Abstract
The pstA gene encodes an integral membrane protein of the phosphate-specific transport system of Escherichia coli. The nucleotide change in the previously described pstA2 allele was found to be a G----A substitution at position 276 of the nucleotide sequence, resulting in the premature termination of translation. Three mutations in the pstA gene were produced by site-directed mutagenesis. The amino acid substitutions resulting from the three site-directed mutations were Arg-170----Gln, Glu-173----Gln, and Arg-220----Gln. These amino acid residues were selected because a previous PstA protein structure prediction placed them within the membrane. The Arg-220----Gln mutation resulted in the loss of phosphate transport through the phosphate-specific transport system, but the alkaline phosphatase activity remained repressed. Neither the Arg-170----Gln nor the Glu-173----Gln mutation affected phosphate transport. The results are discussed in relation to a proposed structure of the PstA protein.