Characterization of CitA-CitB Signal Transduction Activating Genes Involved in Anaerobic Citrate Catabolism in Escherichia coli

被引：11

作者：

Yamamoto, Kaneyoshi ^{[1
,2
,3
]}

Matsumoto, Fumika ^{[3
]}

Minagawa, Shu ^{[3
]}

Oshima, Taku ^{[4
]}

Fujita, Nobuyuki ^{[5
]}

Ogasawara, Naotake ^{[4
]}

Ishihama, Akira ^{[1
,2
]}

机构：

[1] Hosei Univ, Dept Frontier Biosci, Tokyo 1848584, Japan

[2] Hosei Univ, Res Ctr Micronano Technol, Tokyo 1848584, Japan

[3] Kinki Univ, Dept Adv Biosci, Nara 6318505, Japan

[4] Nara Inst Sci & Technol, Grad Sch Informat Sci, Nara 6300101, Japan

[5] Natl Inst Technol & Evaluat, Genome Anal Ctr, Shibuya Ku, Tokyo 1510066, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2009年 / 73卷 / 02期

关键词：

histidine sensor kinase; two-component signal transduction; CitA-CitB; Escherichia coli; NITROGEN REGULATOR-II; SENSOR KINASE CITA; HISTIDINE-KINASE; KLEBSIELLA-PNEUMONIAE; PERIPLASMIC DOMAIN; IN-VITRO; RECEPTOR; AUTOPHOSPHORYLATION; IDENTIFICATION; BINDING;

D O I：

10.1271/bbb.80586

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In Escherichia coli, CitA is a membrane-associated sensor histidine kinase that phosphorylates CitB, the response regulator. It is predicated to play a key role in anaerobic citrate catabolism. The citrate-binding site in CitA is located within its periplasmic domain, while the cytoplasmic domain (CitA-C) is involved in autophosphorylation. We found that autophosphorylation in vitro of CitA-C was induced by DTT. Using the whole set of CitA-C derivatives containing Cys-Ala substitution(s), Cys at 529 was found to be essential to the redox-sensing of autophosphorylation. The phosphorylated CitA-C transferred a phosphate to CUB. DNase-I footprinting assay indicated that CitB specifically bound on the intergenic region between the citA and citC genes. These results characterize the molecular mechanism of the CitA-CitB signal transduction system in E. coli.

引用

页码：346 / 350

页数：5

共 18 条

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