SGD Paper Help


Page Contents:
Greetham D and Grant CM  (2009) Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 29(11):3229-40

Abstract: Peroxiredoxins are ubiquitous enzymes which protect cells against oxidative stress. The first step of catalysis is common to all peroxiredoxins and results in oxidation of a conserved peroxidatic cysteine residue to sulphenic acid. This forms an intermolecular disulphide bridge in the case of 2-Cys peroxiredoxins, which is a substrate for the thioredoxin system. 1-Cys Prx's contain a peroxidatic cysteine, but do not contain a second conserved cysteine residue, and hence the identity of the in vivo reduction system has been unclear. Here, we show that the yeast mitochondrial 1-Cys Prx1 is reactivated by glutathionylation of the catalytic cysteine residue and subsequent reduction by thioredoxin reductase (Trr2) coupled with glutathione. This novel mechanism does not require the usual thioredoxin (Trx3) redox partner of Trr2 for antioxidant activity; although in vitro assays show that the Trr2/Trx3 and Trr2/GSH systems exhibit similar capacities for supporting Prx1 catalysis. Our data also indicate that mitochondria are a main target of cadmium-induced oxidative stress and Prx1 is particularly required to protect against mitochondrial oxidation. This study demonstrates a physiological reaction mechanism for 1-Cys peroxiredoxins and reveals a new role in protection against mitochondrial heavy metal toxicity.

Status: Published Type: Journal Article PubMed ID: 19332553

Topics addressed in this paper

Number of different genes curated to this paper: 8

  • 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.
Topics Genes linked to topics
ALO1 GLR1 GSH1 PRX1 TRR1 TRR2 TRX3 TSA1
Additional Literature blue ball blue ball blue ball blue ball
Function/Process blue ball blue ball blue ball
Genetic Interactions blue ball blue ball blue ball blue ball blue ball
Mutants/Phenotypes blue ball blue ball blue ball blue ball blue ball blue ball blue ball
Primary Literature blue ball blue ball blue ball blue ball
Protein Physical Properties blue ball blue ball
Protein Processing/Modification/Regulation blue ball
Protein Sequence Features blue ball
Strains/Constructs blue ball blue ball blue ball blue ball blue ball blue ball blue ball
Substrates/Ligands/Cofactors blue ball blue ball

Author Searches

To find contact information or other publications by the authors of this paper, follow these three steps:
  1. (1) Choose an author,
  2. (2) Choose a search parameter,
  3. (3) Click to implement
Page Contents: