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A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
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Number of Authors: 132019 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 47, no 16, p. 8807-8820Article in journal (Refereed) Published
Abstract [en]

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 (EQ(2)) 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.

Place, publisher, year, edition, pages
2019. Vol. 47, no 16, p. 8807-8820
National Category
Biochemistry and Molecular Biology
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URN: urn:nbn:se:su:diva-175709DOI: 10.1093/nar/gkz600ISI: 000490576900040PubMedID: 31299085OAI: oai:DiVA.org:su-175709DiVA, id: diva2:1369947
Available from: 2019-11-13 Created: 2019-11-13 Last updated: 2019-11-13Bibliographically approved

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Turnbull, KathrynJohansson, Marcus J. O.
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Department of Molecular Biosciences, The Wenner-Gren Institute
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