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.Základní údaje
Originální název
A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling
Autoři
KASARI, V., A.A. POCHOPIEN, T. MARGUS, V. MURINA, K. TURNBULL, Y. ZHOU, T. NISSAN, M. GRAF, Jiří NOVÁČEK (203 Česká republika, garant, domácí), G.C. ATKINSON, M.J.O. JOHANSSON, D.N. WILSON a V. HAURYLIUK
Vydání
Nucleic acids research, Oxford, Oxford University Press, 2019, 0305-1048
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 11.502
Kód RIV
RIV/00216224:14740/19:00113325
Organizační jednotka
Středoevropský technologický institut
UT WoS
000490576900040
Klíčová slova anglicky
MESSENGER-RNA DECAY; INITIATION-FACTOR; GENE ONTOLOGY; YEAST; ELONGATION; COMPLEX; VISUALIZATION; PURIFICATION; BIOGENESIS; EXPRESSION
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 27. 10. 2024 14:05, Ing. Martina Blahová
Anotace
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.
Návaznosti
90043, velká výzkumná infrastruktura |
|