Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli

FEBS Letters

Kobayashi, Kazuo¹  Tagawa, Seiichi¹ 

[1] The Institute of Scientific and Industrial Research, Osaka University, Mihogaoka 8-1, Ibaraki, Osaka 567-0047, Japan

关键词: SoxR;    Transcriptional activator;    Oxidative stress;    Redox regulation;    NADPH;    Escherichia coli;    IPTG;    isopropyl-β-D-thiogalactopyranoside;    MOPS;    3-(N-morpholino)propane sulfonic acid;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(99)00565-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

SoxR is a transcription factor triggered by oxidative stress in Escherichia coli. Recent evidence suggests that novel redox regulation couples oxidation state to promoter activation. We have isolated the reductase for SoxR in E. coli using an assay of NADPH- and SoxR-dependent cytochrome c reductase activity. When the purified protein was incubated in an anaerobic reaction mixture containing SoxR and NADPH, the reduction of [2Fe-2S] cluster of SoxR was observed by optical and EPR spectroscopy. Our results indicate that the purified protein serves as an NADPH-dependent reduction system for SoxR.

【 授权许可】

Unknown