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. 1984 Mar;4(3):520–528. doi: 10.1128/mcb.4.3.520

Temporal analysis of general control of amino acid biosynthesis in Saccharomyces cerevisiae: role of positive regulatory genes in initiation and maintenance of mRNA derepression.

M D Penn, G Thireos, H Greer
PMCID: PMC368731  PMID: 6325881

Abstract

In Saccharomyces cerevisiae, starvation for a single amino acid results in the derepression of enzyme activities in multiple amino acid biosynthetic pathways. Derepression is a consequence of increased transcription of the genes encoding these enzymes. Analysis of the kinetics of mRNA elevation established that derepression occurs within 5 min of a shift of the culture from rich medium to starvation medium. Any starvation condition was sufficient to trigger an initial high mRNA elevation; however, it was the severity of starvation which determined the steady-state mRNA levels that were subsequently established. The products of the positive regulatory genes AAS101, AAS103, and AAS2 were shown to be required in the initiation phase of this response, whereas the AAS102 gene product was required to maintain the new elevated steady-state mRNA levels. The AAS101 and AAS102 genes were cloned. Consistent with their respective roles in initiation and maintenance of derepression. AAS101 mRNA was found to be expressed at high levels in both rich and starvation media, whereas AAS102 mRNA was derepressed only under starvation conditions. The derepression of AAS102 mRNA is dependent on the AAS101 gene product.

