Evidence for frameshift mutations in the hisH gene of Escherichia coli causing synthesis of a partially active glutamine amidotransferase.
Among eight strains carrying acridine-induced mutations in hisH, five which mapped at four different sites in the promoter-distal region of the gene showed His+ phenotypes on media containing a purine. By complementation analysis, hisH enzyme was shown to be required for growth on purines. Purine-sensitive His+ revertants of strains able to grow on purines carried second-site mutations which in one case could be shown to map in hisG. Strains able to grow on purines were able to grow on 2-thiazolyl-DL-alanine, too. We conclude that frameshift mutations in the promoter-distal part of the hisH gene of E. coli do not completely abolish the activity of the gene product.
Pons
F W
FW
Institut für Mikrobiologie, J.W. Goethe-Universität, Frankfurt am Main, Federal Republic of Germany.
Neubert
U
U
Müller
P
P
D000878:Anthranilate Synthase; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D006639:Histidine / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D019884:Nitrogenous Group Transferases; D011401:Promoter Regions, Genetic; D011687:Purines / Q000378:metabolism; D014161:Transduction, Genetic; D014166:Transferases / Q000235:genetics* / Q000378:metabolism
D011687:Purines; D006639:Histidine; D014166:Transferases; D019884:Nitrogenous Group Transferases; D000878:Anthranilate Synthase; C020655:anthranilate synthase, glutamine amidotransferase subunit