期刊
SCIENCE
卷 347, 期 6217, 页码 75-78出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1259724
关键词
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资金
- Searle Scholars Program
- Stanford University
- NIH [1DP2GM110772-01, GM37949, GM37951]
- Center for RNA Systems Biology [P50 GM102706, U01 GM098254]
- Howard Hughes Medical Institute
- Direct For Computer & Info Scie & Enginr
- Office of Advanced Cyberinfrastructure (OAC) [1341935] Funding Source: National Science Foundation
In Eukarya, stalled translation induces 40S dissociation and recruitment of the ribosome quality control complex (RQC) to the 60S subunit, which mediates nascent chain degradation. Here we report cryo-electron microscopy structures revealing that the RQC components Rqc2p (YPL009C/Tae2) and Ltn1p (YMR247C/Rkr1) bind to the 60S subunit at sites exposed after 40S dissociation, placing the Ltn1p RING (Really Interesting New Gene) domain near the exit channel and Rqc2p over the P-site transfer RNA (tRNA). We further demonstrate that Rqc2p recruits alanine-and threonine-charged tRNA to the A site and directs the elongation of nascent chains independently of mRNA or 40S subunits. Our work uncovers an unexpected mechanism of protein synthesis, in which a protein-not an mRNA-determines tRNA recruitment and the tagging of nascent chains with carboxy-terminal Ala and Thr extensions (CAT tails).
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