The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers

eLife

Martin Jäger¹  Ruedi Aebersold²  Olga T Schubert²  Yiming Chang²  Purnima Klingauf-Nerurkar³  Cohue Peña³  Vikram G Panse³  Daniela Portugal-Calisto³  Martin Altvater³  Michaela Oborská-Oplová³  Sanjana Rao³  Agnese Pisano⁴  Ludovic C Gillet⁴ 

[1] Institute of Biochemistry, ETH Zurich, Zurich, Switzerland;Institute of Biochemistry, ETH Zurich, Zurich, Switzerland;Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland;Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland;

关键词: ribosome assembly;    ribosome quality control;    cytoplasmic maturation;   

DOI  :  10.7554/eLife.52474

来源: DOAJ

【 摘 要 】

Eukaryotic ribosome precursors acquire translation competence in the cytoplasm through stepwise release of bound assembly factors, and proofreading of their functional centers. In case of the pre-60S, these steps include removal of placeholders Rlp24, Arx1 and Mrt4 that prevent premature loading of the ribosomal protein eL24, the protein-folding machinery at the polypeptide exit tunnel (PET), and the ribosomal stalk, respectively. Here, we reveal that sequential ATPase and GTPase activities license release factors Rei1 and Yvh1 to trigger Arx1 and Mrt4 removal. Drg1-ATPase activity removes Rlp24 from the GTPase Nog1 on the pre-60S; consequently, the C-terminal tail of Nog1 is extracted from the PET. These events enable Rei1 to probe PET integrity and catalyze Arx1 release. Concomitantly, Nog1 eviction from the pre-60S permits peptidyl transferase center maturation, and allows Yvh1 to mediate Mrt4 release for stalk assembly. Thus, Nog1 co-ordinates the assembly, maturation and quality control of distant functional centers during ribosome formation.

【 授权许可】

Unknown