Phosphatase localization in bacterial chemotaxis: divergent mechanisms, convergent principles. Phys Biol 2005 Jul 14;2(3):148-58
Date
10/15/2005Pubmed ID
16224120DOI
10.1088/1478-3975/2/3/002Scopus ID
2-s2.0-26944472780 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
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 APAuthor
John Kirby PhD Chair, Center Associate Director, Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Bacillus subtilisBacteria
Bacterial Physiological Phenomena
Bacterial Proteins
Biological Transport
Chemotaxis
Escherichia coli
Escherichia coli Proteins
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins
Phosphoric Monoester Hydrolases
Phosphorylation