Rqc2p and 60 S ribosomal subunits mediate mRNA-independent elongation of nascent chains-Reference-Cited by-同舟云学术

Rqc2p and 60 S ribosomal subunits mediate mRNA-independent elongation of nascent chains

Published:2015-01-02 Issue:6217 Volume:347 Page:75-78
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Shen Peter S.¹,Park Joseph²,Qin Yidan³⁴,Li Xueming⁵,Parsawar Krishna⁶,Larson Matthew H.⁷⁸⁹¹⁰,Cox James¹⁶,Cheng Yifan⁵,Lambowitz Alan M.³⁴,Weissman Jonathan S.⁷⁸⁹¹⁰,Brandman Onn²,Frost Adam¹⁵

Affiliation:

1. Department of Biochemistry, University of Utah, UT 84112, USA.

2. Department of Biochemistry, Stanford University, Palo Alto, CA 94305, USA.

3. Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.

4. Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.

5. Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.

6. Mass Spectrometry and Proteomics Core Facility, University of Utah, UT 84112, USA.

7. Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.

8. Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158, USA.

9. California Institute for Quantitative Biomedical Research, University of California, San Francisco, San Francisco, CA 94158, USA.

10. Center for RNA Systems Biology, University of California, San Francisco, San Francisco, CA 94158, USA.

Abstract

Tagging truncated proteins with CAT tails During the translation of a messenger RNA (mRNA) into protein, ribosomes can sometimes stall. Truncated proteins thus formed can be toxic to the cell and must be destroyed. Shen et al. show that the proteins Ltn1p and Rqc2p, subunits of the ribosome quality control complex, bind to the stalled and partially disassembled ribosome. Ltn1p, a ubiquitin ligase, binds near the nascent polypeptide exit tunnel on the ribosome, well placed to tag the truncated protein for destruction. The Rqc2p protein interacts with the transfer RNA binding sites on the partial ribosome and recruits alanine- and threonine-bearing tRNAs. Rqc2p then catalyzes the addition of these amino acids onto the unfinished protein, in the absence of both the fully assembled ribosome and mRNA. These so-called CAT tails may promote the heat shock response, which helps buffer against malformed proteins. Science , this issue p. 75

Funder

NIH

Howard Hughes Medical Institute

Stanford University

Searle Scholars Program

Center for RNA Systems Biology

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference41 articles.

1. A Ribosome-Bound Quality Control Complex Triggers Degradation of Nascent Peptides and Signals Translation Stress