REFERENCES
- Ausubel, F. Μ., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1987. Current protocols in molecular biology, vol. 2. John Wiley & Sons, Inc., New York.
- Bai, Y., and G. B. Kohlhaw. 1991. Manipulation of the zinc cluster region of transcriptional activator Leu3 by site-directed mutagenesis. Nucleic Acids Res. 19:5991–5997.
- 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 α-isopropylmalate synthase activity and evidence that LEU1 and LEU2 gene expression is controlled by α-isopropylmalate and the product of a regulatory gene. Curr. Genet. 7:369–377.
- Brisco, P. R. G., T. S. Cunningham, and G. B. Kohlhaw. 1987. Cloning, disruption, and chromosomal mapping of yeast LEU3, a putative regulatory gene. Genetics 115:91–99.
- Brisco, P. R. G., and G. B. Kohlhaw. 1990. Regulation of yeast LEU2: total deletion of regulatory gene LEU3 unmasks GCN4- dependent basal level expression of LEU2. J. Biol. Chem. 265:11667–11675.
- Chasman, D. I., J. Leatherwood, Μ. Carey, M. Ptashne, and R. D. Kornberg. 1989. Activation of yeast polymerase II transcription by herpesvirus VP16 and GAL4 derivatives in vitro. Mol. Cell. Biol. 9:4746–4749.
- Cohen, C., and D. A. D. Parry. 1990. α-Helical coiled coils and bundles: how to design an α-helical protein. Proteins 7:1–15.
- Cress, W. D., and S. Triezenberg. 1991. Critical structural elements of the VP16 transcriptional activation domain. Science 251:87–90.
- Damm, K., C. C. Thompson, and R. Μ. Evans. 1989. Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature (London) 339:593–597.
- Friden, P., and P. Schimmel. 1988. LEU3 of Saccharomyces cerevisiae activates multiple genes for branched-chain amino acid biosynthesis by binding to a common decanucleotide core sequence. Mol. Cell. Biol. 8:2690–2697.
- Gill, G., and R. Tjian. 1992. Eukaryotic coactivators associated with the TATA box binding protein. Curr. Opin. Genet. Dev. 2:236–242.
- Hu, Y., and G. Kohlhaw. Unpublished results.
- Ito, H., Y. Fukaka, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
- Jaehning, J., and Μ. Woontner. Personal communication.
- Johnston, Μ. 1987. A model fungal gene regulatory mechanism: the GAL genes of Saccharomyces cerevisiae. Microbiol. Rev. 51:458–476.
- Kohlhaw, G. B. 1990. The leucine biosynthetic pathway in yeast: compartmentation, enzyme regulation, gene expression, p. 33–42. In Z. Barak, D. Μ. Chipman, and J. V. Schloss (ed.), Biosynthesis of branched-chain amino acids. VCH, Weinheim, Germany.
- Li, W., and F. Sherman. 1991. Two types of TATA elements for the CYC1 gene of the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 11:666–676.
- Licht, J. D., Μ. J. Grossel, J. Figge, and U. Μ. Hansen. 1990. Drosophila Krüppel protein in a transcriptional repressor. Na-ture (London) 346:76–79.
- Madden, S. L., D. Μ. Cook, J. F. Morris, A. Gashler, V. P. Sukhatme, and F. J. Rausher. 1991. Transcriptional repression by the WTl Wilms tumor gene product. Science 253:1550–1553.
- Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
- Marmorstein, R., Μ. Carey, Μ. Ptashne, and S. C. Harrison. 1992. DNA recognition by GALA: structure of a protein-DNA complex. Nature (London) 356:408–414.
- Martin, K. J., J. W. Lillie, and Μ. R. Green. 1990. Evidence for interaction of different eukaryotic transcriptional activators with distinct cellular targets. Nature (London) 346:147–152.
- Nielsen, D. A., J. Chou, A. J. Mackrell, Μ. J. Casadaban, and D. F. Steiner. 1983. Expression of a preproinsulin-β-galactosi- dase gene fusion in mammalian cells. Proc. Natl. Acad. Sci. USA 80:5198–5202.
- Parthun, Μ. R., D. A. Mangus, and J. A. Jaehning. 1992. The EGDl product, a yeast homolog of human BTF3, may be involved in GAL4 DNA binding. Mol. Cell. Biol. 12:5683–5689.
- Peters, Μ. H., J. P. Beltzer, and G. B. Kohlhaw. 1990. Expression of the yeast LEU4 gene is subject to four different modes of control. Arch. Biochem. Biophys. 276:294–298.
- Remboutsika, E. Unpublished results.
- Shi, Y∙, E. Seto, L. Chang, and T. Shenk. 1991. Transcriptional repression by YYl, a human GLI-Krüppel-related protein, and relief of repression by adenovirus Ela protein. Cell 67:377–388.
- Sze, J., and G. B. Kohlhaw. 1993. Purification and structural characterization of transcriptional regulator Leu3 of yeast. J. Biol. Chem. 268:2505–2512.
- Sze, J. 1993. The Leu3 protein: a metabolite-dependent transcriptional activator that is also a repressor. Ph.D. thesis. Purdue University, West Lafayette, Ind.
- Sze, J∙, Μ. Woontner, J. Jaehning, and G. B. Kohlhaw. 1992. In vitro transcriptional activation by a metabolic intermediate: activation by Leu3 depends on α-isopropylmalate. Science 258:1143–1145.
- Woontner, M., P. A. Wade, J. Bonner, and J∙ A. Jaehning. 1991. Transcriptional activation in an improved whole-cell extract from Saccharomyces cerevisiae. Mol. Cell. Biol. 11:4555–4560.
- Yutzey, K. E., R. L. Kline, and S. F. Konieczny. 1989. An internal regulatory element controls troponin I gene expression. Mol. Cell. Biol. 9:1397–1405.
- Yutzey, K. E., and S. F. Konieczny. 1992. Different E-box regulatory sequences are functionally distinct when placed within the context of the troponin I enhancer. Nucleic Acids Res. 20:5105–5113.
- Yutzey, K. E., S. J. Rhodes, and S. F. Konieczny. 1990. Differential trans-activation associated with the muscle regulatory factors MyoDl, myogenin, and MRF4. Mol. Cell. Biol. 10:3934–3944.
- Zhou, K. 1991. A molecular switch: structure-function study of yeast regulatory protein Leu3. Ph.D. thesis. Purdue University, West Lafayette, Ind.
- Zhou, K., Y. Bai, and G. B. Kohlhaw. 1990. Yeast regulatory protein Leu3: a structure-function analysis. Nucleic Acids Res. 18:291–298.
- Zhou, K., and G. B. Kohlhaw. 1990. Transcriptional activator Leu3 of yeast: mapping of the transcriptional activation function and significance of activation domain tryptophans. J. Biol. Chem. 265:17409–17412.