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. 1982 May;150(2):969–972. doi: 10.1128/jb.150.2.969-972.1982

Evidence that alpha-isopropylmalate synthase of Saccharomyces cerevisiae is under the "general" control of amino acid biosynthesis.

Y P Hsu, G B Kohlhaw, P Niederberger
PMCID: PMC216453  PMID: 7040348

Abstract

The specific activity and the immunoreactive amount of alpha-isopropylmalate synthase were more than three times above wild-type values in a Saccharomyces cerevisiae mutant (cdr1) with constitutively derepressed levels of enzymes known to be under the "general" control of amino acid biosynthesis. The specific activity was also higher in lysine- and arginine-leaky strains when these were grown under limiting conditions, and in wild-type cells grown in the presence of 5-methyltryptophan. A low specific activity was found in a mutant (ndr1) unable to derepress enzymes of the general control system. Neither isopropylmalate isomerase nor beta-isopropylmalate dehydrogenase responded to general control signals.

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Selected References

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

  1. Brown H. D., Satyanarayana T., Umbarger H. E. Biosynthesis of branched-chain amino acids in yeast: effect of carbon source on leucine biosynthetic enzymes. J Bacteriol. 1975 Mar;121(3):959–969. doi: 10.1128/jb.121.3.959-969.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Delforge J., Messenguy F., Wiame J. M. The regulation of arginine biosynthesis in Saccharomyces cerevisiae. The specificity of argR- mutations and the general control of amino-acid biosynthesis. Eur J Biochem. 1975 Sep 1;57(1):231–239. doi: 10.1111/j.1432-1033.1975.tb02295.x. [DOI] [PubMed] [Google Scholar]
  3. Hampsey D. M., Kohlhaw G. B. Inactivation of yeast alpha-isopropylmalate synthase by CoA. Antagonism between CoA and adenylates and the mechanism of CoA inactivation. J Biol Chem. 1981 Apr 25;256(8):3791–3796. [PubMed] [Google Scholar]
  4. Kohlhaw G. B., Hsu Y. P., Lemmon R. D., Petes T. D. Transposed LEU2 gene of Saccharomyces cerevisiae is regulated normally. J Bacteriol. 1980 Nov;144(2):852–855. doi: 10.1128/jb.144.2.852-855.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Messenguy F., Cooper T. G. Evidence that specific and "general" control of ornithine carbamoyltransferase production occurs at the level of transcription in Saccharomyces cerevisiae. J Bacteriol. 1977 Jun;130(3):1253–1261. doi: 10.1128/jb.130.3.1253-1261.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Miozzari G. F., Niederberger P., Hütter R. Permeabilization of microorganisms by Triton X-100. Anal Biochem. 1978 Oct 1;90(1):220–233. doi: 10.1016/0003-2697(78)90026-x. [DOI] [PubMed] [Google Scholar]
  7. Miozzari G., Niederberger P., Hütter R. Tryptophan biosynthesis in Saccharomyces cerevisiae: control of the flux through the pathway. J Bacteriol. 1978 Apr;134(1):48–59. doi: 10.1128/jb.134.1.48-59.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Niederberger P., Miozzari G., Hütter R. Biological role of the general control of amino acid biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol. 1981 Jul;1(7):584–593. doi: 10.1128/mcb.1.7.584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Reichenbecher V. E., Jr, Fischer M., Gross S. R. Regulation of isopropylmalate isomerase synthesis in Neurospora crassa. J Bacteriol. 1978 Feb;133(2):794–801. doi: 10.1128/jb.133.2.794-801.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ryan E. D., Tracy J. W., Kohlhaw G. B. Subcellular localization of the leucine biosynthetic enzymes in yeast. J Bacteriol. 1973 Oct;116(1):222–225. doi: 10.1128/jb.116.1.222-225.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Satyanarayana T., Umbarger H. E., Lindegren G. Biosynthesis of branched-chain amino acids in yeast: regulation of leucine biosynthesis in prototrophic and leucine auxotrophic strains. J Bacteriol. 1968 Dec;96(6):2018–2024. doi: 10.1128/jb.96.6.2018-2024.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Tracy J. W., Kohlhaw G. B. Evidence for two distinct CoA binding sites on yeast alpha-isopropylmalate synthase. J Biol Chem. 1977 Jun 25;252(12):4085–4091. [PubMed] [Google Scholar]
  13. Ulm E. H., Böhme R., Kohlhaw G. Alpha-isopropylmalate synthase from yeast: purification, kinetic studies, and effect of ligands on stability. J Bacteriol. 1972 Jun;110(3):1118–1126. doi: 10.1128/jb.110.3.1118-1126.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wolfner M., Yep D., Messenguy F., Fink G. R. Integration of amino acid biosynthesis into the cell cycle of Saccharomyces cerevisiae. J Mol Biol. 1975 Aug 5;96(2):273–290. doi: 10.1016/0022-2836(75)90348-4. [DOI] [PubMed] [Google Scholar]

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