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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Phosphate flow between hybrid histidine kinases CheA₃ and CheS₃ controls Rhodospirillum centenum cyst formation
Kuang He1, Jeremiah N Marden1, Ellen M Quardokus2
1Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, United States of America.
Abstract:
Genomic and genetic analyses have demonstrated that many species contain multiple chemotaxis-like signal transduction cascades that likely control processes other than chemotaxis. The Che₃ signal transduction cascade from Rhodospirillum centenum is one such example that regulates development of dormant cysts. This Che-like cascade contains two hybrid response regulator-histidine kinases, CheA₃ and CheS₃, and a single-domain response regulator CheY₃. We demonstrate that cheS₃ is epistatic to cheA₃ and that only CheS₃∼P can phosphorylate CheY₃. We further show that CheA₃ derepresses cyst formation by phosphorylating a CheS₃ receiver domain. These results demonstrate that the flow of phosphate as defined by the paradigm E. coli chemotaxis cascade does not necessarily hold true for non-chemotactic Che-like signal transduction cascades.
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