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

Caillan Crowe-McAuliffe; Hiraku Takada; Victoriia Murina; Christine Polte; Sergo Kasvandik; Tanel Tenson; Zoya Ignatova; Gemma C. Atkinson; Daniel N. Wilson; Vasili Hauryliuk

doi:10.1016/j.molcel.2020.11.002

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

Caillan Crowe-McAuliffe, Hiraku Takada, Victoriia Murina, Christine Polte, Sergo Kasvandik, Tanel Tenson, Zoya Ignatova, Gemma C. Atkinson, Daniel N. Wilson, Vasili Hauryliuk

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	115-126
Journal	Molecular Cell
Volume	81
Issue number	1
DOIs	https://doi.org/10.1016/j.molcel.2020.11.002
Publication status	Published - 2021
Externally published	Yes

Bibliographical note

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.

Free keywords

Hsp15
NEMF
polyalanine tailing
ribosome
RQC
RqcH
RqcP
tRNA movement
YabO

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10.1016/j.molcel.2020.11.002

Cite this

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title = "Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP",

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.",

keywords = "Hsp15, NEMF, polyalanine tailing, ribosome, RQC, RqcH, RqcP, tRNA movement, YabO",

author = "Caillan Crowe-McAuliffe and Hiraku Takada and Victoriia Murina and Christine Polte and Sergo Kasvandik and Tanel Tenson and Zoya Ignatova and Atkinson, {Gemma C.} and Wilson, {Daniel N.} and Vasili Hauryliuk",

note = "Funding Information: We thank Michael Hall for help with cryo-EM data collection. The EM data were collected at the Ume{\aa} 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{\aa} University. This research was supported by grants from the Deutsche Forschungsgemeinschaft ( WI3285/8-1 to D.N.W.), the Swedish Research Council (Vetenskapsr{\aa}det) ( 2017-03783 to V.H. and 2019-01085 to G.C.A.), and Ragnar S{\"o}derbergs stiftelse (to V.H.); a postdoctoral grant from the Ume{\aa} 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{\"u}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. 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: {\textcopyright} 2020 Elsevier Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",

year = "2021",

doi = "10.1016/j.molcel.2020.11.002",

language = "English",

volume = "81",

pages = "115--126",

journal = "Molecular Cell",

issn = "1097-2765",

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T1 - Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP

AU - Crowe-McAuliffe, Caillan

AU - Takada, Hiraku

AU - Murina, Victoriia

AU - Polte, Christine

AU - Kasvandik, Sergo

AU - Tenson, Tanel

AU - Ignatova, Zoya

AU - Atkinson, Gemma C.

AU - Wilson, Daniel N.

AU - Hauryliuk, Vasili

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PY - 2021

Y1 - 2021

N2 - 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.

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KW - Hsp15

KW - NEMF

KW - polyalanine tailing

KW - ribosome

KW - RQC

KW - RqcH

KW - RqcP

KW - tRNA movement

KW - YabO

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SN - 1097-2765

VL - 81

SP - 115

EP - 126

JO - Molecular Cell

JF - Molecular Cell

IS - 1

ER -

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

Abstract

Bibliographical note

Free keywords

Access to Document

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