The Proteasome Lid Triggers COP9 Signalosome Activity during the Transition of Saccharomyces cerevisiae Cells into Quiescence.

Autor: Bramasole L; Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.; Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 31905, Israel., Sinha A; Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel., Harshuk D; Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.; Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 31905, Israel., Cirigliano A; Department of Biology and Biotechnology 'Charles Darwin', La Sapienza University of Rome, 00185 Rome, Italy., Gurevich S; Department of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel., Yu Z; Department of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel., Carmeli RL; Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel., Glickman MH; Department of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel., Rinaldi T; Department of Biology and Biotechnology 'Charles Darwin', La Sapienza University of Rome, 00185 Rome, Italy., Pick E; Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel. elahpic@research.haifa.ac.il.; Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 31905, Israel. elahpic@research.haifa.ac.il.
Jazyk: angličtina
Zdroj: Biomolecules [Biomolecules] 2019 Sep 04; Vol. 9 (9). Date of Electronic Publication: 2019 Sep 04.
DOI: 10.3390/biom9090449
Abstrakt: The class of Cullin-RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes, a handful of which are associated with the proteasome. The CRL activity is triggered by modification of the Cullin subunit with the ubiquitin-like protein, NEDD8 (also known as Rub1 in Saccharomyces cerevisiae ). Cullin modification is then reversed by hydrolytic action of the COP9 signalosome (CSN). As the NEDD8-Rub1 catalytic cycle is not essential for the viability of S. cerevisiae , this organism is a useful model system to study the alteration of Rub1-CRL conjugation patterns. In this study, we describe two distinct mutants of Rpn11, a proteasome-associated deubiquitinating enzyme, both of which exhibit a biochemical phenotype characterized by high accumulation of Rub1-modified Cdc53-Cullin1 (yCul1) upon entry into quiescence in S. cerevisiae . Further characterization revealed proteasome 19S-lid-associated deubiquitination activity that authorizes the hydrolysis of Rub1 from yCul1 by the CSN complex. Thus, our results suggest a negative feedback mechanism via proteasome capacity on upstream ubiquitinating enzymes.
Competing Interests: The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.
Databáze: MEDLINE
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