tailieunhanh - Báo cáo khoa học: Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome

The yeast 20S proteasome is subject to sulfhydryl redox alterations, such as the oxidation of cysteine residues (Cys-SH) into cysteine sulfenic acid (Cys-SOH), followed by S-glutathionylation (Cys-S-SG). Proteasome S-glutath-ionylation promotes partial loss of chymotrypsin-like activity and post-acidic cleavage without alteration of the trypsin-like proteasomal activity. | ễFEBS Journal Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome Gustavo M. Silva1 2 Luis . Netto2 Karen F. Discola2 Gilberto M. Piassa-Filho1 Daniel C. Pimenta1 Jose A. Barcena3 and Marilene Demasi1 1 Institute Butantan Laboratorio de Bioquimica e Biofisica Sao Paulo Brazil 2 Departamento de Genetica e Biologia Evolutiva Instituto de Biociencias Universidade de Sao Paulo Brazil 3 Departamento de Bioquimica y Biologia Molecular Universidad de Cordoba Spain Keywords 20S proteasome deglutathionylation glutaredoxin S-glutathionylation thioredoxins Correspondence M. Demasi Instituto Butantan Laboratorio de Bioquimica e Biofisica Avenida Vital Brasil 1500 05503 900 Sao Paulo Brazil Fax 55 11 3726 7222 ext. 2018 Tel 55 11 3726 7222 ext. 2101 E-mail marimasi@ Received 8 December 2007 revised 31 March 2008 accepted 3 April 2008 doi The yeast 20S proteasome is subject to sulfhydryl redox alterations such as the oxidation of cysteine residues Cys-SH into cysteine sulfenic acid Cys-SOH followed by S-glutathionylation Cys-S-SG . Proteasome S-glutath-ionylation promotes partial loss of chymotrypsin-like activity and post-acidic cleavage without alteration of the trypsin-like proteasomal activity. Here we show that the 20S proteasome purified from stationary-phase cells was natively S-glutathionylated. Moreover recombinant glut-aredoxin 2 removes glutathione from natively or in vitro S-glutathionylated 20S proteasome allowing the recovery of chymotrypsin-like activity and post-acidic cleavage. Glutaredoxin 2 deglutathionylase activity was dependent on its entry into the core particle as demonstrated by stimulating S-glutathionylated proteasome opening. Under these conditions degluta-thionylation of the 20S proteasome and glutaredoxin 2 degradation were increased when compared to non-stimulated samples. Glutaredoxin 2 fragmentation by the 20S proteasome was evaluated by .

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