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Cell Rep. 2013 Dec 12;5(5):1425-35. doi: 10.1016/j.celrep.2013.10.036. Epub 2013 Nov 21.

A peroxiredoxin promotes H2O2 signaling and oxidative stress resistance by oxidizing a thioredoxin family protein.

Author information

1
Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK.
2
Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK. Electronic address: b.a.morgan@ncl.ac.uk.
3
Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK. Electronic address: e.a.veal@ncl.ac.uk.

Abstract

H2O2 can cause oxidative damage associated with age-related diseases such as diabetes and cancer but is also used to initiate diverse responses, including increased antioxidant gene expression. Despite significant interest, H2O2-signaling mechanisms remain poorly understood. Here, we present a mechanism for the propagation of an H2O2 signal that is vital for the adaptation of the model yeast, Schizosaccharomyces pombe, to oxidative stress. Peroxiredoxins are abundant peroxidases with conserved antiaging and anticancer activities. Remarkably, we find that the only essential function for the thioredoxin peroxidase activity of the Prx Tpx1(hPrx1/2) in resistance to H2O2 is to inhibit a conserved thioredoxin family protein Txl1(hTxnl1/TRP32). Thioredoxins regulate many enzymes and signaling proteins. Thus, our discovery that a Prx amplifies an H2O2 signal by driving the oxidation of a thioredoxin-like protein has important implications, both for Prx function in oxidative stress resistance and for responses to H2O2.

PMID:
24268782
PMCID:
PMC3898613
DOI:
10.1016/j.celrep.2013.10.036
[Indexed for MEDLINE]
Free PMC Article

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