FUNCTIONAL CLONING OF THE DIHYDROPTEROATE SYNTHASE GENE OF STAPHYLOCOCCUS-HAEMOLYTICUS

A 1.7-kilobase fragment of the Staphylococcus haemolyticus chromosome containing the dihydropteroate synthase gene has been cloned by comple mentation in a temperature-sensitive mutant of Escherichia coli. The g ene, designated folP, predicts a gene product of 29613 Da which shares significant amino acid sequence identity with other known bacterial d ihydropteroate synthases. Analysis of the DNA sequence upstream and do wnstream of folP identified two further, incomplete open reading frame s, one of which shows predicted amino acid sequence similarity to a se cond bacterial folic acid synthesis enzyme, dihydroneopterin aldolase.