Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue

Franckenberg, Sibylle; Becker, Thomas; Beckmann, Roland

doi:10.1016/j.sbi.2012.08.002

Cited by 38 publications

(24 citation statements)

References 49 publications

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“…7A). eRF1 in its catalytically active state has been proposed to adopt a similar conformation as its homolog Dom34 within the Dom34/Rli1 complex involved in mRNA decay (Franckenberg et al, 2012). Indeed, both factors adopt a similar but not identical orientation.…”

Section: Resultsmentioning

confidence: 99%

Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES

et al. 2015

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Summary The Cricket paralysis virus (CrPV) uses an internal ribosomal entry site (IRES) to hijack the ribosome. In a remarkable RNA-based mechanism involving neither initiation factor nor initiator tRNA, the CrPV IRES jump starts translation in the elongation phase from the ribosomal A-site. Here we present cryo-EM maps of 80S•CrPV-STOP•eRF1•eRF3•GMPPNP and 80S•CrPV-STOP•eRF1 complexes revealing a previously unseen binding state of the IRES and directly rationalizing that an eEF2-dependent translocation of the IRES is required to allow the first A-site occupation. During this unusual translocation event the IRES undergoes a pronounced conformational change to a more stretched conformation. At the same time our structural analysis provides information about the binding modes of eRF1•eRF3•GMPPNP and eRF1 in a minimal system. It shows that neither eRF3 nor ABCE1 are required for the active conformation of eRF1 at the intersection between eukaryotic termination and recycling.

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Section: Resultsmentioning

confidence: 99%

Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES

et al. 2015

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“…If a ribosome reaches an in-frame stop codon, the essential translation termination factor eRF3-eRF1 (Sup35-Sup45 in yeast) binds and induces hydrolytic cleavage of the peptidyl-tRNA at the ribosomal P-site (23)(24)(25). If a ribosome reaches the very 3= end of a stop codon-free mRNA, its P-site is occupied with a peptidyltRNA; however, the A-site is empty.…”

mentioning

confidence: 99%

Release Factor eRF3 Mediates Premature Translation Termination on Polylysine-Stalled Ribosomes in Saccharomyces cerevisiae

Chiabudini

Tais

Zhang

et al. 2014

Molecular and Cellular Biology

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bRibosome stalling is an important incident enabling the cellular quality control machinery to detect aberrant mRNA. Saccharomyces cerevisiae Hbs1-Dom34 and Ski7 are homologs of the canonical release factor eRF3-eRF1, which recognize stalled ribosomes, promote ribosome release, and induce the decay of aberrant mRNA. Polyadenylated nonstop mRNA encodes aberrant proteins containing C-terminal polylysine segments which cause ribosome stalling due to electrostatic interaction with the ribosomal exit tunnel. Here we describe a novel mechanism, termed premature translation termination, which releases C-terminally truncated translation products from ribosomes stalled on polylysine segments. Premature termination during polylysine synthesis was abolished when ribosome stalling was prevented due to the absence of the ribosomal protein Asc1. In contrast, premature termination was enhanced, when the general rate of translation elongation was lowered. The unconventional termination event was independent of Hbs1-Dom34 and Ski7, but it was dependent on eRF3. Moreover, premature termination during polylysine synthesis was strongly increased in the absence of the ribosome-bound chaperones ribosome-associated complex (RAC) and Ssb (Ssb1 and Ssb2). On the basis of the data, we suggest a model in which eRF3-eRF1 can catalyze the release of nascent polypeptides even though the ribosomal A-site contains a sense codon when the rate of translation is abnormally low.

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“…The current model for NSD suggests that the Dom34/Pelota:Hbs1 complex enters the empty A site of the ribosome that is stalled at the 3' end of nonstop mRNA, promotes the ribosome dissociation, enabling access of the Ski:Exosome exonuclease complex from the 3' end of nonstop mRNAs [5,15,16]. Several lines of in vivo and in vitro observations support this view.…”

Section: Introductionmentioning

confidence: 85%

A functional involvement of ABCE1, eukaryotic ribosome recycling factor, in nonstop mRNA decay in Drosophila melanogaster cells

et al. 2014

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Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue

Cited by 38 publications

References 49 publications

Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES

Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES

Release Factor eRF3 Mediates Premature Translation Termination on Polylysine-Stalled Ribosomes in Saccharomyces cerevisiae

A functional involvement of ABCE1, eukaryotic ribosome recycling factor, in nonstop mRNA decay in Drosophila melanogaster cells

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