Genetic analysis, structural modeling, and direct coupling analysis suggest a mechanism for phosphate signaling in Escherichia coli

Proper phosphate signaling is essential for robust growth of Escherichia coli and many other bacteria. The phosphate signal is mediated by a classic two component signal system composed of PhoR and PhoB. The PhoR histidine kinase is responsible for phosphorylating/dephosphorylating the response regu...

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Bibliographic Details
Published in:	BMC genetics Vol. 16 Suppl 2; no. S2; p. S2
Main Authors:	Gardner, Stewart G, Miller, Justin B, Dean, Tanner, Robinson, Tanner, Erickson, McCall, Ridge, Perry G, McCleary, William R
Format:	Journal Article
Language:	English
Published:	England BioMed Central 23-04-2015
Subjects:	ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Models, Molecular Phosphates - metabolism Signal Transduction Transcription Factors - chemistry Transcription Factors - metabolism
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Summary:	Proper phosphate signaling is essential for robust growth of Escherichia coli and many other bacteria. The phosphate signal is mediated by a classic two component signal system composed of PhoR and PhoB. The PhoR histidine kinase is responsible for phosphorylating/dephosphorylating the response regulator, PhoB, which controls the expression of genes that aid growth in low phosphate conditions. The mechanism by which PhoR receives a signal of environmental phosphate levels has remained elusive. A transporter complex composed of the PstS, PstC, PstA, and PstB proteins as well as a negative regulator, PhoU, have been implicated in signaling environmental phosphate to PhoR. This work confirms that PhoU and the PstSCAB complex are necessary for proper signaling of high environmental phosphate. Also, we identify residues important in PhoU/PhoR interaction with genetic analysis. Using protein modeling and docking methods, we show an interaction model that points to a potential mechanism for PhoU mediated signaling to PhoR to modify its activity. This model is tested with direct coupling analysis. These bioinformatics tools, in combination with genetic and biochemical analysis, help to identify and test a model for phosphate signaling and may be applicable to several other systems.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1471-2156 1471-2156
DOI:	10.1186/1471-2156-16-S2-S2