A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance

Glutaredoxins represent a ubiquitous family of proteins that 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 baker's yeast, we found three so-far uncharacterized glutaredoxin-l...

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Bibliographic Details
Published in:Molecular biology of the cell 2008-06, Vol.19 (6), p.2673-2680
Main Authors: Mesecke, Nikola, Spang, Anne, Deponte, Marcel, Herrmann, Johannes M
Format: Article
Language:English
Subjects:
Cell Fractionation
Cell Membrane - drug effects
Cell Membrane - metabolism
Fluorescent Antibody Technique
Gene Deletion
Glutaredoxins - chemistry
Glutaredoxins - metabolism
Golgi Apparatus - drug effects
Golgi Apparatus - metabolism
Oxidants - pharmacology
Oxidative Stress - drug effects
Protein Folding
Protein Structure, Tertiary
Protein Transport - drug effects
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae - growth & development
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Sequence Homology, Amino Acid
Solubility - drug effects
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Summary:Glutaredoxins represent a ubiquitous family of proteins that 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 baker's yeast, we found three so-far uncharacterized glutaredoxin-like proteins that we named Grx6, Grx7, and Grx8. Grx6 and Grx7 represent closely related monothiol glutaredoxins that 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 such as 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.
ISSN:1059-1524
1939-4586
1939-4586
DOI:10.1091/mbc.E07-09-0896