N-terminal acetylation of cellular proteins creates specific degradation signals
SCIE
SCOPUS
- Title
- N-terminal acetylation of cellular proteins creates specific degradation signals
- Authors
- Hwang, CS; Shemorry, A; Varshavsky, A
- Date Issued
- 2010-02-19
- Publisher
- American Association for the Advancement of Science
- Abstract
- The retained N-terminal methionine (Met) residue of a nascent protein is often N-terminally acetylated (Nt-acetylated). Removal of N-terminal Met by Met-aminopeptidases frequently leads to Nt-acetylation of the resulting N-terminal alanine (Ala), valine (Val), serine (Ser), threonine (Thr), and cysteine (Cys) residues. Although a majority of eukaryotic proteins (for example, more than 80% of human proteins) are cotranslationally Nt-acetylated, the function of this extensively studied modification is largely unknown. Using the yeast Saccharomyces cerevisiae, we found that the Nt-acetylated Met residue could act as a degradation signal (degron), targeted by the Doa10 ubiquitin ligase. Moreover, Doa10 also recognized the Nt-acetylated Ala, Val, Ser, Thr, and Cys residues. Several examined proteins of diverse functions contained these N-terminal degrons, termed N-Ac-degrons, which are a prevalent class of degradation signals in cellular proteins.
- Keywords
- END RULE PATHWAY; UBIQUITIN LIGASE; MAT-ALPHA-2 REPRESSOR; YEAST; ACETYLTRANSFERASE; PROTEOMICS; RETICULUM; MEMBRANE; SENSOR; GENES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/25000
- DOI
- 10.1126/SCIENCE.1183147
- ISSN
- 0036-8075
- Article Type
- Article
- Citation
- SCIENCE, vol. 327, no. 5968, page. 973 - 977, 2010-02-19
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- There are no files associated with this item.
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