Receptor structure in the bacterial sensing system.

E A Wang; D E Koshland

doi:10.1073/pnas.77.12.7157

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Receptor structure in the bacterial sensing system.

E A Wang·D E Koshland

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Abstract

The primary receptors for aspartate and serine in bacterial chemotaxis have been shown to be the 60,000-dalton proteins encoded by the tar and tsr genes. The evidence is: (i) overproduction of the tar gene product at various levels by recombinant DNA techniques produces proportionate increases in aspartate binding; (ii) aspartate binding copurifies with [3H]methyl-labeled tar gene product; (iii) antibody to tar and tsr protein fragments precipitates a single species of protein (60,000 daltons) which retains binding capacity and [3H]carboxymethyl label. Partially purified tar gene product can be reconstituted into artificial vesicles and retains aspartate binding and aspartate-sensitive methylation and demethylation. These results show that the aspartate and serine receptors are transmembrane proteins of a single polypeptide chain with the receptor recognition site on the outside of the membrane and the covalent methylation site on the inside.

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Aspartic Acid Bacterial Proteins Chemotaxis DNA, Recombinant Escherichia coli Genes Macromolecular Substances Protein Binding Receptors, Drug Serine Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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E A Wang, D E Koshland. 1980. Receptor structure in the bacterial sensing system.. https://doi.org/10.1073/pnas.77.12.7157

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