Evidence for Frameshift Mutations in the Hish Gene of Escherichia Coli Causing Synthesis of a Partially Active Glutamine Amidotransferase |
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| Authors: | F. W. Pons U. Neubert P. Muller |
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| Affiliation: | Institut fur Mikrobiologie, J. W. Goethe-Universitat, Theodor-Stern-Kai 7, Haus 75A, D-6000 Frankfurt am Main, Federal Republic of Germany |
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| Abstract: | 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. |
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