Thiol-based H2O2 signalling in microbial systems
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 switch...
| Autores: | , , , , , , , , , , |
|---|---|
| Formato: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2014 |
| País: | España |
| Recursos: | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| Repositorio: | Recercat. Dipósit de la Recerca de Catalunya |
| OAI Identifier: | oai:recercat.cat:10230/23855 |
| Acesso em linha: | http://hdl.handle.net/10230/23855 http://dx.doi.org/10.1016/j.redox.2014.01.015 |
| Access Level: | acceso abierto |
| Palavra-chave: | Escheríchia coli Saccharomyces cerevisiae -- Metabolisme Schizosaccharomyces pombe -- Metabolisme H2O2 sensor Cys oxidation OxyR Pap1 Yap1 S. pombe |
| Resumo: | 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. |
|---|