Transmembrane signaling in bacterial chemoreceptors.
Bacterial chemoreceptors mediate chemotaxis by recognizing specific chemicals and regulating a noncovalently associated histidine kinase. Ligand binding to the external domain of the membrane-spanning receptor generates a transmembrane signal that modulates kinase activity inside the cell. This transmembrane signaling is being investigated by novel strategies, which have revealed a remarkably subtle conformational signal carried by a signaling helix that spans the entire length of the >350-A-long receptor. Multiple, independent lines of evidence indicate that, in the periplasmic and transmembrane domains, conformational signaling is a piston-type sliding of the signaling helix towards the cytoplasm.
Falke
J J
JJ
Department of Chemistry and Biochemistry, University of Colorado, 80309-0215, Boulder, CO, USA. falke@colorado.edu
Hazelbauer
G L
GL
D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins; D002462:Cell Membrane / Q000378:metabolism; D002628:Chemoreceptor Cells / Q000378:metabolism*; D015398:Signal Transduction
D001426:Bacterial Proteins