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-Å-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.
CITATION STYLE
Falke, J. J., & Hazelbauer, G. L. (2001, April 1). Transmembrane signaling in bacterial chemoreceptors. Trends in Biochemical Sciences. https://doi.org/10.1016/S0968-0004(00)01770-9
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