author_facet Kasari, Villu
Pochopien, Agnieszka A
Margus, Tõnu
Murina, Victoriia
Turnbull, Kathryn
Zhou, Yang
Nissan, Tracy
Graf, Michael
Nováček, Jiří
Atkinson, Gemma C
Johansson, Marcus J O
Wilson, Daniel N
Hauryliuk, Vasili
Kasari, Villu
Pochopien, Agnieszka A
Margus, Tõnu
Murina, Victoriia
Turnbull, Kathryn
Zhou, Yang
Nissan, Tracy
Graf, Michael
Nováček, Jiří
Atkinson, Gemma C
Johansson, Marcus J O
Wilson, Daniel N
Hauryliuk, Vasili
author Kasari, Villu
Pochopien, Agnieszka A
Margus, Tõnu
Murina, Victoriia
Turnbull, Kathryn
Zhou, Yang
Nissan, Tracy
Graf, Michael
Nováček, Jiří
Atkinson, Gemma C
Johansson, Marcus J O
Wilson, Daniel N
Hauryliuk, Vasili
spellingShingle Kasari, Villu
Pochopien, Agnieszka A
Margus, Tõnu
Murina, Victoriia
Turnbull, Kathryn
Zhou, Yang
Nissan, Tracy
Graf, Michael
Nováček, Jiří
Atkinson, Gemma C
Johansson, Marcus J O
Wilson, Daniel N
Hauryliuk, Vasili
Nucleic Acids Research
A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
Genetics
author_sort kasari, villu
spelling Kasari, Villu Pochopien, Agnieszka A Margus, Tõnu Murina, Victoriia Turnbull, Kathryn Zhou, Yang Nissan, Tracy Graf, Michael Nováček, Jiří Atkinson, Gemma C Johansson, Marcus J O Wilson, Daniel N Hauryliuk, Vasili 0305-1048 1362-4962 Oxford University Press (OUP) Genetics http://dx.doi.org/10.1093/nar/gkz600 <jats:title>Abstract</jats:title><jats: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.</jats:p> A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling Nucleic Acids Research
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title A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_unstemmed A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_full A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_fullStr A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_full_unstemmed A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_short A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_sort a role for the saccharomyces cerevisiae abcf protein new1 in translation termination/recycling
topic Genetics
url http://dx.doi.org/10.1093/nar/gkz600
publishDate 2019
physical 8807-8820
description <jats:title>Abstract</jats:title><jats: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.</jats:p>
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author Kasari, Villu, Pochopien, Agnieszka A, Margus, Tõnu, Murina, Victoriia, Turnbull, Kathryn, Zhou, Yang, Nissan, Tracy, Graf, Michael, Nováček, Jiří, Atkinson, Gemma C, Johansson, Marcus J O, Wilson, Daniel N, Hauryliuk, Vasili
author_facet Kasari, Villu, Pochopien, Agnieszka A, Margus, Tõnu, Murina, Victoriia, Turnbull, Kathryn, Zhou, Yang, Nissan, Tracy, Graf, Michael, Nováček, Jiří, Atkinson, Gemma C, Johansson, Marcus J O, Wilson, Daniel N, Hauryliuk, Vasili, Kasari, Villu, Pochopien, Agnieszka A, Margus, Tõnu, Murina, Victoriia, Turnbull, Kathryn, Zhou, Yang, Nissan, Tracy, Graf, Michael, Nováček, Jiří, Atkinson, Gemma C, Johansson, Marcus J O, Wilson, Daniel N, Hauryliuk, Vasili
author_sort kasari, villu
container_issue 16
container_start_page 8807
container_title Nucleic Acids Research
container_volume 47
description <jats:title>Abstract</jats:title><jats: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.</jats:p>
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spelling Kasari, Villu Pochopien, Agnieszka A Margus, Tõnu Murina, Victoriia Turnbull, Kathryn Zhou, Yang Nissan, Tracy Graf, Michael Nováček, Jiří Atkinson, Gemma C Johansson, Marcus J O Wilson, Daniel N Hauryliuk, Vasili 0305-1048 1362-4962 Oxford University Press (OUP) Genetics http://dx.doi.org/10.1093/nar/gkz600 <jats:title>Abstract</jats:title><jats: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.</jats:p> A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling Nucleic Acids Research
spellingShingle Kasari, Villu, Pochopien, Agnieszka A, Margus, Tõnu, Murina, Victoriia, Turnbull, Kathryn, Zhou, Yang, Nissan, Tracy, Graf, Michael, Nováček, Jiří, Atkinson, Gemma C, Johansson, Marcus J O, Wilson, Daniel N, Hauryliuk, Vasili, Nucleic Acids Research, A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling, Genetics
title A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_full A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_fullStr A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_full_unstemmed A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_short A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
title_sort a role for the saccharomyces cerevisiae abcf protein new1 in translation termination/recycling
title_unstemmed A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
topic Genetics
url http://dx.doi.org/10.1093/nar/gkz600