Abstract
Mutations leading to borrelidin resistance in Escherichia coli by overproduction of threonyl-transfer ribonucleic acid synthetase were anaylzed genetically. The regulatory mutations were closely linked to the treonyl-transfer ribonucleic acid synthetase structural gene (thrS), located clockwise to it. The mutation that causes the threefold-increased enzyme level was more distant from thrS than the mutation responsible for the ninefold overproduction. Both mutations were cis dominant in merodiploid strains, indicating that they affected promoter-operator-like control elements. Overproduction was restricted to threonyl-transfer ribonucleic acid synthetase and was not observed for the products of genes neighboring thrS (e.g., infC, pheS, pheT, and argS), providing evidence that thrS is transcribed singly and that gene amplificationis not a likely basis for increased thrS experession.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bachmann B. J. Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol Rev. 1972 Dec;36(4):525–557. doi: 10.1128/br.36.4.525-557.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baer M., Low K. B., Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase. J Bacteriol. 1979 Jul;139(1):165–175. doi: 10.1128/jb.139.1.165-175.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cassio D., Waller J. -P. Purification and properties of methionyl-tRNA synthetase from E. coli K 12 carrying the F32 episome. FEBS Lett. 1971 Feb 9;12(6):309–312. doi: 10.1016/0014-5793(71)80002-9. [DOI] [PubMed] [Google Scholar]
- Cheung A., Morgan S., Low K. B., Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. VI. Mutants with increased levels of glutaminyl-transfer ribonucleic acid synthetase and of glutamine transfer ribonucleic acid. J Bacteriol. 1979 Jul;139(1):176–184. doi: 10.1128/jb.139.1.176-184.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Comer M. M., Böck A. Genes for the alpha and beta subunits of the phenylalanyl-transfer ribonucleic acid synthetase of Escherichia coli. J Bacteriol. 1976 Aug;127(2):923–933. doi: 10.1128/jb.127.2.923-933.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fayerman J. T., Vann M. C., Williams L. S., Umbarger H. E. ilvU, a locus in Escherichia coli affecting the derepression of isoleucyl-tRNA synthetase and the RPC-5 chromatographic profiles of tRNAIle and tRNAVal. J Biol Chem. 1979 Oct 10;254(19):9429–9440. [PubMed] [Google Scholar]
- Folk W. R., Berg P. Duplication of the structural gene for glycyl-transfer RNA synthetase in Escherichia coli. J Mol Biol. 1971 Jun 14;58(2):595–610. doi: 10.1016/0022-2836(71)90374-3. [DOI] [PubMed] [Google Scholar]
- Grüll J. M., Hennecke H., Fröhler J., Thomale J., Nass G., Böck A. Escherichia coli mutants overproducing phenylalanyl- and threonyl-tRNA synthetase. J Bacteriol. 1979 Jan;137(1):480–489. doi: 10.1128/jb.137.1.480-489.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hennecke H., Böck A., Thomale J., Nass G. Threonyl-transfer ribonucleic acid synthetase from Escherichia coli: subunit structure and genetic analysis of the structural gene by means of a mutated enzyme and of a specialized transducing lambda bacteriophage. J Bacteriol. 1977 Sep;131(3):943–950. doi: 10.1128/jb.131.3.943-950.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hütter R., Poralla K., Zachau H. G., Zähner H. Stoffwechselprodukte von Mikroorganismen. 51. Uber die Wirkungsweise von Borrelidin-Hemmung des Threonineinbaus in sRNA. Biochem Z. 1966 Mar 28;344(2):190–196. [PubMed] [Google Scholar]
- LaRossa R. A., Mao J. I., Low K. B., Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli. III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels. J Mol Biol. 1977 Dec 25;117(4):1049–1059. doi: 10.1016/s0022-2836(77)80012-0. [DOI] [PubMed] [Google Scholar]
- Morgan S. D., Söll D. Regulation of the biosynthesis of aminoacid: tRNA ligases and of tRNA. Prog Nucleic Acid Res Mol Biol. 1978;21:181–207. doi: 10.1016/s0079-6603(08)60270-6. [DOI] [PubMed] [Google Scholar]
- Nass G., Thomale J. Alteration of structure of level of threonyl-tRNA-synthetase in Borrelidin resistant mutants of E. coli. FEBS Lett. 1974 Feb 15;39(2):182–186. doi: 10.1016/0014-5793(74)80046-3. [DOI] [PubMed] [Google Scholar]
- Neidhardt F. C., Bloch P. L., Pedersen S., Reeh S. Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol. 1977 Jan;129(1):378–387. doi: 10.1128/jb.129.1.378-387.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Neidhardt F. C., Bloch P. L., Smith D. F. Culture medium for enterobacteria. J Bacteriol. 1974 Sep;119(3):736–747. doi: 10.1128/jb.119.3.736-747.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Neihardt F. C., Parker J., McKeever W. G. Function and regulation of aminoacyl-tRNA synthetases in prokaryotic and eukaryotic cells. Annu Rev Microbiol. 1975;29:215–250. doi: 10.1146/annurev.mi.29.100175.001243. [DOI] [PubMed] [Google Scholar]
- Ny T., Thomale J., Hjalmarsson K., Nass G., Björk G. R. Non-coordinate regulation of enzymes involved in transfer RNA metabolism in Escherichia coli. Biochim Biophys Acta. 1980 Apr 30;607(2):277–284. doi: 10.1016/0005-2787(80)90080-5. [DOI] [PubMed] [Google Scholar]
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
- O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
- Paetz W., Nass G. Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12. Eur J Biochem. 1973 Jun;35(2):331–337. doi: 10.1111/j.1432-1033.1973.tb02843.x. [DOI] [PubMed] [Google Scholar]
- Piepersberg A., Hennecke H., Engelhard M., Nass G., Böck A. Cross-reactivity of phenylalanyl-transfer ribonucleic acid ligases from different microorganisms. J Bacteriol. 1975 Dec;124(3):1482–1488. doi: 10.1128/jb.124.3.1482-1488.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Springer M., Graffe M., Grunberg-Manago M. Genetic organization of the E. coli chromosome around the structural gene for initiation factor IF3 (infC). Mol Gen Genet. 1979 Feb 1;169(3):337–343. doi: 10.1007/BF00382279. [DOI] [PubMed] [Google Scholar]
- Theall G., Low K. B., Söll D. Regulation of the biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli. IV. Mutants with increased levels of leucyl- or seryl-tRNA synthetase. Mol Gen Genet. 1979 Jan 31;169(2):205–211. doi: 10.1007/BF00271672. [DOI] [PubMed] [Google Scholar]
- Thomale J., Nass G. Change of isoaccepting threonyl-tRNA and contitutively increased level of threonyl-tRNA-synthetase in E. coli. FEBS Lett. 1975 Aug 1;56(1):111–114. doi: 10.1016/0014-5793(75)80122-0. [DOI] [PubMed] [Google Scholar]
- Thomale J., Nass G. Genetically determined differences in concentrations of isoaccepting tRNAs in Escherichia coli. Nucleic Acids Res. 1977 Dec;4(12):4313–4322. doi: 10.1093/nar/4.12.4313. [DOI] [PMC free article] [PubMed] [Google Scholar]