LEU3 of Saccharomyces cerevisiae Activates Multiple Genes for Branched-Chain Amino Acid Biosynthesis by Binding to a Common Decanucleotide Core Sequence

LITERATURE CITED

• Andreadis, A., Y.-P. Hsu, M. Hermodson, G. Kohlhaw, and P. Schimmel. 1984. Yeast LEV2: repression of mRNA levels by leucine and primary structure of the gene product. J. Biol. Chem. 259:8059–8062.
   PubMed Web of Science ®Google Scholar
• Armaleo, D., M. Fischer, and S. R. Gross. 1985. Effect of α-isopropylmalate on the synthesis of RNA and protein in Neurospora. Mol. Gen. Genet. 200:346–349.
   PubMedGoogle Scholar
• Arndt, K., and G. R. Fink. 1986. GCN4 protein, a positive transcription factor in yeast, binds general control promoters at all 5′ TGACTC 3′ sequences. Proc. Natl. Acad. Sci. USA 83:8516–8520.
   PubMed Web of Science ®Google Scholar
• Baichwal, V. R., T. S. Cunningham, P. R. Gatzek, and G. B. Kohlhaw. 1983. Leucine biosynthesis in yeast: identification of two genes (LEU4, LEU5) that affect alpha-isopropylmalate synthase activity and evidence that LEU1 and LEU2 gene expression is controlled by alpha-isopropylmalate and the product of a regulatory gene. Curr. Genet. 7:369–377.
   PubMed Web of Science ®Google Scholar
• Friden, P., and P. Schimmel. 1987. LEU3 of Saccharomyces cerevisiae encodes a factor for control of RNA levels of a group of leucine-specific genes. Mol. Cell. Biol. 7:2708–2717.
   PubMedGoogle Scholar
• Fried, M., and D. Crothers. 1981. Equilibrium and kinetics of lac repressor-operator interaction by polyacrylamide gel electrophoresis. Nucleic Acids Res. 9:6505–6525.
   PubMed Web of Science ®Google Scholar
• Garner, M., and A. Revzin. 1981. A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: applications to components of the E. coli lactose operon regulatory system. Nucleic Acids Res. 9:3047–3060.
   PubMed Web of Science ®Google Scholar
• Giniger, E., S. M. Varnum, and M. Ptashne. 1985. Specific DNA binding of GAL4, a positive regulatory protein of yeast. Cell 40:767–774.
   PubMed Web of Science ®Google Scholar
• Guarente, L. 1983. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol. 101:181–191.
   PubMed Web of Science ®Google Scholar
• Guarente, L. 1984. Yeast promoters: positive and negative elements. Cell 36:799–800.
   PubMed Web of Science ®Google Scholar
• Guarente, L., and T. Mason. 1983. Heme regulates transcription of the CYC1 gene of S. cerevisiae via an upstream activation site. Cell 32:1279–1286.
   PubMed Web of Science ®Google Scholar
• Hope, I. A., and K. Struhl. 1985. GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthesis in yeast. Cell 43:177–188.
   PubMed Web of Science ®Google Scholar
• Hope, I. A., and K. Struhl. 1987. GCN4, a eukaryotic transcriptional activator, binds as a dimer to target DNA. EMBO J. 6:2781–2784.
   PubMed Web of Science ®Google Scholar
• Hsu, Y.-P., G. Kohlhaw, and P. Niederberger. 1982. Evidence that alpha-isopropylmalate synthase of Saccharomyces cerevisiae is under the general control of amino acid biosynthesis. J. Bacteriol. 150:969–972.
   PubMed Web of Science ®Google Scholar
• Hsu, Y.-P., and P. Schimmel. 1984. Yeast LEV1: repression of mRNA levels by leucine and relationship of 5′-noncoding regionto that of LEW. J. Biol. Chem. 259:3714–3719.
   PubMed Web of Science ®Google Scholar
• Jones, E. W., and G. R. Fink. 1982. Regulation of amino acid and nucleotide biosynthesis in yeast, p. 181–299. In J. N. Strathem, E. W. Jones and J. R. Broach (ed.), The molecular biology of the yeast Saccharomyces: metabolism and gene expression. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Kohlhaw, G. B. 1983. Regulation of leucine biosynthesis in lower eukaryotes, p. 285–299. In K. H. Herrmann and R. L. Somerville (ed.), Amino acid biosynthesis and genetic regulation. Addison-Wesley Publishing Co., Inc., Reading, Mass.
