Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

Phosphatase localization in bacterial chemotaxis: divergent mechanisms, convergent principles. Phys Biol 2005 Jul 14;2(3):148-58



Pubmed ID




Scopus ID

2-s2.0-26944472780   21 Citations


Chemotaxis is the process by which cells sense changes in their chemical environment and move towards more favorable conditions. In divergent species of bacteria, the chemotaxis proteins localize to the poles of the cell and information is transferred to the flagellar motors through the phosphorylation of a soluble protein CheY. Using mathematical models and computer simulation, we demonstrate that phosphatase localization controls the spatial distribution of CheY-P in the cytosol at steady state. Remarkably, the location of the phosphatase is not conserved in different species of bacteria. The sole phosphatase in Escherichia coli is localized with the signaling complex and the primary phosphatase in Bacillus subtilis is localized at the flagellar motors. Despite these alternate pathway structures, both designs minimize differences in the concentration of phosphorylated CheY proximal to each motor unlike a design where the phosphatase is freely diffusing in the cytoplasm. These results suggest that motile bacteria have evolved alternate mechanisms to ensure that each motor receives roughly the same signal at steady state. The hypothesis is that complex networks have evolved to satisfy certain design principles in order to function robustly. While specific mechanisms are different, the underlying principles of phosphatase localization in E. coli and B. subtilis appear to be the same.

Author List

Rao CV, Kirby JR, Arkin AP


John Kirby PhD Chair, Center Associate Director, Professor in the Microbiology and Immunology department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Bacillus subtilis
Bacterial Physiological Phenomena
Bacterial Proteins
Biological Transport
Escherichia coli
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins
Phosphoric Monoester Hydrolases