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 switc...

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Main Authors: Susanna Boronat, Alba Domènech, Esther Paulo, Isabel A. Calvo, Sarela García-Santamarina, Patricia García, Javier Encinar del Dedo, Anna Barcons, Erica Serrano, Mercè Carmona, Elena Hidalgo
Format: Article
Language:English
Published: Elsevier 2014-01-01
Series:Redox Biology
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2213231714000305
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spelling doaj-705108d7f2a04e168fb259dcee159e252020-11-25T02:40:22ZengElsevierRedox Biology2213-23172014-01-012C39539910.1016/j.redox.2014.01.015Thiol-based H2O2 signalling in microbial systemsSusanna BoronatAlba DomènechEsther PauloIsabel A. CalvoSarela García-SantamarinaPatricia GarcíaJavier Encinar del DedoAnna BarconsErica SerranoMercè CarmonaElena Hidalgo 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. http://www.sciencedirect.com/science/article/pii/S2213231714000305H2O2 sensorCys oxidationOxyRPap1Yap1S. pombe
collection DOAJ
language English
format Article
sources DOAJ
author Susanna Boronat
Alba Domènech
Esther Paulo
Isabel A. Calvo
Sarela García-Santamarina
Patricia García
Javier Encinar del Dedo
Anna Barcons
Erica Serrano
Mercè Carmona
Elena Hidalgo
spellingShingle Susanna Boronat
Alba Domènech
Esther Paulo
Isabel A. Calvo
Sarela García-Santamarina
Patricia García
Javier Encinar del Dedo
Anna Barcons
Erica Serrano
Mercè Carmona
Elena Hidalgo
Thiol-based H2O2 signalling in microbial systems
Redox Biology
H2O2 sensor
Cys oxidation
OxyR
Pap1
Yap1
S. pombe
author_facet Susanna Boronat
Alba Domènech
Esther Paulo
Isabel A. Calvo
Sarela García-Santamarina
Patricia García
Javier Encinar del Dedo
Anna Barcons
Erica Serrano
Mercè Carmona
Elena Hidalgo
author_sort Susanna Boronat
title Thiol-based H2O2 signalling in microbial systems
title_short Thiol-based H2O2 signalling in microbial systems
title_full Thiol-based H2O2 signalling in microbial systems
title_fullStr Thiol-based H2O2 signalling in microbial systems
title_full_unstemmed Thiol-based H2O2 signalling in microbial systems
title_sort thiol-based h2o2 signalling in microbial systems
publisher Elsevier
series Redox Biology
issn 2213-2317
publishDate 2014-01-01
description 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.
topic H2O2 sensor
Cys oxidation
OxyR
Pap1
Yap1
S. pombe
url http://www.sciencedirect.com/science/article/pii/S2213231714000305
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