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. 1976 Mar;125(3):864–871. doi: 10.1128/jb.125.3.864-871.1976

Regulation of lysine transport by feedback inhibition in Saccharomyces cerevisiae.

C E Morrison, H C Lichstein
PMCID: PMC236160  PMID: 767329

Abstract

A steady-state level of about 240 nmol/mg (dry wt) occurs during lysine transport in Saccharomyces cerevisiae. No subsequent efflux of the accumulated amino acid was detected. Two transport systems mediate lysine transport, a high-affinity, lysine-specific system and an arginine-lysine system for which lysine exhibits a lower affinity. Preloading with lysine, arginine, glutamic acid, or aspartic acid inhibited lysine transport activity; preloading with glutamine, glycine, methionine, phenylalanine, or valine had little effect; however, preloading with histidine stimulated lysine transport activity. These preloading effects correlated with fluctuations in the intracellular lysine and/or arginine pool: lysine transport activity was inhibited when increases in the lysine and/or arginine pool occurred and was stimulated when decreases in the lysine and/or arginine pool occurred. After addition of lysine to a growing culture, lysine transport activity was inhibited more than threefold in one-third of the doubling time of the culture. These results indicate that the lysine-specific and arginine-lysine transport systems are regulated by feedback inhibition that may be mediated by intracellular lysine and arginine.

