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Vol. 18, Issue 6, 2288-2295, June 2007
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Departament de Ciències Experimentals i de la Salut, Universitat Pompeu Fabra, E-08003 Barcelona, Spain
Submitted November 27, 2006;
Revised March 16, 2007;
Accepted March 26, 2007
Monitoring Editor: Thomas Fox
Peroxiredoxins are known to interact with hydrogen peroxide (H2O2) and to participate in oxidant scavenging, redox signal transduction, and heat-shock responses. The two-cysteine peroxiredoxin Tpx1 of Schizosaccharomyces pombe has been characterized as the H2O2 sensor that transduces the redox signal to the transcription factor Pap1. Here, we show that Tpx1 is essential for aerobic, but not anaerobic, growth. We demonstrate that Tpx1 has an exquisite sensitivity for its substrate, which explains its participation in maintaining low steady-state levels of H2O2. We also show in vitro and in vivo that inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid is always preceded by a sulfinic acid form in a covalently linked dimer, which may be important for understanding the kinetics of Tpx1 inactivation. Furthermore, we provide evidence that a strain expressing Tpx1.C169S, lacking the resolving cysteine, can sustain aerobic growth, and we show that small reductants can modulate the activity of the mutant protein in vitro, probably by supplying a thiol group to substitute for cysteine 169.
* These authors contributed equally to this work.
Address correspondence to: Elena Hidalgo (elena.hidalgo{at}upf.edu)
Abbreviations used: DNPH, dinitrophenylhydrazine; DTT, dithiothreitol; GSH, glutathione; ORF, open reading frame; PAGE, polyacrylamide gel electrophoresis; Prx, peroxiredoxin; TCA, trichloroacetic acid.
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M. Jara, A. P. Vivancos, and E. Hidalgo C-terminal truncation of the peroxiredoxin Tpx1 decreases its sensitivity for hydrogen peroxide without compromising its role in signal transduction. Genes Cells, February 1, 2008; 13(2): 171 - 179. [Abstract] [Full Text] [PDF] |
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