Isolation and Characterization of Mutations in the HXK2 Gene of Saccharomyces cerevisiae

LITERATURE CITED

• Alber, T., M. G. Grutter, T. M. Gray, J. A. Wozniak, L. H. Weaver, B.-L. Chen, E. N. Baker, and B. W. Matthews. 1986. Structure and stability of mutant lysozymes from bacteriophage T4. UCLA Symp. Mol. Cell. Biol. New Ser. 39:307–318.
   Google Scholar
• Alber, T., D. Sun, J. A. Nye, D. C. Muchmore, and B. W. Matthews. 1987. Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein. Biochemistry 26:3754–3758.
   PubMed Web of Science ®Google Scholar
• Alber, T., D. Sun, K. Wilson, J. A. Wozniak, S. P. Cook, and B. W. Matthews. 1987. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature (London) 330:41–46.
   PubMed Web of Science ®Google Scholar
• Anderson, C. M., R. C. McDonald, and T. A. Steitz. 1978. Sequencing a protein by X-ray crystallography. I. Interpretation of yeast hexokinase B at 2.5 A resolution by model building. J. Mol. Biol. 123:1–13.
   PubMed Web of Science ®Google Scholar
• Anderson, C. M., R. E. Stenkamp, R. C. McDonald, and T. A. Steitz. 1978. A refined model of the sugar binding site of yeast hexokinase B. J. Mol. Biol. 123:207–219.
   PubMed Web of Science ®Google Scholar
• Anderson, C. M., R. E. Stenkamp, and T. A. Steitz. 1978. Sequencing a protein by X-ray crystallography. II. Refinement of yeast hexokinase B co-ordinates and sequence at 2.1 A resolution. J. Mol. Biol. 123:15–33.
   PubMed Web of Science ®Google Scholar
• Bennett, W. S., Jr., and T. A. Steitz. 1978. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. USA 75:4848–4852.
   PubMed Web of Science ®Google Scholar
• Bennett, W. S., Jr., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5 A resolution. J. Mol. Biol. 140:183–209.
   PubMed Web of Science ®Google Scholar
• Bennett, W. S., Jr., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparison of conformation and active site configuration with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:211–230.
   PubMed Web of Science ®Google Scholar
• Bergmeyer, H. U. (ed.). 1973. p. 473–474. Methods of enzymatic analysis, 2nd ed. Verlag Chemie, Weinheim, Federal Republic of Germany.
   Google Scholar
• Borders, C. L., Jr., K. L. Cipollo, J. F. Jorkasky, and K. E. Neet. 1978. Role of arginyl residues in yeast hexokinase PII. Biochemistry 17:2654–2658.
   PubMedGoogle Scholar
• Botstein, D., S. C. Falco, S. Stewart, M. Brennan, S. Sherer, D. Stinchcomb, K. Struhl, and R. W. Davis. 1979. Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments. Gene 8:17–24.
   PubMed Web of Science ®Google Scholar
• Boyer, H. W., and D. Roulland-Dussoix. 1969. A complementation analysis of the restriction and modification of DNA in E. coli. J. Mol. Biol. 41:458–472.
   Google Scholar
• Broach, J. R.. 1983. Construction of high copy yeast vectors using 2-μιη circle sequences. Methods Enzymol. 101:307–325.
   PubMedGoogle Scholar
• Burnette, W. N.. 1981. “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacryla- mide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195–203.
   PubMed Web of Science ®Google Scholar
• Carlson, M., B. C. Osmond, and D. Botstein. 1981. Mutants of yeast defective in sucrose utilization. Genetics 98:25–40.
   PubMed Web of Science ®Google Scholar
• CoIowick, S. P.. 1973. The hexokinases, p. 1–48. In P. D. Boyer (ed.), The enzymes, 3rd ed., vol. 9. Academic Press, Inc., New York.
   Google Scholar
• Cox, E. C., and D. L. Homer. 1982. Dominant mutators in Escherichia coli. Genetics 100:7–18.
