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. 1989 Mar;171(3):1531–1534. doi: 10.1128/jb.171.3.1531-1534.1989

Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system.

G B Cox 1, D Webb 1, H Rosenberg 1
PMCID: PMC209777  PMID: 2646285

Abstract

Three mutant alleles of the pstC gene and one mutant allele of the pstB gene were produced by site-directed mutagenesis. The pstC gene encodes an integral membrane protein of the phosphate-specific transport (Pst) system of Escherichia coli. The amino acid substitutions resulting from the pstC gene mutations, Arg-237----Gln, Glu-240----Gln, or a combination of both, caused the loss of phosphate transport through the Pst system, but the alkaline phosphatase activity remained repressed. The pstB gene encodes a peripheral membrane protein of the Pst system which carries a putative nucleotide-binding site. The amino acid substitutions Gly-48----Ile and Lys-49----Gln, resulting from the pstB mutations, caused the loss of phosphate transport through the Pst system and the derepression of alkaline phosphatase activity. The residues Gly-48 and Lys-49 are key residues in the putative nucleotide-binding site.

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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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