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A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling

Kasari, Villu ; Pochopien, Agnieszka A. ; Margus, Tõnu ; Murina, Victoriia ; Turnbull, Kathryn ; Zhou, Yang ; Nissan, Tracy ; Graf, Michael ; Nováček, Jiří and Atkinson, Gemma C. LU , et al. (2019) In Nucleic Acids Research 47(16). p.8807-8820
Abstract

Translation is controlled by numerous accessory proteins and translation factors. In the yeast Saccharomyces cerevisiae, translation elongation requires an essential elongation factor, the ABCF ATPase eEF3. A closely related protein, New1, is encoded by a non-essential gene with cold sensitivity and ribosome assembly defect knock-out phenotypes. Since the exact molecular function of New1 is unknown, it is unclear if the ribosome assembly defect is direct, i.e. New1 is a bona fide assembly factor, or indirect, for instance due to a defect in protein synthesis. To investigate this, we employed yeast genetics, cryo-electron microscopy (cryo-EM) and ribosome profiling (Ribo-Seq) to interrogate the molecular function of New1. Overexpression... (More)

Translation is controlled by numerous accessory proteins and translation factors. In the yeast Saccharomyces cerevisiae, translation elongation requires an essential elongation factor, the ABCF ATPase eEF3. A closely related protein, New1, is encoded by a non-essential gene with cold sensitivity and ribosome assembly defect knock-out phenotypes. Since the exact molecular function of New1 is unknown, it is unclear if the ribosome assembly defect is direct, i.e. New1 is a bona fide assembly factor, or indirect, for instance due to a defect in protein synthesis. To investigate this, we employed yeast genetics, cryo-electron microscopy (cryo-EM) and ribosome profiling (Ribo-Seq) to interrogate the molecular function of New1. Overexpression of New1 rescues the inviability of a yeast strain lacking the otherwise strictly essential translation factor eEF3. The structure of the ATPase-deficient (EQ2) New1 mutant locked on the 80S ribosome reveals that New1 binds analogously to the ribosome as eEF3. Finally, Ribo-Seq analysis revealed that loss of New1 leads to ribosome queuing upstream of 3'-terminal lysine and arginine codons, including those genes encoding proteins of the cytoplasmic translational machinery. Our results suggest that New1 is a translation factor that fine-tunes the efficiency of translation termination or ribosome recycling.

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publishing date
type
Contribution to journal
publication status
published
in
Nucleic Acids Research
volume
47
issue
16
pages
8807 - 8820
publisher
Oxford University Press
external identifiers
  • pmid:31299085
  • scopus:85073311572
ISSN
1362-4962
DOI
10.1093/nar/gkz600
language
English
LU publication?
no
additional info
Publisher Copyright: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. Copyright: This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine
id
d6e3caad-95df-41e5-aed0-0a467e6db436
date added to LUP
2021-09-24 20:32:56
date last changed
2024-04-20 11:52:52
@article{d6e3caad-95df-41e5-aed0-0a467e6db436,
  abstract     = {{<p>Translation is controlled by numerous accessory proteins and translation factors. In the yeast Saccharomyces cerevisiae, translation elongation requires an essential elongation factor, the ABCF ATPase eEF3. A closely related protein, New1, is encoded by a non-essential gene with cold sensitivity and ribosome assembly defect knock-out phenotypes. Since the exact molecular function of New1 is unknown, it is unclear if the ribosome assembly defect is direct, i.e. New1 is a bona fide assembly factor, or indirect, for instance due to a defect in protein synthesis. To investigate this, we employed yeast genetics, cryo-electron microscopy (cryo-EM) and ribosome profiling (Ribo-Seq) to interrogate the molecular function of New1. Overexpression of New1 rescues the inviability of a yeast strain lacking the otherwise strictly essential translation factor eEF3. The structure of the ATPase-deficient (EQ2) New1 mutant locked on the 80S ribosome reveals that New1 binds analogously to the ribosome as eEF3. Finally, Ribo-Seq analysis revealed that loss of New1 leads to ribosome queuing upstream of 3'-terminal lysine and arginine codons, including those genes encoding proteins of the cytoplasmic translational machinery. Our results suggest that New1 is a translation factor that fine-tunes the efficiency of translation termination or ribosome recycling.</p>}},
  author       = {{Kasari, Villu and Pochopien, Agnieszka A. and Margus, Tõnu and Murina, Victoriia and Turnbull, Kathryn and Zhou, Yang and Nissan, Tracy and Graf, Michael and Nováček, Jiří and Atkinson, Gemma C. and Johansson, Marcus J.O. and Wilson, Daniel N. and Hauryliuk, Vasili}},
  issn         = {{1362-4962}},
  language     = {{eng}},
  number       = {{16}},
  pages        = {{8807--8820}},
  publisher    = {{Oxford University Press}},
  series       = {{Nucleic Acids Research}},
  title        = {{A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling}},
  url          = {{http://dx.doi.org/10.1093/nar/gkz600}},
  doi          = {{10.1093/nar/gkz600}},
  volume       = {{47}},
  year         = {{2019}},
}