Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome

被引：134

作者：

Becker, Thomas ^{[1
,2
]}

Armache, Jean-Paul ^{[1
,2
]}

Jarasch, Alexander ^{[1
,2
]}

Anger, Andreas M. ^{[1
,2
]}

Villa, Elizabeth ^{[3
]}

Sieber, Heidemarie ^{[1
,2
]}

Motaal, Basma Abdel ^{[1
,2
]}

Mielke, Thorsten ^{[4
,5
]}

Berninghausen, Otto ^{[1
,2
]}

Beckmann, Roland ^{[1
,2
]}

机构：

[1] Univ Munich, Gene Ctr, Munich, Germany

[2] Univ Munich, Dept Biochem, Ctr Integrated Prot Sci Munich, Munich, Germany

[3] Max Planck Inst Biochem, Dept Biol Struct, D-82152 Martinsried, Germany

[4] Max Planck Inst Mol Genet, UltraStrukturNetzwerk, Berlin, Germany

[5] Charite, Inst Med Phys & Biophys, D-13353 Berlin, Germany

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 06期

关键词：

TERMINATION FACTOR ERF1; STOP CODON RECOGNITION; RELEASE FACTOR ERF3; CRYSTAL-STRUCTURE; ELECTRON-MICROSCOPY; CRYO-EM; SACCHAROMYCES-CEREVISIAE; EUKARYOTIC RIBOSOME; ESCHERICHIA-COLI; EF-TU;

D O I：

10.1038/nsmb.2057

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.

引用

页码：715 / U116

页数：7

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