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
EID Scopus
2-s2.0-85073311572
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
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