   PubMed Web of Science ®Google Scholar
• Degnen, G. E., and E. C. Cox. 1974. Conditional mutator gene in Escherichia coli: isolation, mapping and effector studies. J. Bacteriol. 117:477–487.
   PubMed Web of Science ®Google Scholar
• Derechin, M., A. Ramel, N. R. Lazarus, and E. A. Barnard. 1966. Yeast hexokinase. II. Molecular weight and dissociation behavior. Biochemistry 5:4017–4025.
   Web of Science ®Google Scholar
• Derechin, M., Y. M. Rustum, and E. A. Barnard. 1972. Dissociation of yeast hexokinase under the influence of substrate. Biochemistry 11:1793–1797.
   PubMedGoogle Scholar
• Easterby, J. S., and M. A. Rosemeyer. 1972. Purification and subunit interactions of yeast hexokinase. Eur. J. Biochem. 28:241–252.
   PubMedGoogle Scholar
• Entian, K.-D.. 1980. Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in catabolite repression in yeast. Mol. Gen. Genet. 178:633–637.
   PubMedGoogle Scholar
• Entian, K.-D., and K.-U. Frohlich. 1984. Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering catabolite repression. J. Bacteriol. 158:29–35.
   PubMed Web of Science ®Google Scholar
• Entian, K.-D., E. Kopetzki, K. U. Frohlich, and D. Mecke. 1984. Cloning of hexokinase isoenzyme PI from Saccharomyces cerevisiae: PI transformants confirm the unique role of hexokinase isoenzyme PII for glucose repression in yeast. Mol. Gen. Genet. 198:50–54.
   PubMedGoogle Scholar
• Fowler, R. G., G. E. Degnen, and E. C. Cox. 1974. Mutational specificity of a conditional Escherichia coli mutator, mutD5. Mol. Gen. Genet. 133:179–191.
   PubMedGoogle Scholar
• Fraenkel, D. G.. 1986. Mutants in glucose metabolism. Annu. Rev. Biochem. 55:317–337.
   PubMedGoogle Scholar
• Frohlich, K.-U., K.-D. Entian, and D. Mecke. 1984. Cloning and restriction analysis of the hexokinase PII gene of the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 194:144–148.
   PubMedGoogle Scholar
• Frohlich, K.-U., K.-D. Entian, and D. Mecke. 1985. The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression. Gene 36:105–111.
   PubMed Web of Science ®Google Scholar
• Goldstein, A., and J. O. Lampen. 1975. β-D-Fructofuranoside fructohydrolase from yeast. Methods Enzymol. 42C:504–511.
   Google Scholar
• Grutter, M. G., T. M. Gray, L. H. Weaver, T. Alter, K. Wilson, and B. W. Matthews. 1987. Structural studies of mutants of the lysozyme of bacteriophage T4: the temperature-sensitive mutant protein Thr157→Ile. J. Mol. Biol. 197:315–329.
   PubMedGoogle Scholar
• Grutter, M. G., R. B. Hawkes, and B. W. Matthews. 1979. Molecular basis of thermostability in the lysozyme from bacteriophage T4. Nature (London) 277:667–669.
   PubMed Web of Science ®Google Scholar
• Grutter, M. G., L. H. Weaver, T. M. Gray, and B. W. Matthews. 1983. Structure, function, and evolution of the lysozyme from bacteriophage T4, p. 356–360. In C. K. Matthews, E. M. Kutter, G. Mosig, and P. B. Berget (ed.), Bacteriophage T4. American Society for Microbiology, Washington, D.C.
   Google Scholar
• Haltiner, M., T. Kempe, and R. Tjian. 1985. A novel strategy for constructing clustered point mutations. Nucleic Acids Res. 13:1015–1025.
