Thiol-based H2O2 signalling in microbial systems

Boronat i Llop, Susanna, 1965-; Domènech, Alba; Paulo Mirasol, Esther, 1984-; Calvo, Isabel A.; García Santamarina, Sarela, 1978-; García, Patrícia; Encinar del Dedo, Javier; Barcons-Simon, Anna; Serrano, Erica; Carmona, Mercè; Hidalgo Hernando, Elena

doi:http://dx.doi.org/10.1016/j.redox.2014.01.015

Thiol-based H2O2 signalling in microbial systems

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Boronat S, Domènech A, Paulo E, Calvo IA, García-Santamarina S, García P et al. Thiol-based H2O2 signalling in microbial systems. Redox Biology. 2014;2:395-9. DOI: 10.1016/j.redox.2014.01.015

Abstract

Cysteine residues, and in particular their thiolate groups, react not only with reactive oxygen species but also with electrophiles and with reactive nitrogen species. Thus, cysteine oxidation has often been linked to the toxic effects of some of these reactive molecules. However, thiol-based switches are common in protein sensors of antioxidant cascades, in both prokaryotic and eukaryotic organisms. We will describe here three redox sensors, the transcription factors OxyR, Yap1 and Pap1, which respond by disulfide bond formation to hydrogen peroxide stress, focusing specially on the differences among the three peroxide-sensing mechanisms.