PMID:18206967
| Citation |
Yamamoto, Y, Ritz, D, Planson, AG, Jönsson, TJ, Faulkner, MJ, Boyd, D, Beckwith, J and Poole, LB (2008) Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity. Mol. Cell 29:36-45 |
|---|---|
| Abstract |
The bacterial peroxiredoxin AhpC, a cysteine-dependent peroxidase, can be converted through a single amino acid insertion to a disulfide reductase, AhpC*, active in the glutathione and glutaredoxin pathway. Here we show that, whereas AhpC* is inactive as a peroxidase, other point mutants in AhpC can confer the in vivo disulfide reductase activity without abrogating peroxidase activity. Moreover, AhpC* and several point mutants tested in vitro exhibit an enhanced reductase activity toward mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo requirements for these components. Remarkably, this Grx-S-SG reductase activity relies not on the peroxidatic cysteine but rather on the resolving cysteine that plays only a secondary role in the peroxidase mechanism. Furthermore, putative conformational changes, which impart this unusual Grx-S-SG reductase activity, are transmissible across subunits. Thus, AhpC and potentially other peroxiredoxins in this widespread family can elaborate a new reductase function that alleviates disulfide stress. |
| Links |
PubMed PMC2239235 Online version:10.1016/j.molcel.2007.11.029 |
| Keywords |
Amino Acid Substitution; Cysteine/metabolism; Dimerization; Disulfides/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Glutaredoxins/metabolism; Glutathione/metabolism; Hydrogen Peroxide/metabolism; Models, Molecular; Mutagenesis, Insertional; Oxidation-Reduction; Oxidative Stress; Oxidoreductases/chemistry; Oxidoreductases/genetics; Oxidoreductases/physiology; Peroxiredoxins/chemistry; Peroxiredoxins/genetics; Peroxiredoxins/physiology; Point Mutation; Protein Conformation; Protein Subunits; Substrate Specificity; Trinucleotide Repeats |
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