The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase |
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| Authors: | Kerrie M. Jones Michael J. McPherson Andrew J. Baron Iain W. Mattaj Claudia L. Riordan John C. Wootton |
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| Affiliation: | (1) Department of Genetics, University of Leeds, LS29JT Leeds, UK;(2) Department of Biochemistry and Molecular Biology, University of Leeds, LS29JT Leeds, UK;(3) Present address: European Molecular Biology Laboratory, Meyerhofstrasse 1, W-6900 Heidelberg, Germany;(4) Present address: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, 20894 Bethesda, MD, USA |
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| Abstract: | gdhA1 is a spontaneous mutant of Escherichia coli that causes complete loss of activity of the NADP-specific glutamate dehydrogenase (GDH) encoded by the gdhA gene. The gdhA1 mutational site has been identified by recombinational mapping, polymerase chain reaction (PCR) amplification and DNA sequencing, as an A to G transition at nucleotide 274 of the gdhA coding sequence, resulting in an amino acid change of lysine 92 to glutamic acid. The mutant enzyme forms hybrid hexamers with a wild-type GDH, providing a useful system for analysis of conformational integrity of mutational variants. |
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| Keywords: | gdhA1 point mutation Deletion analysis Recombination frequency PCR DNA sequencing |
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