Abstract
The enzymatic defects in a number of Bacillus subtilis mutants of the alpha-ketoglutarate dehydrogenase complex lacking activity have been investigated. Mutants in the citK locus, as well as a series of deletions of unknown length covering the citK locus, are deficient in E1 of the complex, alpha-ketoglutarate dehydrogenase, but have normal activities of E2, dehydrolipoyl transsuccinylase, and E3, lipoamide dehydrogenase. The citK mutants and the citL22 mutant show in vitro complementation of alpha-ketoglutarate dehydrogenase complex activity. The citL22 mutant is severely deficient in lipoamide dehydrogenase activity, and, as a result, lacks activity for both the alpha-ketoglutarate and the pyruvate dehydrogenase complexes. Thus, the E3 components of both complexes are identical. The citL22 mutation maps between ura and metC on the chromosome.
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Selected References
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- Anagnostopoulos C., Spizizen J. REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS. J Bacteriol. 1961 May;81(5):741–746. doi: 10.1128/jb.81.5.741-746.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bachmann E., Allmann D. W., Green D. E. The membrane systems of the mitochondrion. I. The S fraction of the outer membrane of beef heart mitochondria. Arch Biochem Biophys. 1966 Jul;115(1):153–164. doi: 10.1016/s0003-9861(66)81051-2. [DOI] [PubMed] [Google Scholar]
- Goldstein B. J., Zahler S. A. Uptake of branched-chain alpha-keto acids in Bacillus subtilis. J Bacteriol. 1976 Jul;127(1):667–670. doi: 10.1128/jb.127.1.667-670.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Guest J. R., Creaghan I. T. Further studies with lipoamide dehydrogenase mutants of Escherichia coli K12. J Gen Microbiol. 1974 Mar;81(1):237–245. doi: 10.1099/00221287-81-1-237. [DOI] [PubMed] [Google Scholar]
- Guest J. R., Creaghan I. T. Gene-protein relationships of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and characterization of lipoamide dehydrogenase mutants. J Gen Microbiol. 1973 Mar;75(1):197–210. doi: 10.1099/00221287-75-1-197. [DOI] [PubMed] [Google Scholar]
- Guest J. R. Gene-protein relationships of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: Chromosomal location of the lipoamide dehydrogenase gene. J Gen Microbiol. 1974 Feb;80(2):523–532. doi: 10.1099/00221287-80-2-523. [DOI] [PubMed] [Google Scholar]
- Herbert A. A., Guest J. R. Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and alpha-ketoglutarate dehydrogenase-less mutants. J Gen Microbiol. 1968 Oct;53(3):363–381. doi: 10.1099/00221287-53-3-363. [DOI] [PubMed] [Google Scholar]
- Herbert A. A., Guest J. R. Studies with alpha-ketoglutarate dehydrogenase mutants of Escherichia coli. Mol Gen Genet. 1969 Oct 13;105(2):182–190. doi: 10.1007/BF00445687. [DOI] [PubMed] [Google Scholar]
- Hoch J. A., Barat M., Anagnostopoulos C. Transformation and transduction in recombination-defective mutants of Bacillus subtilis. J Bacteriol. 1967 Jun;93(6):1925–1937. doi: 10.1128/jb.93.6.1925-1937.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rutberg B., Hoch J. A. Citric acid cycle: gene-enzyme relationships in Bacillus subtilis. J Bacteriol. 1970 Nov;104(2):826–833. doi: 10.1128/jb.104.2.826-833.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Staal S. P., Hoch J. A. Conditional dihydrostreptomycin resistance in Bacillus subtilis. J Bacteriol. 1972 Apr;110(1):202–207. doi: 10.1128/jb.110.1.202-207.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tu C. L., Kaneda T. Activities of alpha-ketoisovalerate, pyruvate, and alpha-ketoglutarate dehydrogenases in a mutant of Bacillus subtilis. Can J Microbiol. 1976 Apr;22(4):592–597. doi: 10.1139/m76-088. [DOI] [PubMed] [Google Scholar]
- Zahler S. A., Korman R. Z., Rosenthal R., Hemphill H. E. Bacillus subtilis bacteriophage SPbeta: localization of the prophage attachment site, and specialized transduction. J Bacteriol. 1977 Jan;129(1):556–558. doi: 10.1128/jb.129.1.556-558.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]