1887

Abstract

The immunological properties of ten lipoamide dehydrogenase mutants of were investigated with antiserum raised against purified lipoamide dehydrogenase. Seven mutants were CRM+ (cross-reacting material present) as they contained lipoamide dehydrogenase proteins exhibiting either complete or partial immunological identity with the wild-type protein. This indicates that at least seven of the mutations affect the lipoamide dehydrogenase structural gene (). The remaining three mutants (CRM-) contained no detectable cross-reacting protein. None of the mutations were sensitive to any of three different -suppressors. Genetic analysis by P1-transduction showed that all the mutant sites were clustered very near the distal gene () of the region which specifies the dehydrogenase () and transacetylase () components of the pyruvate dehydrogenase multienzyme complex. Calculations based on the recombination frequency between an mutant and the nearest mutant site support the conclusion that apart from the possible presence of a regulatory element, the and genes are contiguous.

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/content/journal/micro/10.1099/00221287-81-1-237
1974-03-01
2024-04-24
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References

  1. Alwine J. C., Russell F. M., Murray K. N. 1973; Characterization of an Escherichia coli mutant deficient in dihydrolipoyl dehydrogenase activity. Journal of Bacteriology 115:1–8
    [Google Scholar]
  2. Creaghan I. T., Guest J. R. 1972; Amber mutants of the α-ketoglutarate dehydrogenase gene of Escherichia coli K12. Journal of General Microbiology 71:207–220
    [Google Scholar]
  3. Flatgaard J. E., Hoehn B., Henning U. 1971; Mutants of Escherichia coli k-12 which synthesize the pyruvate dehydrogenase complex constitutively. Archives of Biochemistry and Biophysics 143:461–470
    [Google Scholar]
  4. Gasser F., Gasser C. 1971; Immunological relationships among lactic dehydrogenases in the genera Lactobacillus and Leuconostoc. Journal of Bacteriology 106:113–125
    [Google Scholar]
  5. Guest J. R. 1974; Gene-protein relationships of the α-keto acid dehydrogenase complexes of Escherichia coli K12: chromosomal location of the lipoamide dehydrogenase gene. Journal of General Microbiology 80:523–532
    [Google Scholar]
  6. Guest J. R., Creaghan I. T. 1972; Lipoamide dehydrogenase mutants of Escherichia colikI2. Biochemical Journal 130:8P
    [Google Scholar]
  7. Guest J. R., Creaghan I. T. 1973; Gene-protein relationship of the α-keto acid dehydrogenase complexes of Escherichia coli k12: isolation and characterization of lipoamide dehydrogenase mutants. Journal of General Microbiology 73:197–210
    [Google Scholar]
  8. Hayakawa T., Aikawa T., Otsuka K., Koike M. 1967; Immunochemical relationships among pig heart lipoamide dehydrogenases. Journal of Biochemistry 62:396–397
    [Google Scholar]
  9. Henning U., Dennert G., Hertel R., Shipp E. S. 1966; Translation of the structural genes of the E. coli pyruvate dehydrogenase complex. Cold Spring Harbor Symposia for Quantitative Biology 31:227–234
    [Google Scholar]
  10. Henning U., Hertz C. 1964; Ein Strukturgen-Komplex für den Pyruvat-Dehydrogenase-Komplex von Escherichia coli kI2. Zeitschrift für Vererbungslehre 95:260–275
    [Google Scholar]
  11. Herbert A. A., Guest J. R. 1968; Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and α-ketoglutarate dehydrogenase-less mutants. Journal of General Microbiology 53:363–381
    [Google Scholar]
  12. Herbert A. A., Guest J. R. 1969; Studies with α-ketoglutarate dehydrogenase mutants of Escherichia coli. Molecular and General Genetics 105:182–190
    [Google Scholar]
  13. Taylor A. L. 1970; Current linkage map of Escherichia coli. Bacteriological Reviews 34:155–175
    [Google Scholar]
  14. Vogel O., Hoehn B., Henning U. 1972; Molecular structure of the pyruvate dehydrogenase complex from Escherichia coli k-12. Proceedings of the National Academy of Sciences of the United States of America 69:1615–1619
    [Google Scholar]
  15. Wu T. T. 1966; A model for three-point analysis of random general transduction. Genetics 54:405–410
    [Google Scholar]
  16. Yanofsky C., Drapeau G. R., Guest J. R., Carlton B. C. 1967; The complete amino acid sequence of the tryptophan synthetase A protein (a subunit) and its colinear relationship with the genetic map of the A gene. Proceedings of the National Academy of Sciences of the United States of America 57:296–298
    [Google Scholar]
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