Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis. Mol Microbiol 2003 Mar;47(5):1353-66

Date

02/27/2003

Pubmed ID

12603740

DOI

10.1046/j.1365-2958.2003.03375.x

Scopus ID

2-s2.0-0037340214 (requires institutional sign-in at Scopus site)   32 Citations

Abstract

Escherichia coli cells use two distinct sensory circuits during chemotaxis towards carbohydrates. One circuit requires the phosphoenolpyruvate-dependent phosphotransferase system (PTS) and is independent of any specific chemoreceptor, whereas the other uses a chemoreceptor-dependent sensory mechanism analogous to that used during chemotaxis towards amino acids. Work on the carbohydrate chemotaxis sensory circuit of Bacillus subtilis reported in this article indicates that the B. subtilis circuit is different from either of those used by E. coli. Our chemotactic analysis of B. subtilis strains expressing various chimeric chemoreceptors indicates that the cytoplasmic, C-terminal module of the chemoreceptor McpC acts as a sensory-input element during carbohydrate chemotaxis. Our results also indicate that PTS-mediated carbohydrate transport, but not carbohydrate metabolism, is required for production of a chemotactic signal. We propose a model in which PTS-transport-induced chemotactic signals are transmitted to the C-terminal module of McpC for control of chemotaxis towards PTS carbohydrates.

Author List

Kristich CJ, Glekas GD, Ordal GW

Author

Christopher J. Kristich PhD 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 Proteins
Carbohydrate Metabolism
Carbohydrates
Chemotaxis
Cytoplasm
Escherichia coli
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins
Models, Molecular
Phosphoenolpyruvate Sugar Phosphotransferase System
Protein Conformation
Protein Structure, Tertiary
Recombinant Fusion Proteins
Signal Transduction
Species Specificity
Structure-Activity Relationship