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Comparative Study
. 2002 May 3;109(3):383-96.
doi: 10.1016/s0092-8674(02)00723-7.

OxyR: a molecular code for redox-related signaling

Sung Oog Kim  1 , Kunal Merchant, Raphael Nudelman, Wayne F Beyer Jr, Teresa Keng, Joseph DeAngelo, Alfred Hausladen, Jonathan S Stamler
Affiliations
Free article
Comparative Study

OxyR: a molecular code for redox-related signaling

Sung Oog Kim et al. Cell. .
Free article

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.

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