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Protein alpha-N-acetylation studied by N-terminomics

Petra Van Damme UGent, Thomas Arnesen and Kris Gevaert UGent (2011) FEBS JOURNAL. 278(20). p.3822-3834
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
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
journal title
FEBS JOURNAL
FEBS J.
volume
278
issue
20
pages
3822 - 3834
Web of Science type
Review
Web of Science id
000295335500005
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
3.79 (2011)
JCR rank
89/286 (2011)
JCR quartile
2 (2011)
ISSN
1742-464X
DOI
10.1111/j.1742-4658.2011.08230.x
project
Bioinformatics: from nucleotids to networks (N2N)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1978415
handle
http://hdl.handle.net/1854/LU-1978415
date created
2012-01-04 16:20:26
date last changed
2016-12-19 15:45:28
@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},
}

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.