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

Liming Chen, Denise Muhlrad, Vasili Hauryliuk, Zhihong Cheng, Meng Kiat Lim, Viktoriya Shyp, Roy Parker, Haiwei Song

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

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.

Originalspråkengelska
Sidor (från-till)1233-1240
TidskriftNature Structural and Molecular Biology
Volym17
Nummer10
DOI
StatusPublished - 2010 okt.
Externt publiceradJa

Bibliografisk information

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.

Ämnesklassifikation (UKÄ)

  • Biokemi och molekylärbiologi

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