   PubMedGoogle Scholar
• Hecht, M. H., H. C. M. Nelson, and R. T. Sauer. 1983. Mutations in λ repressor's amino terminal domain: implications for protein stability and DNA binding. Proc. Natl. Acad. Sci. USA 80:2676–2680.
   PubMed Web of Science ®Google Scholar
• Hecht, N. H., J. M. Sturtevant, and R. T. Sauer. 1984. Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage λ repressor. Proc. Natl. Acad. Sci. USA 81:5685–5689.
   PubMedGoogle Scholar
• Hoffman, C. S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267–272.
   PubMed Web of Science ®Google Scholar
• Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Kopetzki, E., K.-D. Entian, and D. Mecke. 1985. Complete nucleotide sequence of the hexokinase PI gene (HXK1) of Saccharomyces cerevisiae. Gene 39:95–102.
   PubMedGoogle Scholar
• Korneluk, R. G., F. Quan, and R. A. Gravel. 1985. Rapid and reliable dideoxy sequencing of double stranded DNA. Gene 64:317–323.
   Google Scholar
• Kunes, S., H. Ma, K. Overbye, M. S. Fox, and D. Botstein. 1987. Fine structure recombinational analysis of cloned genes using yeast transformation. Genetics 115:73–81.
   PubMedGoogle Scholar
• Kuo, C., and J. L. Campbell. 1983. Cloning of Saccharomyces cerevisiae DNA replication genes: isolation of the CDC8 gene and two genes that compensate for the cdc8-1 mutation. Mol. Cell. Biol. 3:1730–1337.
   PubMedGoogle Scholar
• Lobo, Z., and P. K. Maitra. 1977. Genetics of yeast hexokinases. Genetics 86:727–744.
   PubMed Web of Science ®Google Scholar
• Lobo, Z., and P. K. Maitra. 1977. Physiological role of glucose-phosphorylating enzymes in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 182:639–645.
   PubMedGoogle Scholar
• Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.
   PubMed Web of Science ®Google Scholar
• Ma, H., L. M. Bloom, C. T. Walsh, and D. Botstein. 1989. The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:5643–5649.
   PubMedGoogle Scholar
• Ma, H., and D. Botstein. 1986. Effects of null mutations in the hexokinase genes of Saccharomyces cerevisiae on catabolite repression. Mol. Cell. Biol. 6:4046–4052.
   PubMed Web of Science ®Google Scholar
• Ma, H., S. Kunes, P. J. Schatz, and D. Botstein. 1987. Plasmid construction by homologous recombination in yeast. Gene 58:201–216.
   PubMed Web of Science ®Google Scholar
• Maitra, P. K.. 1975. Glucokinase from yeast. Methods Enzymol. 42:25–30.
   PubMedGoogle Scholar
• Maitra, P. K., and Z. Lobo. 1983. Genetics of yeast glucokinase. Genetics 105:501–515.
   PubMedGoogle Scholar
• McDonald, R. C., T. A. Steitz, and D. M. Engelman. 1979. Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose-6-phosphate. Biochemistry 18:338–342.
   PubMed Web of Science ®Google Scholar
• Muratsubaki, H., and T. Katsume. 1979. Distribution of hexokinase isoenzymes depending on a carbon source in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 86:1030–1036.
   PubMedGoogle Scholar
• Neff, N. F., J. H. Thomas, P. Grisafi, and D. Botstein. 1983. Isolation of the β-tubulin gene from yeast and demonstration of its essential function in vivo. Cell 33:211–219.
   PubMed Web of Science ®Google Scholar
• Nelson, H. C. M., and R. T. Sauer. 1986. Interaction of mutant λ repressors with operator and non-operator DNA. J. Mol. Biol. 192:27–38.
   PubMedGoogle Scholar
• Otieno, S., A. K. Bhargava, D. Serelis, and E. A. Barnard. 1977. Evidence for a single essential thiol in the yeast hexokinase molecule. Biochemistry 16:4249–4255.
