PMID:6784119
| Citation |
Wang, EA and Koshland, DE Jr (1980) Receptor structure in the bacterial sensing system. Proc. Natl. Acad. Sci. U.S.A. 77:7157-61 |
|---|---|
| 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. |
| Links | |
| Keywords |
Aspartic Acid; Bacterial Proteins/isolation & purification; Chemotaxis; DNA, Recombinant; Escherichia coli/physiology; Genes; Macromolecular Substances; Protein Binding; Receptors, Drug/isolation & purification; Serine |
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