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ThetrpD gene specifies a polypeptide which has both glutamine amidotransferase and phosphoribosyl anthranilate (PRA) transferase activities. Deletions fusing segments oftrpD to the gene preceding it in the operon,trpE , were selected in strains carrying varioustrpD point mutations. The selection procedure required both that a deletion entertrpE and that it restore the PRA transferase activity which the parenttrpD point mutant lacked. Deletion mutants were found which had PRA transferase activity although the first third oftrpD was deleted. The existence of the mutants proves that a terminal segment oftrpD is sufficient to specify a polypeptide having PRA transferase activity. The location of the deletion end points on the genetic map oftrpD defines the extent of thetrpD segment required for PRA transferase activity. This segment did not overlap the initial region oftrpD required to specify the glutamine amidotransferase function of thetrpD polypeptide. These results support the hypothesis (M. Grieshaber and R. Bauerle, 1972; H. Zalkin and L. H. Hwang, 1971) that the bifunctionaltrpD polypeptide might have evolved by fusion of a gene specifying a glutamine amidotransferase with a gene directing PRA transferase synthesis.

Localization of Two Functions of the Phosphoribosyl Anthranilate Transferase of Escherichia coli to Distinct Regions of the Polypeptide Chain