OxyR: a molecular code for redox-related signaling.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Kim, SO; Merchant, K; Nudelman, R; Beyer, WF; Keng, T; DeAngelo, J; Hausladen, A; Stamler, JS

Published Date

  • May 2002

Published In

Volume / Issue

  • 109 / 3

Start / End Page

  • 383 - 396

PubMed ID

  • 12015987

Pubmed Central ID

  • 12015987

Electronic International Standard Serial Number (EISSN)

  • 1097-4172

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(02)00723-7

Language

  • eng