Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex

Lyumkis Dmitry; dos Passos Dario Oliveira; Tahara Erich B.Webb KristoforBennett Eric J.Vinterbo StaalPotter Clinton S.Carragher BridgetJoazeiro Claudio A. P.

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Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex

机译：Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex

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All organisms have evolved mechanisms to manage the stalling of ribosomes upon translation of aberrant mRNA. In eukaryotes, the large ribosomal subunit-associated quality control complex (RQC), composed of the listerin/Ltn1 E3 ubiquitin ligase and cofactors, mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. How RQC recognizes stalled ribosomes and performs its functions has not been understood. Using single-particle cryoelectron microscopy, we have determined the structure of the RQC complex bound to stalled 60S ribosomal subunits. The structure establishes how Ltn1 associates with the large ribosomal subunit and properly positions its E3-catalytic RING domain to mediate nascent chain ubiquitylation. The structure also reveals that a distinguishing feature of stalled 60S particles is an exposed, nascent chain-conjugated tRNA, and that the Tae2 subunit of RQC, which facilitates Ltn1 binding, is responsible for selective recognition of stalled 60S subunits. RQC components are engaged in interactions across a large span of the 60S subunit surface, connecting the tRNA in the peptidyl transferase center to the distally located nascent chain tunnel exit. This work provides insights into a mechanism linking translation and protein degradation that targets defective proteins immediately after synthesis, while ignoring nascent chains in normally translating ribosomes.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2014年第45期|15981-15986|共6页
作者
Lyumkis Dmitry; dos Passos Dario Oliveira; Tahara Erich B.Webb KristoforBennett Eric J.Vinterbo StaalPotter Clinton S.Carragher BridgetJoazeiro Claudio A. P.;
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作者单位

Scripps Res Inst, Dept Cell & Mol Biol, La Jolla, CA 92037 USA;

Scripps Res Inst, Natl Resource Automated Mol Microscopy, La Jolla, CA 92037 USA;

Univ Calif San Diego, Div Biol Sci, Sect Cell & Dev Biol, La Jolla, CA 92093 USAUniv Calif San Diego, Div Biomed Informat, La Jolla, CA 92093 USA;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Tae2/Nemf; translational surveillance; protein quality control; cryo-EM; listerin/Ltn1 E3 ubiquitin ligase;

Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex

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