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. 1981 Oct;78(10):6038–6042. doi: 10.1073/pnas.78.10.6038

Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences.

C F Higgins, G F Ames
PMCID: PMC348972  PMID: 6273842

Abstract

The hisJ and argT genes of Salmonella typhimurium encode two periplasmic binding proteins, J and LAO, which are involved in histidine and arginine transport, respectively, and which interact with a common membrane-bound component, the P protein. The complete nucleotide sequences of these two genes have been determined. The two genes show extensive homology (70%) and presumably arose by tandem duplication of a single ancestral gene. The two encoded proteins now perform distinct functions but still retain sufficient homology to permit interaction with the same site on the membrane-bound P protein. Three lines of evidence have allowed both the amino acid-binding site and the site involved in the interaction with the P protein to be assigned to specific regions of each binding protein: (i) the distribution of amino acid differences between the two proteins; (ii) the properties of a functional chimeric protein, produced by a deletion mutant in which the first half of the argT gene is fused to the second half of the hisJ gene; (iii) the sequence change in a mutant J protein unable to interact with P.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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