Analysis of chimeric chemoreceptors in Bacillus subtilis reveals a role for CheD in the function of the McpC HAMP domain. J Bacteriol 2004 Sep;186(17):5950-5
Date
08/20/2004Pubmed ID
15317802Pubmed Central ID
PMC516843DOI
10.1128/JB.186.17.5950-5955.2004Scopus ID
2-s2.0-4344663857 (requires institutional sign-in at Scopus site) 16 CitationsAbstract
Motile prokaryotes use a sensory circuit for control of the motility apparatus in which ligand-responsive chemoreceptors regulate phosphoryl flux through a modified two-component signal transduction system. The chemoreceptors exhibit a modular architecture, comprising an N-terminal sensory module, a C-terminal output module, and a HAMP domain that connects the N- and C-terminal modules and transmits sensory information between them via an unknown mechanism. The sensory circuits mediated by two chemoreceptors of Bacillus subtilis have been studied in detail. McpB is known to regulate chemotaxis towards the attractant asparagine in a CheD-independent manner, whereas McpC requires CheD to regulate chemotaxis towards the attractant proline. Although CheD is a phylogenetically widespread chemotaxis protein, there exists only a limited understanding of its function. We have constructed chimeras between McpB and McpC to probe the role of CheD in facilitating sensory transduction by McpC. We found that McpC can be converted to a CheD-independent receptor by the replacement of one-half of its HAMP domain with the corresponding sequence from McpB, suggesting that McpC HAMP domain function is complex and may require intermolecular interactions with the CheD protein. When considered in combination with the previous observation that CheD catalyzes covalent modification of the C-terminal modules of B. subtilis receptors, these results suggest that CheD may interact with chemoreceptors at multiple, functionally distinct sites.
Author List
Kristich CJ, Ordal GWAuthor
Christopher J. Kristich PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAsparagine
Bacillus subtilis
Bacterial Proteins
Chemoreceptor Cells
Chemotactic Factors
Chemotaxis
Membrane Proteins
Molecular Sequence Data
Movement
Proline
Protein Binding
Protein Structure, Tertiary
Receptors, Cell Surface
Recombinant Fusion Proteins
Sequence Alignment
