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The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAArg and tRNALys isoacceptors in the P site

Turnbull, Kathryn ; Paternoga, Helge ; von der Weth, Esther ; Egorov, Artyom A LU orcid ; Pochopien, Agnieszka A ; Zhang, Yujie ; Nersisyan, Lilit ; Margus, Tõnu ; Johansson, Marcus J O LU and Pelechano, Vicent , et al. (2024) In Nucleic Acids Research p.1-16
Abstract

The efficiency of translation termination is determined by the nature of the stop codon as well as its context. In eukaryotes, recognition of the A-site stop codon and release of the polypeptide are mediated by release factors eRF1 and eRF3, respectively. Translation termination is modulated by other factors which either directly interact with release factors or bind to the E-site and modulate the activity of the peptidyl transferase center. Previous studies suggested that the Saccharomyces cerevisiae ABCF ATPase New1 is involved in translation termination and/or ribosome recycling, however, the exact function remained unclear. Here, we have applied 5PSeq, single-particle cryo-EM and readthrough reporter assays to provide insight into... (More)

The efficiency of translation termination is determined by the nature of the stop codon as well as its context. In eukaryotes, recognition of the A-site stop codon and release of the polypeptide are mediated by release factors eRF1 and eRF3, respectively. Translation termination is modulated by other factors which either directly interact with release factors or bind to the E-site and modulate the activity of the peptidyl transferase center. Previous studies suggested that the Saccharomyces cerevisiae ABCF ATPase New1 is involved in translation termination and/or ribosome recycling, however, the exact function remained unclear. Here, we have applied 5PSeq, single-particle cryo-EM and readthrough reporter assays to provide insight into the biological function of New1. We show that the lack of New1 results in ribosomal stalling at stop codons preceded by a lysine or arginine codon and that the stalling is not defined by the nature of the C-terminal amino acid but rather by the identity of the tRNA isoacceptor in the P-site. Collectively, our results suggest that translation termination is inefficient when ribosomes have specific tRNA isoacceptors in the P-site and that the recruitment of New1 rescues ribosomes at these problematic termination contexts.

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organization
publishing date
type
Contribution to journal
publication status
epub
subject
in
Nucleic Acids Research
pages
1 - 16
publisher
Oxford University Press
external identifiers
  • pmid:39217469
ISSN
1362-4962
DOI
10.1093/nar/gkae748
language
English
LU publication?
yes
additional info
© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.
id
a3f696ed-74d2-403e-b4ba-0c75251d9063
date added to LUP
2024-09-02 06:33:53
date last changed
2024-09-02 08:39:19
@article{a3f696ed-74d2-403e-b4ba-0c75251d9063,
  abstract     = {{<p>The efficiency of translation termination is determined by the nature of the stop codon as well as its context. In eukaryotes, recognition of the A-site stop codon and release of the polypeptide are mediated by release factors eRF1 and eRF3, respectively. Translation termination is modulated by other factors which either directly interact with release factors or bind to the E-site and modulate the activity of the peptidyl transferase center. Previous studies suggested that the Saccharomyces cerevisiae ABCF ATPase New1 is involved in translation termination and/or ribosome recycling, however, the exact function remained unclear. Here, we have applied 5PSeq, single-particle cryo-EM and readthrough reporter assays to provide insight into the biological function of New1. We show that the lack of New1 results in ribosomal stalling at stop codons preceded by a lysine or arginine codon and that the stalling is not defined by the nature of the C-terminal amino acid but rather by the identity of the tRNA isoacceptor in the P-site. Collectively, our results suggest that translation termination is inefficient when ribosomes have specific tRNA isoacceptors in the P-site and that the recruitment of New1 rescues ribosomes at these problematic termination contexts.</p>}},
  author       = {{Turnbull, Kathryn and Paternoga, Helge and von der Weth, Esther and Egorov, Artyom A and Pochopien, Agnieszka A and Zhang, Yujie and Nersisyan, Lilit and Margus, Tõnu and Johansson, Marcus J O and Pelechano, Vicent and Wilson, Daniel N and Hauryliuk, Vasili}},
  issn         = {{1362-4962}},
  language     = {{eng}},
  month        = {{09}},
  pages        = {{1--16}},
  publisher    = {{Oxford University Press}},
  series       = {{Nucleic Acids Research}},
  title        = {{The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAArg and tRNALys isoacceptors in the P site}},
  url          = {{http://dx.doi.org/10.1093/nar/gkae748}},
  doi          = {{10.1093/nar/gkae748}},
  year         = {{2024}},
}