期刊
PROTEOMICS
卷 15, 期 14, 页码 2385-2401出版社
WILEY
DOI: 10.1002/pmic.201400619
关键词
alpha-amino group; Acetylation; Cell biology; N-terminal; Protein modification; Substrate specificity
资金
- Research Council of Norway [197136, 230865]
- Norwegian Cancer Society
- Bergen Research Foundation (BFS)
- Western Norway Regional Health Authority
- Meltzer Research Fund
The vast majority of eukaryotic proteins are N-terminally modified by one or more processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include different peptidases, transferases, and ligases. Methionine aminopeptidases excise the initiator methionine leaving the nascent polypeptide with a newly exposed amino acid that may be further modified. N-terminal acetyl-, methyl-, myristoyl-, and palmitoyltransferases may attach an acetyl, methyl, myristoyl, or palmitoyl group, respectively, to the -amino group of the target protein N-terminus. With the action of ubiquitin ligases, one or several ubiquitin molecules are transferred, and hence, constitute the N-terminal modification. Modifications at protein N-termini represent an important contribution to proteomic diversity and complexity, and are essential for protein regulation and cellular signaling. Consequently, dysregulation of the N-terminal modifying enzymes is implicated in human diseases. We here review the different protein N-terminal modifications occurring co- or post-translationally with emphasis on the responsible enzymes and their substrate specificities.
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