Mutational analysis of the histidine-containing phosphotransfer (HPt) signaling domain of the ArcB sensor in Escherichia coli.
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.
Matsushika
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A
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan.
Mizuno
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T
D000595:Amino Acid Sequence; D000693:Anaerobiosis; D020134:Catalytic Domain; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D000071677:Histidine Kinase; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics*; D015398:Signal Transduction / Q000502:physiology*; D013329:Structure-Activity Relationship