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Selected References

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

  1. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bonven B., Gulløv K. Peptide chain elongation rate and ribosomal activity in Saccharomyces cerevisiae as a function of the growth rate. Mol Gen Genet. 1979 Feb 26;170(2):225–230. doi: 10.1007/BF00337800. [DOI] [PubMed] [Google Scholar]
  3. Botstein D., Falco S. C., Stewart S. E., Brennan M., Scherer S., Stinchcomb D. T., Struhl K., Davis R. W. Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments. Gene. 1979 Dec;8(1):17–24. doi: 10.1016/0378-1119(79)90004-0. [DOI] [PubMed] [Google Scholar]
  4. Boyer H. W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J Mol Biol. 1969 May 14;41(3):459–472. doi: 10.1016/0022-2836(69)90288-5. [DOI] [PubMed] [Google Scholar]
  5. Clarke L., Carbon J. Functional expression of cloned yeast DNA in Escherichia coli: specific complementation of argininosuccinate lyase (argH) mutations. J Mol Biol. 1978 Apr 25;120(4):517–532. doi: 10.1016/0022-2836(78)90351-0. [DOI] [PubMed] [Google Scholar]
  6. Cryer D. R., Eccleshall R., Marmur J. Isolation of yeast DNA. Methods Cell Biol. 1975;12:39–44. doi: 10.1016/s0091-679x(08)60950-4. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Donahue T. F., Daves R. S., Lucchini G., Fink G. R. A short nucleotide sequence required for regulation of HIS4 by the general control system of yeast. Cell. 1983 Jan;32(1):89–98. doi: 10.1016/0092-8674(83)90499-3. [DOI] [PubMed] [Google Scholar]
  9. Donahue T. F., Farabaugh P. J., Fink G. R. The nucleotide sequence of the HIS4 region of yeast. Gene. 1982 Apr;18(1):47–59. doi: 10.1016/0378-1119(82)90055-5. [DOI] [PubMed] [Google Scholar]
  10. Gainer H., Barker J. L., Wollberg Z. Preferential incorporation of extracellular amino acids into neuronal proteins. J Neurochem. 1975 Aug;25(2):177–179. doi: 10.1111/j.1471-4159.1975.tb12246.x. [DOI] [PubMed] [Google Scholar]
  11. Gehrke L., Ilan J. Preferential utilization of exogenously supplied leucine for protein synthesis in estradiol-induced and uninduced cockerel liver explants. Proc Natl Acad Sci U S A. 1983 Jun;80(11):3274–3278. doi: 10.1073/pnas.80.11.3274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gross K. J., Pogo A. O. Control mechanism of ribonucleic acid synthesis in eukaryotes. The effect of amino acid and glucose starvation and cycloheximide on yeast deoxyribonucleic acid-dependent ribonucleic acid polymerases. J Biol Chem. 1974 Jan 25;249(2):568–576. [PubMed] [Google Scholar]
  13. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hinnebusch A. G., Fink G. R. Positive regulation in the general amino acid control of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1983 Sep;80(17):5374–5378. doi: 10.1073/pnas.80.17.5374. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hinnebusch A. G., Fink G. R. Repeated DNA sequences upstream from HIS1 also occur at several other co-regulated genes in Saccharomyces cerevisiae. J Biol Chem. 1983 Apr 25;258(8):5238–5247. [PubMed] [Google Scholar]
  16. Hinnen A., Hicks J. B., Fink G. R. Transformation of yeast. Proc Natl Acad Sci U S A. 1978 Apr;75(4):1929–1933. doi: 10.1073/pnas.75.4.1929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ilan J., Ilan J. Preferential channeling of exogenously supplied methionine into protein by sea urchin embryos. J Biol Chem. 1981 Mar 25;256(6):2830–2834. [PubMed] [Google Scholar]
  18. Klopotowski T., Wiater A. Synergism of aminotriazole and phosphate on the inhibition of yeast imidazole glycerol phosphate dehydratase. Arch Biochem Biophys. 1965 Dec;112(3):562–566. doi: 10.1016/0003-9861(65)90096-2. [DOI] [PubMed] [Google Scholar]
  19. Mandel M., Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970 Oct 14;53(1):159–162. doi: 10.1016/0022-2836(70)90051-3. [DOI] [PubMed] [Google Scholar]
  20. Messenguy F., Colin D., ten Have J. P. Regulation of compartmentation of amino acid pools in Saccharomyces cerevisiae and its effects on metabolic control. Eur J Biochem. 1980 Jul;108(2):439–447. doi: 10.1111/j.1432-1033.1980.tb04740.x. [DOI] [PubMed] [Google Scholar]
  21. Messenguy F. Concerted repression of the synthesis of the arginine biosynthetic enzymes by aminoacids: a comparison between the regulatory mechanisms controlling aminoacid biosyntheses in bacteria and in yeast. Mol Gen Genet. 1979 Jan 16;169(1):85–95. doi: 10.1007/BF00267549. [DOI] [PubMed] [Google Scholar]
  22. Messenguy F., Delforge J. Role of transfer ribonucleic acids in the regulation of several biosyntheses in Saccharomyces cerevisiae. Eur J Biochem. 1976 Aug 16;67(2):335–339. doi: 10.1111/j.1432-1033.1976.tb10696.x. [DOI] [PubMed] [Google Scholar]
  23. Messenguy F., Dubois E. Participation of transcriptional and post-transcriptional regulatory mechanisms in the control of arginine metabolism in yeast. Mol Gen Genet. 1983;189(1):148–156. doi: 10.1007/BF00326068. [DOI] [PubMed] [Google Scholar]
  24. Meussdoerffer F., Fink G. R. Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae. J Biol Chem. 1983 May 25;258(10):6293–6299. [PubMed] [Google Scholar]
  25. Miozzari G., Niederberger P., Hütter R. Action of tryptophan analogues in Saccharomyces cerevisiae. Arch Microbiol. 1977 Dec 15;115(3):307–316. doi: 10.1007/BF00446457. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Moat A. G., Ahmad F., Alexander J. K., Barnes I. J. Alteration in the amino acid content of yeast during growth under various nutritional conditions. J Bacteriol. 1969 May;98(2):573–578. doi: 10.1128/jb.98.2.573-578.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Nasmyth K. A., Reed S. I. Isolation of genes by complementation in yeast: molecular cloning of a cell-cycle gene. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2119–2123. doi: 10.1073/pnas.77.4.2119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. 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]
  30. Penn M. D., Galgoci B., Greer H. Identification of AAS genes and their regulatory role in general control of amino acid biosynthesis in yeast. Proc Natl Acad Sci U S A. 1983 May;80(9):2704–2708. doi: 10.1073/pnas.80.9.2704. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Petersen N. S., McLaughlin C. S., Nierlich D. P. Half life of yeast messenger RNA. Nature. 1976 Mar 4;260(5546):70–72. doi: 10.1038/260070a0. [DOI] [PubMed] [Google Scholar]
  32. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  33. Rytka J. Positive selection of general amino acid permease mutants in Saccharomyces cerevisiae. J Bacteriol. 1975 Feb;121(2):562–570. doi: 10.1128/jb.121.2.562-570.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Schürch A., Miozzari J., Hütter R. Regulation of tryptophan biosynthesis in Saccharomyces cerevisiae: mode of action of 5-methyl-tryptophan and 5-methyl-tryptophan-sensitive mutants. J Bacteriol. 1974 Mar;117(3):1131–1140. doi: 10.1128/jb.117.3.1131-1140.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Silverman S. J., Rose M., Botstein D., Fink G. R. Regulation of HIS4-lacZ fusions in Saccharomyces cerevisiae. Mol Cell Biol. 1982 Oct;2(10):1212–1219. doi: 10.1128/mcb.2.10.1212. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Sripati C. E., Warner J. R. Isolation, characterization, and translation of mRNA from yeast. Methods Cell Biol. 1978;20:61–81. doi: 10.1016/s0091-679x(08)62009-9. [DOI] [PubMed] [Google Scholar]
  37. Stinchcomb D. T., Mann C., Davis R. W. Centromeric DNA from Saccharomyces cerevisiae. J Mol Biol. 1982 Jun 25;158(2):157–190. doi: 10.1016/0022-2836(82)90427-2. [DOI] [PubMed] [Google Scholar]
  38. Struhl K., Davis R. W. Transcription of the his3 gene region in Saccharomyces cerevisiae. J Mol Biol. 1981 Nov 5;152(3):535–552. doi: 10.1016/0022-2836(81)90267-9. [DOI] [PubMed] [Google Scholar]
  39. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Wahl G. M., Stern M., Stark G. R. Efficient transfer of large DNA fragments from agarose gels to diazobenzyloxymethyl-paper and rapid hybridization by using dextran sulfate. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3683–3687. doi: 10.1073/pnas.76.8.3683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Walz A., Ratzkin B., Carbon J. Control of expression of a cloned yeast (Saccharomyces cerevisiae) gene (trp5) by a bacterial insertion element (IS2). Proc Natl Acad Sci U S A. 1978 Dec;75(12):6172–6176. doi: 10.1073/pnas.75.12.6172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Watson T. G. Amino-acid pool composition of Saccharomyces cerevisiae as a function of growth rate and amino-acid nitrogen source. J Gen Microbiol. 1976 Oct;96(2):263–268. doi: 10.1099/00221287-96-2-263. [DOI] [PubMed] [Google Scholar]
  43. 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]
  44. Wieslander L. A simple method to recover intact high molecular weight RNA and DNA after electrophoretic separation in low gelling temperature agarose gels. Anal Biochem. 1979 Oct 1;98(2):305–309. doi: 10.1016/0003-2697(79)90145-3. [DOI] [PubMed] [Google Scholar]
  45. 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]
  46. Zalkin H., Yanofsky C. Yeast gene TRP5: structure, function, regulation. J Biol Chem. 1982 Feb 10;257(3):1491–1500. [PubMed] [Google Scholar]

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