The N-terminal methionine of cellular proteins as a degradation signal
SCIE
SCOPUS
- Title
- The N-terminal methionine of cellular proteins as a degradation signal
- Authors
- Kim, HK; Kim, RR; Oh, JH; Cho, H; Varshavsky, A; Hwang, CS
- Date Issued
- 2014-01-16
- Publisher
- Cell Press
- Abstract
- The Arg/N-end rule pathway targets for degradation proteins that bear specific unacetylated N-terminal residues while the Ac/N-end rule pathway targets proteins through their N-infinity-terminally acetylated (Nt-acetylated) residues. Here, we show that Ubr1, the ubiquitin ligase of the Arg/N-end rule pathway, recognizes unacetylated N-terminal methionine if it is followed by a hydrophobic residue. This capability of Ubr1 expands the range of substrates that can be targeted for degradation by the Arg/N-end rule pathway because virtually all nascent cellular proteins bear N-terminal methionine. We identified Msn4, Sry1, Arl3, and Pre5 as examples of normal or misfolded proteins that can be destroyed through the recognition of their unacetylated N-terminal methionine. Inasmuch as proteins bearing the Nt-acetylated N-terminal methionine residue are substrates of the Ac/N-end rule pathway, the resulting complementarity of the Arg/N-end rule and Ac/N-end rule pathways enables the elimination of protein substrates regardless of acetylation state of N-terminal methionine in these substrates.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/14996
- DOI
- 10.1016/J.CELL.2013.11.031
- ISSN
- 0092-8674
- Article Type
- Article
- Citation
- Cell, vol. 156, no. 1-2, page. 158 - 169, 2014-01-16
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