Hostname: page-component-848d4c4894-8kt4b Total loading time: 0 Render date: 2024-07-02T02:28:45.675Z Has data issue: false hasContentIssue false
  • English
  • Français

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 ,
W. A. Venables  and
H. J. W. Wijsman
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

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

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
Information
Genetics Research , Volume 38 , Issue 2 , October 1981 , pp. 197 - 208
Copyright
Copyright © Cambridge University Press 1981

References

REFERENCES

Beelen, R. H. J., Feldmann, A. M. & Wijsman, H. J. W. (1973). A regulatory gene and a structural gene for alaninase in Escherichia coli. Molecular and General Genetics 121, 369–374.CrossRefGoogle Scholar
Bloom, F. R. & Mcfall, E. (1975). Isolation and characterization of D-serine deaminase constitutive mutants by utilization of D-serine as sole carbon or nitrogen source. Journal of Bacteriology 121, 1078–1084.CrossRefGoogle ScholarPubMed
Bloom, F. R., Mcfall, E., Young, M. C. & Carothers, A. M. (1975). Positive control in the D-serine deaminase system of Escherichia coli K12. Journal of Bacteriology 121, 1092–1101.Google Scholar
Churchwood, G. G. & Holland, I. B. (1976). Envelope synthesis during the cell cycle in Escherichia coli B/r. Journal of Molecular Biology 105, 245–261.Google Scholar
Englesberg, E., Irr, J., Power, J. & Lee, N. (1965). Positive control of enzyme synthesis by gene C in the L-arabinose system. Journal of Bacteriology 90, 946–947.CrossRefGoogle Scholar
Franklin, F. C. H. & Venables, W. A. (1976). Biochemical, genetic and regulatory studies of alanine catabolism in Escherichia coli K12. Molecular and General Genetics 149, 229–237.Google Scholar
Hofnung, M. & Schwartz, M. (1971). Mutations allowing growth on maltose of Escherichia coli K12 strains with a deleted malT gene. Molecular and General Genetics 112, 117–132.Google Scholar
Jacob, F. & Monod, J. (1961). Genetic regulatory mechanisms in the synthesis of proteins. Journal of Molecular Biology 3, 318–356.CrossRefGoogle ScholarPubMed
Kuhn, J. & Somerville, R. L. (1971). Mutant strains of Escherichia coli K12 that utilize D-aminoacids. Proceedings of the National Academy of Science, U.S.A. 68, 2484–2487.CrossRefGoogle Scholar
Lennox, E. S. (1955). Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190–206.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle Scholar
Mcfall, E. (1964). Pleiotropic mutations in the D-serine deaminase system of Escherichia coli. Journal of Molecular Biology 9, 754–762.CrossRefGoogle ScholarPubMed
Olsiewski, P. J., Kaczorowski, G. J. & Walsh, C. (1980). Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B. Journal of Biological Chemistry 255, 4487–4494.Google Scholar
Wild, J., Walczak, W., Grynkiewicz, K.-K. & Klopotowski, T. (1973). D-amino acid dehydrogenase: the enzyme of the first step of D-histidine and D-methionine racemization in Salmonella typhimurium. Molecular and General Genetics 128, 131–146.CrossRefGoogle Scholar
Wild, J. & Klopotowski, T. (1975). Insensitivity of D-amino acid dehydrogenase synthesis to catabolic repression in dadR mutants of Salmonella typhimurium. Molecular and General Gentics 136, 63–73.Google Scholar
Wild, J., Filutowicz, M. & Klopotowski, T. (1978). Utilization of D-amino acids by dadR mutants of Salmonella typhimurium. Archives of Microbiology 118, 71–77.Google Scholar
Willson, C., Perrin, D., Cohn, M., Jacob, F. & Monod, J. (1964). Non-inducible mutants of the regulator gene in the ‘lactose’ system of Escherichia coli. Journal of Molecular Biology 8, 582–592.CrossRefGoogle ScholarPubMed