Abstract
Pyrimidine-repressible carbamyl phosphate synthetase P was synthesized in parallel with aspartate transcarbamylase during growth of Bacillus subtilis on glucose-nutrient broth. Both enzymes were inactivated at the end of exponential growth, but at different rates and by different mechanisms. Unlike the inactivation of aspartate transcarbamylase, the inactivation of carbamyl phosphate synthetase P was not interrupted by deprivation for oxygen or in a tricarboxylic acid cycle mutant. The arginine-repressible isozyme carbamyl phosphate synthetase A was synthesized in parallel with ornithine transcarbamylase during the stationary phase under these growth conditions. Again, both enzymes were subsequently inactivated, but at different rates and by apparently different mechanisms. The inactivation of carbamyl phosphate synthetase A was not affected in a protease-deficient mutatn the inactivation of ornithine transcarbamylase was greatly slowed.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Carls R. A., Hanson R. S. Isolation and characterization of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1971 Jun;106(3):848–855. doi: 10.1128/jb.106.3.848-855.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Deutscher M. P., Kornberg A. Biochemical studies of bacterial sporulation and germination. 8. Patterns of enzyme development during growth and sporulation of Baccillus subtilis. J Biol Chem. 1968 Sep 25;243(18):4653–4660. [PubMed] [Google Scholar]
- Hageman J. H., Carlton B. C. Effects of mutational loss of specific intracellular proteases on the sporulation of Bacillus subtilis. J Bacteriol. 1973 May;114(2):612–617. doi: 10.1128/jb.114.2.612-617.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maurizi M. R., Brabson J. S., Switzer R. L. Immunochemical studies of the inactivation of aspartate transcarbamylase by stationary phase Bacillus subtilis cells. Evidence for selective, energy-dependent degradation. J Biol Chem. 1978 Aug 25;253(16):5585–5593. [PubMed] [Google Scholar]
- Maurizi M. R., Switzer R. L. Apparent inactivation of inosine 5'-monophosphate dehydrogenase in sporulating Bacillus subtilis Is an artifact of in vitro proteolysis. J Bacteriol. 1975 Sep;123(3):1269–1272. doi: 10.1128/jb.123.3.1269-1272.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nelson D. L., Kornberg A. Biochemical studies of bacterial sporulation and germination. 18. Free amino acids in spores. J Biol Chem. 1970 Mar 10;245(5):1128–1136. [PubMed] [Google Scholar]
- Paulus T. J., Switzer R. L. Characterization of pyrimidine-repressible and arginine-repressible carbamyl phosphate synthetases from Bacillus subtilis. J Bacteriol. 1979 Jan;137(1):82–91. doi: 10.1128/jb.137.1.82-91.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Prescott L. M., Jones M. E. Modified methods for the determination of carbamyl aspartate. Anal Biochem. 1969 Dec;32(3):408–419. doi: 10.1016/s0003-2697(69)80008-4. [DOI] [PubMed] [Google Scholar]
- Setlow P., Primus G. Protein metabolism during germination of Bacillus megaterium spores. I. Protein synthesis and amino acid metabolism. J Biol Chem. 1975 Jan 25;250(2):623–630. [PubMed] [Google Scholar]
- Switzer R. L. The inactivation of microbial enzymes in vivo. Annu Rev Microbiol. 1977;31:135–157. doi: 10.1146/annurev.mi.31.100177.001031. [DOI] [PubMed] [Google Scholar]
- Turnbough C. L., Jr, Switzer R. L. Oxygen-dependent inactivation of glutamine phosphoribosylpyrophosphate amidotransferase in stationary-phase cultures of Bacillus subtilis. J Bacteriol. 1975 Jan;121(1):108–114. doi: 10.1128/jb.121.1.108-114.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Waindle L. M., Switzer R. L. Inactivation of aspartic transcarbamylase in sporulating Bacillus subtilis: demonstration of a requirement for metabolic energy. J Bacteriol. 1973 May;114(2):517–527. doi: 10.1128/jb.114.2.517-527.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yousten A. A., Hanson R. S. Sporulation of tricarboxylic acid cycle mutants of Bacillus subtilis. J Bacteriol. 1972 Feb;109(2):886–894. doi: 10.1128/jb.109.2.886-894.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]