Advanced search
1 file | 325.60 KB

Protein alpha-N-acetylation studied by N-terminomics

(2011) FEBS JOURNAL. 278(20). p.3822-3834
Author
Organization
Project
Bioinformatics: from nucleotids to networks (N2N)
Abstract
Cotranslational protein N-terminal modifications, including proteolytic maturation such as initiator methionine excision by methionine aminopeptidases and N-terminal blocking, occur universally. Protein alpha-N-acetylation, or the transfer of the acetyl moiety of acetyl-coenzyme A to nascent protein N-termini, catalysed by multisubunit N-terminal acetyltransferase complexes, generally takes place during protein translation. Nearly all protein modifications are known to influence different protein aspects such as folding, stability, activity and localization, and several studies have indicated similar functions for protein alpha-N-acetylation. However, until recently, protein alpha-N-acetylation remained poorly explored, mainly due to the absence of targeted proteomics technologies. The recent emergence of N-terminomics technologies that allow isolation of protein N-terminal peptides, together with proteogenomics efforts combining experimental and informational content have greatly boosted the field of alpha-N-acetylation. In this review, we report on such emerging technologies as well as on breakthroughs in our understanding of protein N-terminal biology.
Keywords
MESSENGER-RNA, POSTTRANSLATIONAL MODIFICATIONS, SACCHAROMYCES-CEREVISIAE, TRANSLATION INITIATION, ACETYLTRANSFERASE COMPLEX, TERMINAL ACETYLATION, INTEGRAL MEMBRANE-PROTEIN, ARF-LIKE GTPASE, protein N-termini, N-terminomics, positional proteomics, N-terminal acetyltransferase, N-acetylome, cotranslational modification, combined fractional diagonal chromatography, acetyl-coenzyme A, alpha-N-acetylation, (alternative) translation initiation sites, EVOLUTIONARY CONSERVATION, ARABIDOPSIS-THALIANA

Downloads

    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 325.60 KB

Citation

Please use this url to cite or link to this publication:

Chicago
Van Damme, Petra, Thomas Arnesen, and Kris Gevaert. 2011. “Protein alpha-N-acetylation Studied by N-terminomics.” Febs Journal 278 (20): 3822–3834.
APA
Van Damme, Petra, Arnesen, T., & Gevaert, K. (2011). Protein alpha-N-acetylation studied by N-terminomics. FEBS JOURNAL, 278(20), 3822–3834.
Vancouver
1.
Van Damme P, Arnesen T, Gevaert K. Protein alpha-N-acetylation studied by N-terminomics. FEBS JOURNAL. 2011;278(20):3822–34.
MLA
Van Damme, Petra, Thomas Arnesen, and Kris Gevaert. “Protein alpha-N-acetylation Studied by N-terminomics.” FEBS JOURNAL 278.20 (2011): 3822–3834. Print.
@article{1978415,
  abstract     = {Cotranslational protein N-terminal modifications, including proteolytic maturation such as initiator methionine excision by methionine aminopeptidases and N-terminal blocking, occur universally. Protein alpha-N-acetylation, or the transfer of the acetyl moiety of acetyl-coenzyme A to nascent protein N-termini, catalysed by multisubunit N-terminal acetyltransferase complexes, generally takes place during protein translation. Nearly all protein modifications are known to influence different protein aspects such as folding, stability, activity and localization, and several studies have indicated similar functions for protein alpha-N-acetylation. However, until recently, protein alpha-N-acetylation remained poorly explored, mainly due to the absence of targeted proteomics technologies. The recent emergence of N-terminomics technologies that allow isolation of protein N-terminal peptides, together with proteogenomics efforts combining experimental and informational content have greatly boosted the field of alpha-N-acetylation. In this review, we report on such emerging technologies as well as on breakthroughs in our understanding of protein N-terminal biology.},
  author       = {Van Damme, Petra and Arnesen, Thomas and Gevaert, Kris},
  issn         = {1742-464X},
  journal      = {FEBS JOURNAL},
  keyword      = {MESSENGER-RNA,POSTTRANSLATIONAL MODIFICATIONS,SACCHAROMYCES-CEREVISIAE,TRANSLATION INITIATION,ACETYLTRANSFERASE COMPLEX,TERMINAL ACETYLATION,INTEGRAL MEMBRANE-PROTEIN,ARF-LIKE GTPASE,protein N-termini,N-terminomics,positional proteomics,N-terminal acetyltransferase,N-acetylome,cotranslational modification,combined fractional diagonal chromatography,acetyl-coenzyme A,alpha-N-acetylation,(alternative) translation initiation sites,EVOLUTIONARY CONSERVATION,ARABIDOPSIS-THALIANA},
  language     = {eng},
  number       = {20},
  pages        = {3822--3834},
  title        = {Protein alpha-N-acetylation studied by N-terminomics},
  url          = {http://dx.doi.org/10.1111/j.1742-4658.2011.08230.x},
  volume       = {278},
  year         = {2011},
}

Altmetric
View in Altmetric
Web of Science
Times cited: