期刊
FEBS JOURNAL
卷 278, 期 20, 页码 3822-3834出版社
WILEY
DOI: 10.1111/j.1742-4658.2011.08230.x
关键词
acetyl-coenzyme A; (alternative) translation initiation sites; alpha-N-acetylation; combined fractional diagonal chromatography; cotranslational modification; N-acetylome; N-terminal acetyltransferase; N-terminomics; positional proteomics; protein N-termini
资金
- Fund for Scientific Research-Flanders (Belgium) [G.0042.07, G.0440,10]
- Ghent University [BOF07/GOA/012]
- Inter University Attraction Poles [IUAP06]
- Norwegian Research Council [197136]
- Norwegian Cancer Society
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.
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