Space filling model of Che A protein in the CheY binding domain based on comparison of Bordetella and E. coli sequences. Amino acids 159-227 of the E. coli sequence are shown.

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Show Me the Way to Go Home Evolution of
chemotaxis proteins MCP and CheA in the
transition from a free-living to pathogenic life
style in Bordetella Christine Bezotte, Mark
Forsyth, Michael LaGier, Lorraine Olendzenski
Methyl-accepting chemotaxis (MCP) proteins vary
according to lifestyle
Background Chemotaxis in bacteria involves
methyl accepting chemotaxis receptor proteins
(MCP) that sense the attractants and repellents
in the environment and interact with a histidine
kinase CheA initiating a phosphorylation cascade
that affects flagellar rotation. Hypothesis
Proteins associated with chemotaxis will be
differentially selected in pathogenic species
compared to free-living representatives. We
compared the MCPs and CheA proteins in species of
pathogenic and a free-living Bordetella
species.
Predicted chemotaxis pathway in Bordetella
pertussis
A unique MCP among sequenced Bordetella species?
Schematic of protein interactions in bacterial
chemotaxis.
Rooted Clustal distance tree of aligned CheA
proteins generated Biology Workbench.
Space filling model of Che A protein in the CheY
binding domain based on comparison of Bordetella
and E. coli sequences. Amino acids 159-227 of
the E. coli sequence are shown.
Alignment of Che A protein from B.
bronchioseptica, B. parapertussis, B. pertussis,
B. avium, B. petrii and E. coli.