OxyR: a molecular code for redox sensing?
Helmann discusses the controversy surrounding the activation of the bacterial redox-regulated transcription factor OxyR. Evidence from different sources, including crystallographic data, has led to opposing models for the chemical changes that activate OxyR. Is it an intramolecular disulfide-linkage? Is it oxidation of a single cysteine residue to a sulfenic acid? Are there different active forms depending on the type of cysteine modification: intramolecular disulfide bond, sulfenic acid, S-nitrosothiol, or mixed disulfide with glutathione? These issues are discussed in the broader context of transcriptional regulation and how particular regulators may activate distinct genetic programs depending on the precise state of the regulator produced in response to environmental cues.
Helmann
John D
JD
Department of Microbiology, Cornell University, Ithaca, NY 14853-8101, USA. jdh9@cornell.edu
D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D004268:DNA-Binding Proteins; D019281:Dimerization; D005786:Gene Expression Regulation / Q000502:physiology; D005798:Genes, Bacterial / Q000502:physiology; D005809:Genes, Regulator / Q000502:physiology; D010084:Oxidation-Reduction; D012097:Repressor Proteins / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*; D014158:Transcription, Genetic / Q000502:physiology
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors