J 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

Štítky

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
Název: CIISB