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TitleProtein synthesis. Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains.
Journal, issue, pagesScience, Vol. 347, Issue 6217, Page 75-78, Year 2015
Publish dateJan 2, 2015
AuthorsPeter S Shen / Joseph Park / Yidan Qin / Xueming Li / Krishna Parsawar / Matthew H Larson / James Cox / Yifan Cheng / Alan M Lambowitz / Jonathan S Weissman / Onn Brandman / Adam Frost /
PubMed AbstractIn 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 ...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").
External linksScience / PubMed:25554787 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 8.4 Å
Structure data

EMDB-2811:
Electron cryo-microscopy of yeast 60S ribosome
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-2812:
Electron cryo-microscopy of Rqc2 bound to yeast 60S ribosome
Method: EM (single particle) / Resolution: 5.0 Å

EMDB-6169:
Electron cryo-microscopy of Rqc2 bound to yeast 60S ribosome, Rqc2-focused alignment
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-6170:
Electron cryo-microscopy of Ltn1, Rqc2 bound to yeast 60S ribosome
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-6171:
Electron cryo-microscopy of peptidyl-tRNA bound to yeast 60S ribosome
Method: EM (single particle) / Resolution: 5.9 Å

EMDB-6172:
Electron cryo-microscopy of Tif6p bound to peptidyl-tRNA-60S ribosomes
Method: EM (single particle) / Resolution: 5.4 Å

EMDB-6173:
Electron cryo-microscopy of peptidyl-(~A/P)tRNA-60S particles, ES27out
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-6174:
Electron cryo-microscopy of peptidyl-(~A/P)tRNA-60S particles, ES27in
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-6175:
Electron cryo-microscopy of peptidyl-(~E and ~P/E)tRNA-60S particles, L1 closed
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-6176:
Electron cryo-microscopy of RQC particles purified from Rqc2-deletion yeast strain
Method: EM (single particle) / Resolution: 8.4 Å

EMDB-6201:
Electron cryo-microscopy of peptidyl-tRNA bound to yeast 60S ribosome
Method: EM (single particle) / Resolution: 4.1 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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