PMID:19202292
| Citation |
Yamamoto, K, Matsumoto, F, Minagawa, S, Oshima, T, Fujita, N, Ogasawara, N and Ishihama, A (2009) Characterization of CitA-CitB signal transduction activating genes involved in anaerobic citrate catabolism in Escherichia coli. Biosci. Biotechnol. Biochem. 73:346-50 |
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| Abstract |
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 CitB. 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. |
| Links | |
| Keywords |
Anaerobiosis; Citric Acid/metabolism; Cytoplasm/metabolism; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Genes, Bacterial; Oxidation-Reduction; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/metabolism; Protein Structure, Tertiary; Signal Transduction/genetics; Substrate Specificity; Transcription Factors/metabolism |
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