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Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli

Guoyong Li, University of Massachusetts - Amherst

Abstract

How does a bacteria integrate a variety of signals received at its surface and respond with flagella rotation either in CCW or in CW? Several experimental approaches have been used to identify possible mechanism of transmembrane signaling. The different studies suggest different mechanisms of transmembrane signaling (Milburn et al., 1991; Lynch and Koshland, 1992; Chervitz and Falke, 1996; Maddock and Shapiro, 1993; Long and Weis, 1992; Liu et al., 1997; Li et al., 1997). However, most of the evidence including the one from this study either directly or indirectly points out that a receptor cluster probably serves as a working unit for signal integration and processing upon ligand binding. In this study we have observed that the level of covalent modification on the serine receptor strongly influences serine binding affinity while the receptor is in a complex. The ligand concentration dependence is construed as a change in the ligand binding affinity. Certainly, we consider that these binding affinity changes are the result of receptor covalent modification.^

Subject Area

Biology, Microbiology|Chemistry, Biochemistry|Biophysics, General

Recommended Citation

Guoyong Li, "Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli" (January 1, 2000). Doctoral Dissertations Available from Proquest. Paper AAI9988815.
http://scholarworks.umass.edu/dissertations/AAI9988815

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