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Selected References

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  1. Benko P. V., Wood T. C., Segel I. H. Multiplicity and regulation of amino acid transport in Penicillium chrysogenum. Arch Biochem Biophys. 1969 Feb;129(2):498–508. doi: 10.1016/0003-9861(69)90207-0. [DOI] [PubMed] [Google Scholar]
  2. Bhattacharjee J. K., Sinha A. K. Relationship among the genes, enzymes, and intermediates of the biosynthetic pathway of lysine in Saccharomyces. Mol Gen Genet. 1972;115(1):26–30. doi: 10.1007/BF00272214. [DOI] [PubMed] [Google Scholar]
  3. Boller T., Dürr M., Wiemken A. Characterization of a specific transport system for arginine in isolated yeast vacuoles. Eur J Biochem. 1975 May;54(1):81–91. doi: 10.1111/j.1432-1033.1975.tb04116.x. [DOI] [PubMed] [Google Scholar]
  4. Crabeel M., Grenson M. Regulation of histidine uptake by specific feedback inhibition of two histidine permeases in Saccharomyces cerevisiae. Eur J Biochem. 1970 May 1;14(1):197–204. doi: 10.1111/j.1432-1033.1970.tb00278.x. [DOI] [PubMed] [Google Scholar]
  5. Dubois E. L., Grenson M. Absence of involvement of glutamine synthetase and of NAD-linked glutamate dehydrogenase in the nitrogen catabolite repression of arginase and other enzymes in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1974 Sep 9;60(1):150–157. doi: 10.1016/0006-291x(74)90185-5. [DOI] [PubMed] [Google Scholar]
  6. Dubois E., Grenson M., Wiame J. M. Release of the "ammonia effect" on three catabolic enzymes by NADP-specific glutamate dehydrogenaseless mutations in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1973 Feb 20;50(4):967–972. doi: 10.1016/0006-291x(73)91500-3. [DOI] [PubMed] [Google Scholar]
  7. Dubois E., Grenson M., Wiame J. M. The participation of the anabolic glutamate dehydrogenase in the nitrogen catabolite repression of arginase in Saccharomyces cerevisiae. Eur J Biochem. 1974 Oct 2;48(2):603–616. doi: 10.1111/j.1432-1033.1974.tb03803.x. [DOI] [PubMed] [Google Scholar]
  8. Gits J. J., Grenson M. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. 3. Evidence for a specific methionine-transporting system. Biochim Biophys Acta. 1967 Jul 3;135(3):507–516. doi: 10.1016/0005-2736(67)90040-5. [DOI] [PubMed] [Google Scholar]
  9. Grenson M., Hou C. Ammonia inhibition of the general amino acid permease and its suppression in NADPH-specific glutamate dehydrogenaseless mutants of saccharomyces cerevisiae. Biochem Biophys Res Commun. 1972 Aug 21;48(4):749–756. doi: 10.1016/0006-291x(72)90670-5. [DOI] [PubMed] [Google Scholar]
  10. Grenson M., Hou C., Crabeel M. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV. Evidence for a general amino acid permease. J Bacteriol. 1970 Sep;103(3):770–777. doi: 10.1128/jb.103.3.770-777.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Grenson M., Mousset M., Wiame J. M., Bechet J. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. I. Evidence for a specific arginine-transporting system. Biochim Biophys Acta. 1966 Oct 31;127(2):325–338. doi: 10.1016/0304-4165(66)90387-4. [DOI] [PubMed] [Google Scholar]
  12. Grenson M. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. II. Evidence for a specific lysine-transporting system. Biochim Biophys Acta. 1966 Oct 31;127(2):339–346. doi: 10.1016/0304-4165(66)90388-6. [DOI] [PubMed] [Google Scholar]
  13. Gross W., Burkhardt K. L. Multiple transport systems for basic amino acid transport in Streptomyces hydrogenans. Biochim Biophys Acta. 1973 Mar 16;298(2):437–445. doi: 10.1016/0005-2736(73)90371-4. [DOI] [PubMed] [Google Scholar]
  14. Hunter D. R., Segel I. H. Acidic and basic amino acid transport systems of Penicillium chrysogenum. Arch Biochem Biophys. 1971 May;144(1):168–183. doi: 10.1016/0003-9861(71)90466-8. [DOI] [PubMed] [Google Scholar]
  15. Hunter D. R., Segel I. H. Control of the general amino acid permease of Penicillium chrysogenum by transinhibition and turnover. Arch Biochem Biophys. 1973 Jan;154(1):387–399. doi: 10.1016/0003-9861(73)90071-4. [DOI] [PubMed] [Google Scholar]
  16. Hynes M. J. Alterations in the control of glutamate uptake in mutants of Aspergillus nidulans. Biochem Biophys Res Commun. 1973 Sep 18;54(2):685–689. doi: 10.1016/0006-291x(73)91477-0. [DOI] [PubMed] [Google Scholar]
  17. Jensen D. E., Neidhardt F. C. Effect of growth rate on histidine catabolism and histidase synthesis in Aerobacter aerogenes. J Bacteriol. 1969 Apr;98(1):131–142. doi: 10.1128/jb.98.1.131-142.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kotyk A., Ríhová L. Transport of -aminoisobutyric acid in Saccharomyces cerevisiae. Biochim Biophys Acta. 1972 Nov 2;288(2):380–389. doi: 10.1016/0005-2736(72)90259-3. [DOI] [PubMed] [Google Scholar]
  19. Kuznar J., Schwencke J., Magaña-Schwencke N. Sarcosine and imino acid uptake in Saccharomyces chevalieri. Derepression by nitrogen starvation. Biochim Biophys Acta. 1973 Aug 22;318(2):273–280. doi: 10.1016/0005-2736(73)90120-x. [DOI] [PubMed] [Google Scholar]
  20. Murphy J. T., Spence K. D. Transport of S-adenosylmethionine in Saccharomyces cerevisiae. J Bacteriol. 1972 Feb;109(2):499–504. doi: 10.1128/jb.109.2.499-504.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pall M. L. Amino acid transport in Neurospora crassa. 3. Acidic amino acid transport. Biochim Biophys Acta. 1970 Sep 15;211(3):513–520. doi: 10.1016/0005-2736(70)90256-7. [DOI] [PubMed] [Google Scholar]
  22. Pall M. L. Amino acid transport in Neurospora crassa. I. Properties of two amino acid transport systems. Biochim Biophys Acta. 1969 Jan 28;173(1):113–127. doi: 10.1016/0005-2736(69)90042-x. [DOI] [PubMed] [Google Scholar]
  23. Pall M. L. Amino acid transport in Neurospora crassa. IV. Properties and regulation of a methionine transport system. Biochim Biophys Acta. 1971 Mar 9;233(1):201–214. doi: 10.1016/0005-2736(71)90372-5. [DOI] [PubMed] [Google Scholar]
  24. Pall M. L., Kelly K. A. Specificity of transinhibition of amino acid transport in neurospora. Biochem Biophys Res Commun. 1971 Mar 5;42(5):940–947. doi: 10.1016/0006-291x(71)90521-3. [DOI] [PubMed] [Google Scholar]
  25. Pateman J. A., Kinghorn J. R., Dunn E., Forbes E. Ammonium regulation in Aspergillus nidulans. J Bacteriol. 1973 Jun;114(3):943–950. doi: 10.1128/jb.114.3.943-950.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pateman J. A., Kinghorn J. R., Dunn E. Regulatory aspects of L-glutamate transport in Aspergillus nidulans. J Bacteriol. 1974 Aug;119(2):534–542. doi: 10.1128/jb.119.2.534-542.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Ramos F., Thuriaux P., Wiame J. M., Bechet J. The participation of ornithine and citrulline in the regulation of arginine metabolism in Saccharomyces cerevisiae. Eur J Biochem. 1970 Jan;12(1):40–47. doi: 10.1111/j.1432-1033.1970.tb00818.x. [DOI] [PubMed] [Google Scholar]
  28. Ring K., Gross W., Heinz E. Negative feedback regulation of amino acid transport in Streptomyces hydrogenans. Arch Biochem Biophys. 1970 Mar;137(1):243–252. doi: 10.1016/0003-9861(70)90431-5. [DOI] [PubMed] [Google Scholar]
  29. Robinson J. H., Anthony C., Drabble W. T. Regulation of the acidic amino-acid permease of Aspergillus nidulans. J Gen Microbiol. 1973 Nov;79(1):65–80. doi: 10.1099/00221287-79-1-65. [DOI] [PubMed] [Google Scholar]
  30. Schwencke J., Magaña-Schwencke N. Derepression of a proline transport system in Saccharomyces chevalieri by nitrogen starvation. Biochim Biophys Acta. 1969 Mar 11;173(2):302–312. doi: 10.1016/0005-2736(69)90113-8. [DOI] [PubMed] [Google Scholar]
  31. Skye G. E., Segel I. H. Independent regulation of cysteine and cystine transport in Penicillium chrysogenum. Arch Biochem Biophys. 1970 May;138(1):306–318. doi: 10.1016/0003-9861(70)90311-5. [DOI] [PubMed] [Google Scholar]
  32. Subramanian K. N., Weiss R. L., Davis R. H. Use of external, biosynthetic, and organellar arginine by Neurospora. J Bacteriol. 1973 Jul;115(1):284–290. doi: 10.1128/jb.115.1.284-290.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  34. Weiss R. L. Intracellular localization of ornithine and arginine pools in Neurospora. J Biol Chem. 1973 Aug 10;248(15):5409–5413. [PubMed] [Google Scholar]
  35. Wiemken A., Dürr M. Characterization of amino acid pools in the vacuolar compartment of Saccharomyces cerevisiae. Arch Microbiol. 1974;101(1):45–57. doi: 10.1007/BF00455924. [DOI] [PubMed] [Google Scholar]

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