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A more recent version of this article appeared on June 1, 2008
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Submitted on September 13, 2007
Revised on March 25, 2008
Accepted on April 2, 2008
*Institute of Physiological Chemistry, University of Munich, 81377 Munich, Germany;
Biozentrum, University of Basel, CH-4056 Basel, Switzerland;
Cell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany
Monitoring Editor: Jeffrey Brodsky
Glutaredoxins represent a ubiquitous family of proteins which catalyze the reduction of disulfide bonds in their substrate proteins by use of reduced glutathione. In an attempt to identify the full complement of glutaredoxins in bakers yeast, we found three so far uncharacterized glutaredoxin-like proteins which we named Grx6, Grx7 and Grx8. Grx6 and Grx7 represent closely related monothiol glutaredoxins which are synthesized with N-terminal signal sequences. Both proteins are located in the cis-Golgi thereby representing the first glutaredoxins found in a compartment of the secretory pathway. In contrast to formerly described monothiol glutaredoxins, Grx6 and Grx7 showed a high glutaredoxin activity in vitro. Grx6 and Grx7 overlap in their activity and deletion mutants lacking both proteins show growth defects and a strongly increased sensitivity toward oxidizing agents like hydrogen peroxide or diamide. Our observations suggest that Grx6 and Grx7 do not play a general role in the oxidative folding of proteins in the early secretory pathway but rather counteract the oxidation of specific thiol groups in substrate proteins.
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