   Google Scholar
• Laughon, A., and R. F. Gesteland. 1984. Primary structure of the Saccharomyces cerevisiae GAL4 gene. Mol. Cell. Biol. 4:260–267.
   PubMedGoogle Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Maniatis, T., S. Goodbourn, and J. A. Fischer. 1987. Regulation of inducible and tissue specific gene expression. Science 236:1237–1245.
   PubMed Web of Science ®Google Scholar
• McKnight, S., and R. Tijan. 1986. Transcriptional selectivity of viral genes in mammalian cells. Cell 46:795–805.
   PubMed Web of Science ®Google Scholar
• Messenguy, F. E., E. Dubois, and F. Descamps. 1986. Nucleotide sequence of the ARGRII regulatory gene and amino acid sequence homologies between ARGRII, PPRI and GAL4 regulatory proteins. Eur. J. Biochem. 157:77–81.
   PubMedGoogle Scholar
• Miller, J., A. D. McLachlan, and A. Klug. 1985. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 4:1609–1614.
   PubMed Web of Science ®Google Scholar
• Olshan, A. R., and S. R. Gross. 1974. Role of the leu3 cistron in the regulation of the synthesis of isoleucine and valine biosynthetic enzymes of Neurospora. J. Bacteriol. 118:374–384.
   PubMedGoogle Scholar
• Pabo, C. O., and M. Lewis. 1982. The operator-binding domain of lambda repressor: structure and DNA recognition. Nature (London) 298:443–451.
   PubMed Web of Science ®Google Scholar
• Pfeifer, K., B. Arcangioli, and L. Guarente. 1987. Yeast HAP1 activator competes with the factor RC2 for binding to the upstream activation site UAS1 of the CYC1 gene. Cell 49:9–18.
   PubMed Web of Science ®Google Scholar
• Pfeifer, K., T. Prezant, and L. Guarente. 1987. Yeast HAP1 activator binds to two upstream activation sites of different sequence. Cell 49:19–27.
   PubMedGoogle Scholar
• Polacco, J. C., and S. R. Gross. 1973. The product of the LEU3 cistron as a regulatory element for the production of the leucine biosynthetic enzymes of Neurospora. Genetics 74:443–459.
   PubMedGoogle Scholar
• Rothstein, R. 1983. One step gene disruption in yeast. Methods Enzymol. 101:202–211.
   PubMed Web of Science ®Google Scholar
• Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Siebenlist, U., and W. Gilbert. 1980. Contacts between Escherichia coli RNA polymerase and an early promoter of the phage T7. Proc. Natl. Acad. Sci. USA 77:122–126.
   PubMed Web of Science ®Google Scholar
• Struhl, K. 1987. Promoters, activator proteins and the mechanism of transcriptional initiation in yeast. Cell 49:295–297.
   PubMed Web of Science ®Google Scholar
• Takeda, Y., D. H. Ohlendorf, W. F. Anderson, and B. W. Matthews. 1983. DNA binding proteins. Science 221:1020–1026.
   PubMed Web of Science ®Google Scholar
• Thomas, J. H., N. F. Neff, and D. Botstein. 1985. Isolation and characterization of mutations in the β-tubulin gene of S. cerevisiae. Genetics 111:715–734.
   PubMedGoogle Scholar
• Umbarger, H. E. 1978. Amino acid biosynthesis and its regulation. Annu. Rev. Biochem. 47:533–606.
   Web of Science ®Google Scholar
• Von Hippel, P. H., D. G. Bear, W. D. Morgan, and J. A. McSwiggen. 1984. Protein-nucleic acid interactions in transcription: a molecular analysis. Annu. Rev. Biochem. 53:389–446.
   PubMed Web of Science ®Google Scholar
• Zhou, K., P. R. G. Brisco, A. E. Hinkkanen, and G. B. Kohlhaw. 1987. Structure of yeast regulatory gene LEU3 and evidence that LEU3 itself is under general amino acid control. Nucleic Acids Res. 13:5261–5273.
   Google Scholar