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. 1973 Nov;116(2):619–626. doi: 10.1128/jb.116.2.619-626.1973

Mutant of Escherichia coli K-12 Defective in the Transport of Basic Amino Acids

T F R Celis 1, H J Rosenfeld 1, W K Maas 1
PMCID: PMC285426  PMID: 4583243

Abstract

Escherichia coli K-12 possesses two active transport systems for arginine, two for ornithine, and two for lysine. In each case there is a low- and a high-affinity transport system. They have been characterized kinetically and by response to competitive inhibition by arginine, lysine, ornithine and other structurally related amino acids. Competitors inhibit the high-affinity systems of the three amino acids, whereas the low-affinity systems are not inhibited. On the basis of kinetic evidence and competition studies, it is concluded that there is a common high-affinity transport system for arginine, ornithine, and lysine, and three low-affinity specific ones. Repression studies have shown that arginine and ornithine repress each other's specific transport systems in addition to the repression of their own specific systems, whereas lysine represses its own specific transport system. The common transport system was found to be repressible only by lysine. A mutant was studied in which the uptake of arginine, ornithine, and lysine is reduced. The mutation was found to affect both the common and the specific transport systems.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ames G. F., Lever J. E. The histidine-binding protein J is a component of histidine transport. Identification of its structural gene, hisJ. J Biol Chem. 1972 Jul 10;247(13):4309–4316. [PubMed] [Google Scholar]
  2. Anraku Y. Transport of sugars and amino acids in bacteria. 3. Studies on the restoration of active transport. J Biol Chem. 1968 Jun 10;243(11):3128–3135. [PubMed] [Google Scholar]
  3. CLARK A. J. Genetic analysis of a "double male" strain of Escherichia coli K-12. Genetics. 1963 Jan;48:105–120. doi: 10.1093/genetics/48.1.105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Hirshfield I. N., Horn P. C., Hopwood D. A., Maas W. K., DeDeken R. Studies on the mechanism of repression of arginine biosynthesis in Escherichia coli. 3. Repression of enzymes of arginine biosynthesis in arginyl-tRNA synthetase mutants. J Mol Biol. 1968 Jul 14;35(1):83–93. doi: 10.1016/s0022-2836(68)80038-5. [DOI] [PubMed] [Google Scholar]
  6. Hirshfield I. N., Rosenfeld H. J., Leifer Z., Maas W. K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J Bacteriol. 1970 Mar;101(3):725–730. doi: 10.1128/jb.101.3.725-730.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hong J. S., Ames B. N. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3158–3162. doi: 10.1073/pnas.68.12.3158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Maas W. K. Genetic defects affecting an arginine permease and repression of arginine synthesis in Escherichia coli. Fed Proc. 1965 Sep-Oct;24(5):1239–1242. [PubMed] [Google Scholar]
  9. Maas W. K. Mapping of genes involved in the synthesis of spermidine in Escherichia coli. Mol Gen Genet. 1972;119(1):1–9. doi: 10.1007/BF00270439. [DOI] [PubMed] [Google Scholar]
  10. NOVICK R. P., MAAS W. K. Control by endogenously synthesized arginine of the formation of ornithine transcarbamylase in Escherichia coli. J Bacteriol. 1961 Feb;81:236–240. doi: 10.1128/jb.81.2.236-240.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Oxender D. L. Membrane transport. Annu Rev Biochem. 1972;41(10):777–814. doi: 10.1146/annurev.bi.41.070172.004021. [DOI] [PubMed] [Google Scholar]
  12. Reid K. G., Utech N. M., Holden J. T. Multiple transport components for dicarboxylic amino acids in Streptococcus faecalis. J Biol Chem. 1970 Oct 25;245(20):5261–5272. [PubMed] [Google Scholar]
  13. Rosen B. P. Basic amino acid transport in Escherichia coli. J Biol Chem. 1971 Jun 10;246(11):3653–3662. [PubMed] [Google Scholar]
  14. Rosen B. P. Basic amino acid transport in Escherichia coli: properties of canavanine-resistant mutants. J Bacteriol. 1973 Nov;116(2):627–635. doi: 10.1128/jb.116.2.627-635.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rosen B. P., Vasington F. D. Purification and characterization of a histidine-binding protein from Salmonella typhimurium LT-2 and its relationship to the histidine permease system. J Biol Chem. 1971 Sep 10;246(17):5351–5360. [PubMed] [Google Scholar]
  16. Wilson O. H., Holden J. T. Arginine transport and metabolism in osmotically shocked and unshocked cells of Escherichia coli W. J Biol Chem. 1969 May 25;244(10):2737–2742. [PubMed] [Google Scholar]
  17. Winkler H. H., Wilson T. H. The role of energy coupling in the transport of beta-galactosides by Escherichia coli. J Biol Chem. 1966 May 25;241(10):2200–2211. [PubMed] [Google Scholar]

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