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Genetic studies of D-alanine-dehydrogenase-less mutants of Escherichia coli K12

Published online by Cambridge University Press:  14 April 2009

F. C. H. Franklin
Affiliation:
Department of Microbiology, University College, Cardiff, U.K.
W. A. Venables
Affiliation:
Department of Microbiology, University College, Cardiff, U.K.
H. J. W. Wijsman
Affiliation:
Institute of Genetics, University of Amsterdam, Amsterdam, the Netherlands
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Genetic analysis of 12 mutants of Escherichia coli K12 defective in D-alanine dehydrogenase showed that alnA and dad are alternative names for the same locus. dad was shown to be a single gene which codes for a protein of 55000–60000 mol. wt. Study of thermosensitive mutants of dad indicated that its product is a structural component of D-alanine dehydrogenase. The regulatory gene alnR was shown to be involved in positive control of dad expression. This was concluded from (i) the absence of constitutive strains among Dad+ revertants of alnR mutations, (ii) the trans dominance of alnR+ to alnR, and (iii) the failure to isolate fully constitutive strains by any means. To obtain a uniform nomenclature it is proposed to re-name dad as dadB and alnR as dadQ.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1981

References

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