: Structural Dynamics and Gene Regulation." Endocrine Reviews 33, no. 2 (2012): 271–99. http://dx.doi.org/10.1210/er.2011-1033.

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Steroid hormones are synthesized from cholesterol primarily in the adrenal gland and the gonads and play vital roles in normal physiology, the control of development, differentiation, metabolic homeostasis, and reproduction. The actions of these small lipophilic molecules are mediated by intracellular receptor proteins. It is just over 25 yr since the first cDNA for steroid receptors were cloned, a development that led to the birth of a superfamily of ligand-activated transcription factors: the nuclear receptors. The receptor proteins share structurally and functionally related ligand binding

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Zhu, Zheng, Hin Chu, Lei Wen, et al. "Targeting SUMO Modification of the Non-Structural Protein 5 of Zika Virus as a Host-Targeting Antiviral Strategy." International Journal of Molecular Sciences 20, no. 2 (2019): 392. http://dx.doi.org/10.3390/ijms20020392.

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Post-translational modifications of host or viral proteins are key strategies exploited by viruses to support virus replication and counteract host immune response. SUMOylation is a post-translational modification process mediated by a family of ubiquitin-like proteins called small ubiquitin-like modifier (SUMO) proteins. Multiple sequence alignment of 78 representative flaviviruses showed that most (72/78, 92.3%) have a putative SUMO-interacting motif (SIM) at their non-structural 5 (NS5) protein’s N-terminal domain. The putative SIM was highly conserved among 414 pre-epidemic and epidemic Zi

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Araki, S., K. Kaibuchi, T. Sasaki, Y. Hata, and Y. Takai. "Role of the C-terminal region of smg p25A in its interaction with membranes and the GDP/GTP exchange protein." Molecular and Cellular Biology 11, no. 3 (1991): 1438–47. http://dx.doi.org/10.1128/mcb.11.3.1438-1447.1991.

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smg p25A is a ras p21-like small GTP-binding protein which is implicated in the regulated secretory processes. We have recently found that bovine brain smg p25A is geranylgeranylated at its C-terminal region. In this study, we examined the function(s) of the C-terminal region of smg p25A. Limited proteolysis of bovine brain smg p25A with Achromobacter protease I produced an N-terminal fragment and a C-terminal tail. The Mrs of intact smg p25A, the N-terminal fragment, and the C-terminal tail were estimated to be about 24,000, 20,000, and less than 2,000, respectively, by sodium dodecyl sulfate

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