PMID:9972245

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Citation

Matsushika, A and Mizuno, T (1998) Mutational analysis of the histidine-containing phosphotransfer (HPt) signaling domain of the ArcB sensor in Escherichia coli. Biosci. Biotechnol. Biochem. 62:2236-8

Abstract

The Escherichia coli ArcB sensor is involved in anaerobic phosphotransfer signal transduction. ArcB is a hybrid sensor that contains three types of phosphotransfer signaling domains in its primary amino acid sequence, namely, transmitter (or His-Kinase), receiver, and histidine-containing phosphotransfer (HPt) domains. However, examination of the function of the newly-discovered HPt domain (named ArcBc) is still at a very early stage. To gain a general insight into the structure and function of the widespread HPt domains, on the basis of its three-dimensional crystal structure, in this study we constructed a certain set of mutants each having a single amino acid substitution in the HPt domain of ArcB. These ArcBc mutants were characterized and evaluated, based on the in vivo ability to signal the OmpR receiver via trans-phosphorylation.

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Keywords

Amino Acid Sequence; Anaerobiosis; Catalytic Domain; DNA Mutational Analysis; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; Phosphorylation; Protein Kinases/genetics; Signal Transduction/physiology; Structure-Activity Relationship

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