1887

Abstract

Two representative lipoamide dehydrogenase mutants ( and ) were used to locate the gene in the linkage map of by conjugation and detailed transductional analysis with phage P1. Time of entry mapping indicated that the gene was between and and very close to Average cotransduction frequencies between and other markers were: (97 %), (93 %), (84 %), (71 %), (64 %), (8 to 41 %), (38 %), (21 %), (17 %) and and gal (< 1 %). These values, together with the contransduction frequencies for many other pairs of markers in this region and the results of three-factor crosses, established the gene order The very close proximity of and suggested that they may be contiguous and that the gene may be the distal gene in the pyruvate dehydrogenase operon. In this case, the expression of the gene may be governed by a secondary transcriptional promoter in the region in order to generate lipoamide dehydrogenase components for assembly of the α-ketoglutarate dehydrogenase complex. Other possible mechanisms are also discussed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-80-2-523
1974-02-01
2024-04-19
Loading full text...

Full text loading...

/deliver/fulltext/micro/80/2/mic-80-2-523.html?itemId=/content/journal/micro/10.1099/00221287-80-2-523&mimeType=html&fmt=ahah

References

  1. Beelem 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
    [Google Scholar]
  2. Brown K. D. 1970; Formation of aromatic amino acids pools in Escherichia coli k-12. Journal of Bacteriology 104:177–188
    [Google Scholar]
  3. Brown J. P., Perham R. N. 1972; An amino acid sequence in the active site of lipoamide dehydrogenase from the 2-oxoglutarate dehydrogenase complex of E. coli (Crookes strain). FEBS Letters 26:221–224
    [Google Scholar]
  4. Bukhari A. I., Taylor A. L. 1971; Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli. Journal of Bacteriology 105:844–854
    [Google Scholar]
  5. Burleigh B. D.Jun Williams C. H.Jun 1972; The isolation and primary structure of a peptide containing reduction active cystine of Escherichia coli lipoamide dehydrogenase. Journal of Biological Chemistry 247:2077–2082
    [Google Scholar]
  6. Creaghan I. T., Guest J. R. 1972; Amber mutants of the α-ketoglutarate dehydrogenase of Escherichia coliK12. Journal of General Microbiology 71:207–220
    [Google Scholar]
  7. Gholson R. K., Tritz G. J., Matney T. S., Andreoli A. J. 1969; Mode of nicotinamide adenine dinucleotide utilization by Escherichia coli. Journal of Bacteriology 99:895–896
    [Google Scholar]
  8. Guest J. R., Creaghan I. T. 1972; Lipoamide dehydrogenase mutants of Escherichia coli K12. Biochemical Journal 130:8P
    [Google Scholar]
  9. Guest J. R., Creaghan I. T. 1973; Gene-protein relationships 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]
  10. 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]
  11. Henning U., Hertz C. 1964; Ein Strukturgen-Komplex für den Pyruvat-Dehydrogenase-Komplex von Escherichia coli K12. Zeitschrift für Vererbungslehre 95:260–275
    [Google Scholar]
  12. 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]
  13. 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]
  14. Lennox E. S. 1955; Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1:190–206
    [Google Scholar]
  15. Morse D. E., Yanofsky C. 1968; The internal low-efficiency promoter of the tryptophan operon of Escherichia coli. Journal of Molecular Biology 38:447–451
    [Google Scholar]
  16. Pettit F. H., Reed L. J. 1967; α-Keto acid dehydrogenase complexes. VIII. Comparison of dihydrolipoyl dehydrogenase from pyruvate and α-ketoglutarate dehydrogenase complexes of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 58:1126–1130
    [Google Scholar]
  17. Russell R. R. B. 1970 Ph.D. Thesis University of Melbourne, Australia:
  18. Russell R. R. B. 1972; Temperature-sensitive osmotic remedial mutants of Escherichia coli. Journal of Bacteriology 112:661–665
    [Google Scholar]
  19. Taylor A. L. 1970; Current linkage map of Escherichia coli. Bacteriological Reviews 34:155–175
    [Google Scholar]
  20. Taylor A. L., Trotter C. D. 1972; Linkage map of Escherichia coli strain k-12. Bacteriological Reviews 36:504–524
    [Google Scholar]
  21. Vogel H., Bonner D. M. 1956; A convenient growth medium for E. coli and some other micro-organisms. Microbial Genetics Bulletin 13:43–44
    [Google Scholar]
  22. Wuesthoff G., Bauerle R. H. 1970; Mutations creating internal promoter elements in the tryptophan operon of Salmonella typhimurium. Journal of Molecular Biology 49:171–196
    [Google Scholar]
  23. Yura T., Wada C. 1968; Phenethyl alcohol resistance in Escherichia coli. I. Resistance of strain c6oo and its relation to azide resistance. Genetics 59:177–190
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-80-2-523
Loading
/content/journal/micro/10.1099/00221287-80-2-523
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error