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Genetic mapping of a mutation affecting pyridine nucleotide transhydrogenase in Escherichia coli
Author(s) -
R.L. Hanson,
C Rose
Publication year - 1979
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.138.3.783-787.1979
Subject(s) - biology , escherichia coli , biochemistry , mutation , nicotinamide adenine dinucleotide , enzyme , nucleotide , nicotinamide adenine dinucleotide phosphate , adenosine triphosphate , nad+ kinase , microbiology and biotechnology , gene , oxidase test
A mutation, pnt-1, causing loss of pyridine nucleotide transhydrogenase activity in Escherichia coli, was mapped by assaying for the enzyme in extracts of recombinant strains produced by conjugation, F-duction, and P1 transduction. The site of this mutation was near min 35, counterclockwise from man, and it co-transduced 59% with man. The mutation was associated with loss from the cell membrane fraction of energy-independent and adenosine 5'-triphosphate-dependent transhydrogenase activities, but reduced nicotinamide adenine dinucleotide dehydrogenase activity was not affected. Strains were constructed which lack phosphoglucoisomerase (pgi-2) and which carry either pnt+ or pnt-1. Although such strains, when grown on glucose, are expected to produce a large excess of reduced nicotinamide adenine dinucleotide phosphate, the growth rate was not affected by the pnt-1 allele.

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