Abstract:
:Ribosome recycling usually occurs after canonical termination triggered by a stop codon. Additionally, ribosomes that are stalled by aberrant mRNAs need to be recognized and subsequently recycled. In eukaryotes and archaea, the factors involved in canonical termination and ribosome rescue are structurally and functionally related. Both termination and ribosome rescue are mediated by class I release factors (eRF1/aRF1 in eukaryotic/archaeal termination) or their paralogs (Pelota/aPelota for ribosome rescue) and homologs of translational GTPases (eRF3/aEF1α in termination, Hbs1/aEF1α in ribosome rescue). These events are followed by recycling of the ribosome. Recently the ATPase ABCE1 was shown to be the main ribosome recycling factor. In concert with eRF1 or Pelota, ABCE1 dissociates the ribosome into subunits. During the past two years, several structures of ribosome rescue and ribosome recycling complexes have been solved by cryo-electron microscopy and crystallography. These structures along with recent functional data make it possible to propose a molecular model of these late translation events in termination and recycling.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Franckenberg S,Becker T,Beckmann Rdoi
10.1016/j.sbi.2012.08.002subject
Has Abstractpub_date
2012-12-01 00:00:00pages
786-96issue
6eissn
0959-440Xissn
1879-033Xpii
S0959-440X(12)00132-7journal_volume
22pub_type
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
doi:10.1016/j.sbi.2020.10.005
更新日期:2020-10-27 00:00:00
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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更新日期:2017-02-01 00:00:00
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
doi:10.1016/j.sbi.2006.10.003
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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journal_title:Current opinion in structural biology
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abstract::Transmembrane helix-helix interactions mediate the folding and assembly of membrane proteins. Recognition motifs range from GxxxG and leucine zippers to polar side chains and salt bridges. Some canonical membrane proteins contain local charge clusters that are important for folding and function, and which have to be c...
journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
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journal_title:Current opinion in structural biology
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doi:10.1016/j.sbi.2005.08.010
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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abstract::Among the crystal structures of lectins determined recently, three--snowdrop lectin, jacalin and amaranthin--represent new lectin families. Their polypeptide folds share remarkably similar features and consist exclusively of beta structure. Autonomously folded beta-sheet subdomains, inter-related by a pseudothreefold ...
journal_title:Current opinion in structural biology
pub_type: 杂志文章,评审
doi:10.1016/s0959-440x(97)80071-1
更新日期:1997-10-01 00:00:00