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 Bioljournal_title
Nature structural & molecular biologyauthors
Chen L,Muhlrad D,Hauryliuk V,Cheng Z,Lim MK,Shyp V,Parker R,Song Hdoi
10.1038/nsmb.1922subject
Has Abstractpub_date
2010-10-01 00:00:00pages
1233-40issue
10eissn
1545-9993issn
1545-9985pii
nsmb.1922journal_volume
17pub_type
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