   PubMedGoogle Scholar
• Pakula, A. A., V. B. Young, and R. T. Sauer. 1986. Bacteriophage λ cro mutations: effects on activity and intracellular degradation. Proc. Natl. Acad. Sci. USA 83:8829–8833.
   PubMedGoogle Scholar
• Philips, M., D. B. Pho, and L.-A. Pradel. 1979. An essential arginyl residue in yeast hexokinase. Biochim. Biophys. Acta 566:296–304.
   PubMedGoogle Scholar
• Pho, D. B., C. Roustan, A. N. T. Tot, and L.-A. Pradel. 1977. Evidence for an essential glutamyl residue in yeast hexokinase. Biochemistry 16:4533–4537.
   PubMedGoogle Scholar
• Punch, D. L., H. J. Fromm, and F. B. Rudolph. 1973. The hexokinases: kinetic, physical, and regulatory properties. Adv. Enzymol. 39:249–326.
   PubMedGoogle Scholar
• Rose, M., and D. Botstein. 1983. Structure and function of the yeast URA3 gene. Differentially regulated expression of hybrid β-galactosidase from overlapping coding sequences in yeast. J. Mol. Biol. 170:883–904.
   PubMedGoogle Scholar
• Rose, M., P. Grisafi, and D. Botstein. 1984. Structure and function of the yeast URA3 gene: expression in Escherichia coli. Gene 29:113–124.
   PubMedGoogle Scholar
• Rose, M., and F. Winston. 1984. Identification of a Ty insertion within the coding sequence of the S. cerevisiae URA3 gene. Mol. Gen. Genet. 193:557–560.
   PubMedGoogle Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Sherman, F., G. R. Fink, and C. W. Lawrence. 1978. Laboratory manual for a course, methods in yeast genetics, revised ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Shortle, D., P. Grisafi, S. J. Benkovic, and D. Botstein. 1982. Gap misrepair mutagenesis: efficient site-directed induction of tran sition, trans version, and frameshift mutations in vitro. Proc. Natl. Acad. Sci. USA 79:1588–1592.
   PubMed Web of Science ®Google Scholar
• Stachelek, C., J. Stachelek, J. Swan, D. Botstein, and W. Konigsberg. 1986. Identification, cloning and sequence determination of genes specifying hexokinase A and B from yeast. Nucleic Acids Res. 14:945–963.
   PubMedGoogle Scholar
• Steitz, T. A., W. F. Anderson, R. J. Fletterick, and C. M. Anderson. 1977. High resolution crystal structures of yeast hexokinase complexes with substrates, activators, and inhibitors. J. Biol. Chem. 252:4494–4500.
   PubMed Web of Science ®Google Scholar
• Struhl, K.. 1985. Naturally occurring poly (dA-dT) sequences are upstream promoter elements of constitutive transcription in yeast. Proc. Natl. Acad. Sci. USA 82:8419–8423.
   PubMed Web of Science ®Google Scholar
• Trayser, K. A., and S. P. Colowick. 1961. Properties of crystalline hexokinase from yeast. I. Analysis for possible co-factors. Arch. Biochem. Biophys. 94:156–160.
   PubMedGoogle Scholar
• Trayser, K. A., and S. P. Colowick. 1961. Properties of crystalline hexokinase from yeast. II. Studies on ATP-enzyme interaction. Arch. Biochem. Biophys. 94:161–168.
   PubMedGoogle Scholar
• Trayser, K. A., and S. P. Colowick. 1961. Properties of crystalline hexokinase from yeast. III. Studies on glucose-enzyme interaction. Arch. Biochem. Biophys. 94:169–176.
   PubMedGoogle Scholar
• Viola, R. E., and W. W. Cleland. 1978. Use of pH studies to elucidate the chemical mechanism of yeast hexokinase. Biochemistry 17:4111–4117.
   PubMedGoogle Scholar
• Zimmermann, F. K., and I. Scheel. 1977. Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. Mol. Gen. Genet. 154:75–82.
   PubMedGoogle Scholar