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Receptor structure in the bacterial sensing system.

E A Wang, D E Koshland

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1980
    PubMed
    Summary
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    Bacterial chemotaxis relies on tar and tsr genes encoding aspartate and serine receptors. These transmembrane proteins bind ligands externally and undergo methylation internally, crucial for cell signaling.

    Area of Science:

    • Microbiology
    • Molecular Biology
    • Biochemistry

    Background:

    • Bacterial chemotaxis is a fundamental process for microbial survival and adaptation.
    • Aspartate and serine receptors play a critical role in mediating chemotactic responses.
    • The tar and tsr genes encode key proteins involved in signal transduction.

    Purpose of the Study:

    • To identify and characterize the primary receptors for aspartate and serine in bacterial chemotaxis.
    • To elucidate the structural and functional properties of these receptor proteins.

    Main Methods:

    • Recombinant DNA techniques for gene product overproduction.
    • Biochemical assays for ligand binding and protein purification.
    • Immunoprecipitation using antibodies against receptor fragments.

    Related Experiment Videos

  • Reconstitution of purified receptors into artificial vesicles.

    • Main Results:

    • Overproduction of tar gene product correlated with increased aspartate binding.
    • Aspartate binding was found to copurify with the [3H]methyl-labeled tar gene product.
    • Antibody precipitation confirmed a single 60,000-dalton protein species with binding and methylation capabilities.
    • Reconstituted receptors retained aspartate binding and sensitivity to methylation/demethylation.

    Conclusions:

    • The 60,000-dalton proteins encoded by tar and tsr genes are the primary receptors for aspartate and serine.
    • These receptors are transmembrane proteins with extracellular ligand-binding sites and intracellular covalent modification sites.