Detailed Information on Publication Record
2019
A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
KASARI, V., A.A. POCHOPIEN, T. MARGUS, V. MURINA, K. TURNBULL et. al.Basic information
Original name
A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
Authors
KASARI, V., A.A. POCHOPIEN, T. MARGUS, V. MURINA, K. TURNBULL, Y. ZHOU, T. NISSAN, M. GRAF, Jiří NOVÁČEK (203 Czech Republic, guarantor, belonging to the institution), G.C. ATKINSON, M.J.O. JOHANSSON, D.N. WILSON and V. HAURYLIUK
Edition
Nucleic acids research, Oxford, Oxford University Press, 2019, 0305-1048
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 11.502
RIV identification code
RIV/00216224:14740/19:00113325
Organization unit
Central European Institute of Technology
UT WoS
000490576900040
Keywords in English
MESSENGER-RNA DECAY; INITIATION-FACTOR; GENE ONTOLOGY; YEAST; ELONGATION; COMPLEX; VISUALIZATION; PURIFICATION; BIOGENESIS; EXPRESSION
Tags
International impact, Reviewed
Změněno: 27/10/2024 14:05, Ing. Martina Blahová
Abstract
V originále
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.
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