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

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 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.

journal_name

Nat Struct Mol Biol

authors

Chen L,Muhlrad D,Hauryliuk V,Cheng Z,Lim MK,Shyp V,Parker R,Song H

doi

10.1038/nsmb.1922

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

1233-40

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb.1922

journal_volume

17

pub_type

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