Abstract
To construct a threonine-hyperproducing strain of Serratia marcescens Sr41, the six regulatory mutations for three aspartokinases and two homoserine dehydrogenases were combined in a single strain by three transductional crosses. The constructed strain, T-1026, carried the lysC1 mutation leading to lack of feedback inhibition and repression of aspartokinase III, the thrA1(1) mutation desensitizing aspartokinase I to feedback inhibition, the thrA2(1) mutation releasing feedback inhibition of homoserine dehydrogenase I, the two hnr mutations derepressing aspartokinase I and homoserine dehydrogenase I, and the etr-1 mutation derepressing aspartokinase II and homoserine dehydrogenase II. The strain produced ca. 40 mg of threonine per ml of medium containing sucrose and urea. Furthermore, the productivity of strain T-1026 was compared with those of strains devoid of more than one of the six regulatory mutations.
Full text
PDF![1445](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/4f7ac53a52ae/aem00174-0035.png)
![1446](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/aa8141cf485c/aem00174-0036.png)
![1447](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/de33b7edb4f9/aem00174-0037.png)
![1448](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/e34af27b4ed8/aem00174-0038.png)
![1449](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/2546a37798ff/aem00174-0039.png)
![1450](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/0f15b0e347da/aem00174-0040.png)
![1451](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/e254ba73121d/aem00174-0041.png)
![1452](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df09/242483/a2b7b3027b8b/aem00174-0042.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bachmann B. J., Low K. B. Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev. 1980 Mar;44(1):1–56. doi: 10.1128/mr.44.1.1-56.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kisumi M., Komatsubara S., Chibata I. Enhancement of isoleucine hydroxamate-mediated growth inhibition and improvement of isoleucine-producing strains of Serratia marcescens. Appl Environ Microbiol. 1977 Dec;34(6):647–653. doi: 10.1128/aem.34.6.647-653.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kisumi M., Komatsubara S., Sugiura M., Chibata I. Isoleucine hydroxamate, an isoleucine antagonist. J Bacteriol. 1971 Sep;107(3):741–745. doi: 10.1128/jb.107.3.741-745.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Komatsubara S., Kisumi M., Chibata I. Participation of lysine-sensitive aspartokinase in threonine production by S-2-aminoethyl cysteine-resistant mutants of Serratia marcescens. Appl Environ Microbiol. 1979 Nov;38(5):777–782. doi: 10.1128/aem.38.5.777-782.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Komatsubara S., Kisumi M., Chibata I. Threonine production by ethionine-resistant mutants of Serratia marcescens. Appl Environ Microbiol. 1983 May;45(5):1437–1444. doi: 10.1128/aem.45.5.1437-1444.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Komatsubara S., Kisumi M., Chibata I. Transductional construction of a threonine-producing strain of Serratia marcescens. Appl Environ Microbiol. 1979 Dec;38(6):1045–1051. doi: 10.1128/aem.38.6.1045-1051.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Komatsubara S., Kisumi M., Chibata I. Transductional construction of an isoleucine-producing strain of Serratia marcescens. J Gen Microbiol. 1980 Jul;119(1):51–61. doi: 10.1099/00221287-119-1-51. [DOI] [PubMed] [Google Scholar]
- Komatsubara S., Kisumi M., Murata K., Chibata I. Threonine production by regulatory mutants of Serratia marcescens. Appl Environ Microbiol. 1978 May;35(5):834–840. doi: 10.1128/aem.35.5.834-840.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Komatsubara S., Murata K., Kisumi M., Chibata I. Threonine degradation by Serratia marcescens. J Bacteriol. 1978 Aug;135(2):318–323. doi: 10.1128/jb.135.2.318-323.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Matsumoto H., Hosogaya S., Suzuki K., Tazaki T. Arginine gene cluster of Serratia marcescens. Jpn J Microbiol. 1975 Feb;19(1):35–44. doi: 10.1111/j.1348-0421.1975.tb00845.x. [DOI] [PubMed] [Google Scholar]
- Matsumoto H., Tazaki T., Hosogaya S. A generalized transducing phage of Serratia marcescens. Jpn J Microbiol. 1973 Nov;17(6):473–479. doi: 10.1111/j.1348-0421.1973.tb00933.x. [DOI] [PubMed] [Google Scholar]
- Thèze J., Saint-Girons I. Threonine locus of Escherichia coli K-12: genetic structure and evidence for an operon. J Bacteriol. 1974 Jun;118(3):990–998. doi: 10.1128/jb.118.3.990-998.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Umbarger H. E. Amino acid biosynthesis and its regulation. Annu Rev Biochem. 1978;47:532–606. doi: 10.1146/annurev.bi.47.070178.002533. [DOI] [PubMed] [Google Scholar]
- Weiner R. M., Voll M. J., Cook T. M. Nalidixic acid for enrichment of auxotrophs in cultures of Salmonella typhimurium. Appl Microbiol. 1974 Oct;28(4):579–581. doi: 10.1128/am.28.4.579-581.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]