Genetics 1988-11-01

Evidence for frameshift mutations in the hisH gene of Escherichia coli causing synthesis of a partially active glutamine amidotransferase.

F W Pons, U Neubert, P Müller

Index: Genetics 120 , 657-665, (1988)

Full Text: HTML

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.

Related Compounds

Structure Name/CAS No. Articles
BETA-(2-THIAZOLYL)-DL-ALANINE Structure BETA-(2-THIAZOLYL)-DL-ALANINE
CAS:1596-65-2