期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 73, 期 2, 页码 346-350出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.80586
关键词
histidine sensor kinase; two-component signal transduction; CitA-CitB; Escherichia coli
类别
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [18770157]
- Grants-in-Aid for Scientific Research [18770157] Funding Source: KAKEN
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.
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