Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP

Crowe-McAuliffe, Caillan ; Takada, Hiraku ; Murina, Victoriia ; Polte, Christine ; Kasvandik, Sergo ; Tenson, Tanel ; Ignatova, Zoya ; Atkinson, Gemma C. LU ; Wilson, Daniel N. and Hauryliuk, Vasili LU orcid (2021) In Molecular Cell 81(1). p.115-126
Abstract

Crowe-McAuliffe et al. present cryo-EM structures of native ribosome-associated quality control complexes from Bacillus subtilis, revealing how RqcH cooperates with RqcP/YabO to mediate protein synthesis on the large 50S subunit in the absence of the translocase EF-G, mRNA, and the small 30S subunit.

Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Hsp15, NEMF, polyalanine tailing, ribosome, RQC, RqcH, RqcP, tRNA movement, YabO
in
Molecular Cell
volume
81
issue
1
pages
115 - 126
publisher
Cell Press
external identifiers
  • scopus:85097878793
  • pmid:33259810
ISSN
1097-2765
DOI
10.1016/j.molcel.2020.11.002
language
English
LU publication?
no
additional info
Funding Information: We thank Michael Hall for help with cryo-EM data collection. The EM data were collected at the Umeå Core Facility for Electron Microscopy, a node of the Cryo-EM Swedish National Facility, funded by the Knut and Alice Wallenberg , Family Erling Persson , and Kempe Foundations ; SciLifeLab; Stockholm University; and Umeå University. This research was supported by grants from the Deutsche Forschungsgemeinschaft ( WI3285/8-1 to D.N.W.), the Swedish Research Council (Vetenskapsrådet) ( 2017-03783 to V.H. and 2019-01085 to G.C.A.), and Ragnar Söderbergs stiftelse (to V.H.); a postdoctoral grant from the Umeå Centre for Microbial Research (UCMR; to H.T.); the European Union from the European Regional Development Fund through the Centre of Excellence in Molecular Cell Engineering ( 2014-2020.4.01.15-0013 to T.T. and V.H.); and the Estonian Research Council ( PRG335 to T.T. and V.H.). The D.N.W. and V.H. groups are also supported by the Deutsche Zentrum für Luft- und Raumfahrt ( DLR01Kl1820 to D.N.W.) and the Swedish Research Council ( 2018-00956 to V.H.) within the RIBOTARGET consortium under the framework of JPIAMR. Funding Information: We thank Michael Hall for help with cryo-EM data collection. The EM data were collected at the Ume? Core Facility for Electron Microscopy, a node of the Cryo-EM Swedish National Facility, funded by the Knut and Alice Wallenberg, Family Erling Persson, and Kempe Foundations; SciLifeLab; Stockholm University; and Ume? University. This research was supported by grants from the Deutsche Forschungsgemeinschaft (WI3285/8-1 to D.N.W.), the Swedish Research Council (Vetenskapsr?det) (2017-03783 to V.H. and 2019-01085 to G.C.A.), and Ragnar S?derbergs stiftelse (to V.H.); a postdoctoral grant from the Ume? Centre for Microbial Research (UCMR; to H.T.); the European Union from the European Regional Development Fund through the Centre of Excellence in Molecular Cell Engineering (2014-2020.4.01.15-0013 to T.T. and V.H.); and the Estonian Research Council (PRG335 to T.T. and V.H.). The D.N.W. and V.H. groups are also supported by the Deutsche Zentrum f?r Luft- und Raumfahrt (DLR01Kl1820 to D.N.W.) and the Swedish Research Council (2018-00956 to V.H.) within the RIBOTARGET consortium under the framework of JPIAMR. D.N.W. and V.H. designed the study. H.T. and V.M. prepared the cryo-EM samples. H.T. performed biochemical and genetic studies. C.C.-M. processed the cryo-EM data and built and refined the molecular models. S.K. and T.T. performed the mass spectrometry analysis. G.C.A. performed sequence and phylogenetic analysis. C.P and Z.I. performed the tRNA microarray analysis. All authors interpreted the results and helped D.N.W. and C.C.-M. write the paper. The authors declare no competing interests. Publisher Copyright: © 2020 Elsevier Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.
id
801debf3-d435-4593-a8b8-cf797cef4216
date added to LUP
2021-09-24 20:30:36
date last changed
2024-06-15 16:52:08
@article{801debf3-d435-4593-a8b8-cf797cef4216,
  abstract     = {{<p>Crowe-McAuliffe et al. present cryo-EM structures of native ribosome-associated quality control complexes from Bacillus subtilis, revealing how RqcH cooperates with RqcP/YabO to mediate protein synthesis on the large 50S subunit in the absence of the translocase EF-G, mRNA, and the small 30S subunit.</p>}},
  author       = {{Crowe-McAuliffe, Caillan and Takada, Hiraku and Murina, Victoriia and Polte, Christine and Kasvandik, Sergo and Tenson, Tanel and Ignatova, Zoya and Atkinson, Gemma C. and Wilson, Daniel N. and Hauryliuk, Vasili}},
  issn         = {{1097-2765}},
  keywords     = {{Hsp15; NEMF; polyalanine tailing; ribosome; RQC; RqcH; RqcP; tRNA movement; YabO}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{115--126}},
  publisher    = {{Cell Press}},
  series       = {{Molecular Cell}},
  title        = {{Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP}},
  url          = {{http://dx.doi.org/10.1016/j.molcel.2020.11.002}},
  doi          = {{10.1016/j.molcel.2020.11.002}},
  volume       = {{81}},
  year         = {{2021}},
}