Structure of the Dom34-Hbs1 complex and implications for no-go decay
(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
- Chen, Liming ; Muhlrad, Denise ; Hauryliuk, Vasili LU ; Cheng, Zhihong ; Lim, Meng Kiat ; Shyp, Viktoriya ; Parker, Roy and Song, Haiwei
- publishing date
- 2010-10
- 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.
- id
- 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}}, }