SGD Paper 
Mesecke N, et al. (2008) A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance. Mol Biol Cell 19(6):2673-80
Abstract: 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 baker's 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.
| Status: Published | Type: Journal Article | PubMed ID: 18400945 |
Topics addressed in this paper
Number of different genes curated to this paper: 5
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
