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Structure of the Dom34-Hbs1 complex and implications for no-go decay

Chen, Liming ; Muhlrad, Denise ; Hauryliuk, Vasili LU orcid ; Cheng, Zhihong ; Lim, Meng Kiat ; Shyp, Viktoriya ; Parker, Roy and Song, Haiwei (2010) In Nature Structural and Molecular Biology 17(10). p.1233-1240
Abstract

No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions... (More)

No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions to terminate translation and thereby commit mRNAs to NGD. Consistent with this role, NGD at runs of arginine codons, which cause a strong block to elongation, is independent of the Dom34-Hbs1 complex.

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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Nature Structural and Molecular Biology
volume
17
issue
10
pages
1233 - 1240
publisher
Nature Publishing Group
external identifiers
  • scopus:77957801203
  • pmid:20890290
ISSN
1545-9993
DOI
10.1038/nsmb.1922
language
English
LU publication?
no
additional info
Funding Information: We would like to thank the beamline scientists at ID23-1 (European Synchrotron Radiation Facility (ESRF), France) for assistance and access to synchrotron radiation facilities. This work is financially supported by the Biomedical Research Council of A*STAR (Agency for Science, Technology and Research) (H.S.), European Regional Development Fund through the Center of Excellence in Chemical Biology (V.H.) and by the Howard Hughes Medical Institute (R.P.). Copyright: Copyright 2010 Elsevier B.V., All rights reserved.
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eeb1b171-b105-4c5c-8d52-93b1ab648004
date added to LUP
2021-09-24 20:47:57
date last changed
2024-06-15 17:20:25
@article{eeb1b171-b105-4c5c-8d52-93b1ab648004,
  abstract     = {{<p>No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions to terminate translation and thereby commit mRNAs to NGD. Consistent with this role, NGD at runs of arginine codons, which cause a strong block to elongation, is independent of the Dom34-Hbs1 complex.</p>}},
  author       = {{Chen, Liming and Muhlrad, Denise and Hauryliuk, Vasili and Cheng, Zhihong and Lim, Meng Kiat and Shyp, Viktoriya and Parker, Roy and Song, Haiwei}},
  issn         = {{1545-9993}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{1233--1240}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Nature Structural and Molecular Biology}},
  title        = {{Structure of the Dom34-Hbs1 complex and implications for no-go decay}},
  url          = {{http://dx.doi.org/10.1038/nsmb.1922}},
  doi          = {{10.1038/nsmb.1922}},
  volume       = {{17}},
  year         = {{2010}},
}