期刊
CELL
卷 156, 期 1-2, 页码 158-169出版社
CELL PRESS
DOI: 10.1016/j.cell.2013.11.031
关键词
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资金
- National Research Foundation (NRF) of the Korea government (MSIP) [NRF-2011-0021975, NRF-2012R1A4A1028200]
- Korean Healthcare Technology R&D Project of the Ministry of Health Welfare [HI11C1279]
- T.J. Park Science Fellowship of POSCO T.J. Park Foundation
- U.S. National Institutes of Health [DK039520, GM031530]
- Korean Government's NRF-2013-Global Ph.D. Fellowship Program [NRF-2013H1A2A1033225]
- BK21 PLUS Program
- National Research Foundation of Korea [2011-0021975, 2012R1A4A1028200, 21A20131212415] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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.
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