How to Flip the (Redox) Switch

Redox-sensitive transcription factors such as the E. coli OxyR and S. cerevisiae Yap1, are activated by conformational changes that stem from the post-translational modification of reactive protein thiols. Recent studies provide new insights on how different agents that cause redox stress mediate th...

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Veröffentlicht in:	Cell 2002-11, Vol.111 (5), p.607-610
1. Verfasser:	Georgiou, George
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - genetics Bacterial Proteins - metabolism Cysteine - chemistry Cysteine - metabolism Disulfides - chemistry DNA-Binding Proteins - metabolism Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli - metabolism Glutathione Peroxidase - chemistry Glutathione Peroxidase - drug effects Glutathione Peroxidase - metabolism Hydrogen Peroxide - metabolism Hydrogen Peroxide - pharmacology Models, Biological Mutation Oxidation-Reduction Oxidative Stress Protein Conformation Protein Processing, Post-Translational Reactive Oxygen Species - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Transcription Factors - genetics Transcription Factors - metabolism Transcriptional Activation
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Beschreibung
Zusammenfassung:	Redox-sensitive transcription factors such as the E. coli OxyR and S. cerevisiae Yap1, are activated by conformational changes that stem from the post-translational modification of reactive protein thiols. Recent studies provide new insights on how different agents that cause redox stress mediate the activation of transcription through distinct and specific pathways.
ISSN:	0092-8674 1097-4172
DOI:	10.1016/S0092-8674(02)01165-0