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M302304200v1
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Papers In Press, published online ahead of print April 7, 2003
J. Biol. Chem, 10.1074/jbc.M302304200
Submitted on March 5, 2003
Revised on April 2, 2003
Accepted on April 7, 2003

Redox regulation of 3' phospoadenylsulfate reductase from Escherichia coli by glutathione and glutaredoxins

Christopher Horst Lillig, Aristi Potamitou, Jens-Dirk Schwenn, Alexios Vlamis-Gardikas, and Arne Holmgren

Medical Nobel Institute for Biochemistry, Karolinska Institutet, Stockholm S-171 77

Corresponding Author: Arne.Holmgren{at}mbb.ki.se

Inorganic sulfate (SO42-, S+VI) is reduced in vivo to sulfite (SO32-, S+IV) via phosphoadenylylsulfate (PAPS) reductase. Escherichia coli lacking glutathione reductase and glutaredoxins (gor-grxA-grxB-grxC-) grows barely on sulfate. We found that incubation of PAPS reductase with oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the active site Cys 239. A newly developed method based on thiol-specific fluorescent alkylation and gel electrophoresis showed that glutathionylated PAPS reductase is reduced by glutaredoxins via a monothiol-mechanism. This glutathionylated species was also observed in poorly growing gor-grxA-grxB-grxC- cells expressing inactive glutaredoxin 2 (Grx2) C9S-C12S. However, it was absent in better growing cells expressing monothiol Grx2 C12S or wild type Grx2. Reversible glutathionylation may thus regulate the activity of PAPS reductase in vivo.


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