Abstract
Most strains of Bacillus subtilis, dervied from the 168 (Marburg) strain, grow slowly on aspartate as sole carbon source. We isolated a mutant (aspH) that grows rapidly on aspartate because it produces aspartase constitutively. Thus, aspartase is needed for rapid growth on aspartate, whereas aspartate-alpha-ketoglutarate aminotransferase is not needed, as was demonstrated by a mutant lacking that enzyme activity. By two--and three-factor crosses using PBSl transduction, the aspH mutation was located between the aroD and the lys markers of the genetic map. Although sodium ions do not affect growth on glucose or L-malate, they specifically stimulate growth on aspartate in both the parent and the aspH mutant strains. Enzyme activities of crude aspartase and fumarase and of purified aspartase do not increase in the presence of sodium. These results show that stimulation by sodium involves some reaction other than the enzymes catabolizing aspartate. The ease of purification from the aspH strain and the stability of aspartase suggest that the B. subtilis enzyme is particularly useful for aspartate determinations.
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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]
- Frank L., Hopkins I. Sodium-stimulated transport of glutamate in Escherichia coli. J Bacteriol. 1969 Oct;100(1):329–336. doi: 10.1128/jb.100.1.329-336.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HALPERN Y. S., UMBARGER H. E. Conversion of ammonia to amino groups in Escherichia coli. J Bacteriol. 1960 Sep;80:285–288. doi: 10.1128/jb.80.3.285-288.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Halpern Y. S., Barash H., Dover S., Druck K. Sodium and potassium requirements for active transport of glutamate by Escherichia coli K-12. J Bacteriol. 1973 Apr;114(1):53–58. doi: 10.1128/jb.114.1.53-58.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirata H., Kosmakos F. C., Brodie A. F. Active transport of proline in membrane preparations from Mycobacterium phlei. J Biol Chem. 1974 Nov 10;249(21):6965–6970. [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]
- Miner K. M., Frank L. Sodium-stimulated glutamate transport in osmotically shocked cells and membrane vesicles of Escherichia coli. J Bacteriol. 1974 Mar;117(3):1093–1098. doi: 10.1128/jb.117.3.1093-1098.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- RACKER E. Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids. Biochim Biophys Acta. 1950 Jan;4(1-3):211–214. doi: 10.1016/0006-3002(50)90026-6. [DOI] [PubMed] [Google Scholar]
- SAITO H., MIURA K. I. PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT. Biochim Biophys Acta. 1963 Aug 20;72:619–629. [PubMed] [Google Scholar]
- Sterlini J. M., Mandelstam J. Commitment to sporulation in Bacillus subtilis and its relationship to development of actinomycin resistance. Biochem J. 1969 Jun;113(1):29–37. doi: 10.1042/bj1130029. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takahashi I. Joint transfer of genetic markers in Bacillus subtilis. J Bacteriol. 1966 Jan;91(1):101–105. doi: 10.1128/jb.91.1.101-105.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williams V. R., Lartigue D. J. Quaternary structure and certain allosteric properties of aspartase. J Biol Chem. 1967 Jun 25;242(12):2973–2978. [PubMed] [Google Scholar]