The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers
| Autor: | Klingauf-Nerurkar, Purnima, Gillet, Ludovic C, Portugal-Calisto, Daniela, Oborská-Oplová, Michaela, Jäger, Martin, Schubert, Olga T, Pisano, Agnese, Peña, Cohue, Rao, Sanjana, Altvater, Martin, Chang, Yiming, Aebersold, Ruedi, Panse, Vikram G |
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| Přispěvatelé: | University of Zurich, Panse, Vikram G |
| Rok vydání: | 2019 |
| Předmět: |
Ribosomal Proteins
Saccharomyces cerevisiae Proteins 10179 Institute of Medical Microbiology QH301-705.5 Science ribosome quality control 2800 General Neuroscience Nuclear Proteins S. cerevisiae 610 Medicine & health Saccharomyces cerevisiae 1300 General Biochemistry Genetics and Molecular Biology GTP-Binding Proteins Biochemistry and Chemical Biology 2400 General Immunology and Microbiology 570 Life sciences biology Medicine cytoplasmic maturation Biology (General) ribosome assembly Ribosomes Research Article |
| Zdroj: | eLife eLife, 9 eLife, Vol 9 (2020) |
| ISSN: | 2050-084X |
| Popis: | 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. eLife, 9 ISSN:2050-084X |
| Databáze: | OpenAIRE |
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