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Journal Title:

Nucleic Acids Research

Volume:

Volume 44, Number 14

Publisher:

Oxford University Press OUP | 2016-08-19, Pages 6840-6852

Type of Work:

Article | Final Publisher PDF

Abstract: Cotranslational degradation of polypeptide nascent chains plays a critical role in quality control of protein synthesis and the rescue of stalled ribosomes. In eukaryotes, ribosome stalling triggers release of 60S subunits with attached nascent polypeptides, which undergo ubiquitination by the E3 ligase Ltn1 and proteasomal degradation facilitated by the ATPase Cdc48. However, the identity of factors acting upstream in this process is less clear. Here, we examined how the canonical release factors Sup45-Sup35 eRF1-eRF3 and their paralogs Dom34-Hbs1 affect the total population of ubiquitinated nascent chains associated with yeast ribosomes. We found that the availability of the functional release factor complex Sup45-Sup35 strongly influences the amount of ubiquitinated polypeptides associated with 60S ribosomal subunits, while Dom34-Hbs1 generate 60S-associated peptidyl-tRNAs that constitute a relatively minor fraction of Ltn1 substrates. These results uncover two separate pathways that target nascent polypeptides for Ltn1-Cdc48-mediated degradation and suggest that in addition to canonical termination on stop codons, eukaryotic release factors contribute to cotranslational protein quality control.

Subjects: Biology, Cell - Chemistry, Biochemistry - Research Funding: UMDNJ Foundation to N.S.; National Institutes of Health GM093294 to T.A.C. and GM074091 to D.G.P.; National Science Foundation MCB-1516872 to Y.O.C



Funding for open access charge: Rowan University intramural support funds to N.S



Keywords: Science and Technology - Life Sciences and Biomedicine - Biochemistry and Molecular Biology - YEAST SACCHAROMYCES-CEREVISIAE - CHAIN RELEASE FACTORS - PEPTIDYL-TRANSFER-RNA - E3 UBIQUITIN LIGASE - NO-GO DECAY - MESSENGER-RNA - STRUCTURAL BASIS - CONTROL COMPLEX - HYGROMYCIN-B - COTRANSLATIONAL UBIQUITINATION -



Autor: Natalia Shcherbik, Tatiana Chernova, Yury O. Chernoff, Dimitri G. Pestov,

Fuente: https://open.library.emory.edu/



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