Characterization of the nitric oxide-reactive transcriptional activator NorR

被引：15

作者：

D'Autreaux, Benoit ^{[1
]}

Tucker, Nick ^{[2
]}

Spiro, Stephen ^{[3
]}

Dixon, Ray ^{[2
]}

机构：

[1] CEA Saclay, Inst Biol & Technol Saclay, Serv Biol Integrat & Genet Mol, Lab Stress Oxydant & Canc, F-91191 Gif Sur Yvette, France

[2] John Innes Inst, Norwich NR4 7UH, Norfolk, England

[3] Univ Texas Dallas, Dept Mol & Cell Biol, Richardson, TX 75083 USA

来源：

GLOBINS AND OTHER NITRIC OXIDE-REACTIVE PROTEINS, PART B | 2008年 / 437卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/S0076-6879(07)37013-4

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The prokaryotic transcriptional regulator NorR is unusual in that it utilizes a mononuclear ferrous iron center rather than a heme moiety as a means of sensing nitric oxide (NO). Binding of NO to the nonheme iron center in the amino-terminal GAF domain of NorR results in formation of a mononitrosyl iron complex and relieves intramolecular repression within NorR, allowing this regulatory protein, a member of the sigma(54)-dependent family of enhancer-binding proteins, to activate expression of genes required for NO detoxification. This chapter describes detailed protocols for measuring transcriptional activation by Escherichia coli NorR in vivo and in vitro. It also details spectroscopic methods for analysis of the interaction of NO with the nonheme iron center and determination of the NO-binding affinity constant.

引用

页码：235 / 251

页数：17

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