20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

Author Demasi, Marilene Google Scholar
Hand, Adrian Google Scholar
Ohara, Erina Google Scholar
Oliveira, Cristiano L. P. Google Scholar
Bicev, Renata N. Google Scholar
Bertoncini, Clelia A. Autor UNIFESP Google Scholar
Netto, Luis E. S. Google Scholar
Institution Inst Butantan
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Abstract Protein S-glutathionylation is a post-translational modification that controls many cellular pathways. Recently, we demonstrated that the alpha 5-subunit of the 20S proteasome is S-glutathionylated in yeast cells grown to the stationary phase in rich medium containing glucose, stimulating 20S core gate opening and increasing the degradation of oxidized proteins. in the present study, we evaluated the correlation between proteasomal S-glutathionylation and the intracellular redox status. the redox status was controlled by growing yeast cells in distinct carbon sources which induced respiratory (glycerol/ethanol) or fermentative (glucose) metabolism. Cells grown under glycerol/ethanol displayed higher reductive power when compared to cells grown under glucose. When purified from cells grown in glucose, 20S proteasome alpha 5-subunit exhibited an intense anti-glutathione labeling. A higher frequency of the open catalytic chamber gate was observed in the S-glutathionylated preparations as demonstrated by transmission electron microscopy. Therefore, cells that had been grown in glucose displayed an increased ability to degrade oxidized proteins. the results of the present study suggest that 20S proteasomal S-glutathionylation is a relevant adaptive response to oxidative stress that is capable to sense the intracellular redox environment, leading to the removal of oxidized proteins via a process that is not dependent upon ubiquitylation and ATP consumption. (C) 2014 Elsevier Inc. All rights reserved.
Keywords 20S proteasome
S-glutathionylation
S. cerevisiae
Redox modulation
Oxidized proteins
Proteolysis
Language English
Date 2014-09-01
Published in Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 557, p. 65-71, 2014.
ISSN 0003-9861 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 65-71
Origin http://dx.doi.org/10.1016/j.abb.2014.05.002
Access rights Closed access
Type Article
Web of Science ID WOS:000339646600009
URI http://repositorio.unifesp.br/handle/11600/38148

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