title: OxyR: a molecular code for redox-related signaling.
abstract: Redox regulation has been perceived as a simple on-off switch in proteins (corresponding to reduced and oxidized states). Using the transcription factor OxyR as a model, we have generated, in vitro, several stable, posttranslational modifications of the single regulatory thiol (SH), including S-NO, S-OH, and S-SG, and shown that each occurs in vivo. These modified forms of OxyR are transcriptionally active but differ in structure, cooperative properties, DNA binding affinity, and promoter activities. OxyR can thus process different redox-related signals into distinct transcriptional responses. More generally, our data suggest a code for redox control through which allosteric proteins can subserve either graded (cooperative) or maximal (noncooperative) responses, and through which differential responsivity to redox-related signals can be achieved.
authors.affiliation: Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.
authors.forename: Sung Oog
authors.initials: SO
authors.lastname: Kim
authors.forename: Kunal
authors.initials: K
authors.lastname: Merchant
authors.forename: Raphael
authors.initials: R
authors.lastname: Nudelman
authors.forename: Wayne F
authors.initials: WF
authors.lastname: Beyer
authors.forename: Teresa
authors.initials: T
authors.lastname: Keng
authors.forename: Joseph
authors.initials: J
authors.lastname: DeAngelo
authors.forename: Alfred
authors.initials: A
authors.lastname: Hausladen
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Stamler
mesh_terms: D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine / Q000737:chemistry; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D006860:Hydrogen Bonding; D066298:In Vitro Techniques; D008954:Models, Biological; D008958:Models, Molecular; D009154:Mutation; D010084:Oxidation-Reduction; D011401:Promoter Regions, Genetic; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic; D015533:Transcriptional Activation
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D004220:Disulfides; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012097:Repressor Proteins; D013438:Sulfhydryl Compounds; D014157:Transcription Factors; C499299:oxyR protein, E coli; D003545:Cysteine