Abstract
Screening of a mutagenized strain carrying a multicopy ENO1-'lacZ fusion plasmid revealed a new mutation affecting most glycolytic enzyme activities in a pattern resembling that caused by gcr1: levels in the range of 10% of wild-type levels on glycerol plus lactate but somewhat higher on glucose. The recessive single nuclear gene mutation, named gcr2-1, was unlinked to gcr1, and GCR1 in multiple copies did not restore enzyme levels. GCR2 was obtained by complementation from a YCp50 genomic library; the complemented strain had normal enzyme levels, as did a strain with GCR2 in multiple copies. GCR2 in multiple copies did not suppress gcr1. A chromosomal gcr2 null mutant was constructed; its pattern of enzyme activities resembled that of the gcr2-1 mutant and, like the gcr2-1 mutant, its growth defect on glucose was only partial (in contrast to the glucose negativity of the gcr1 mutant). Northern (RNA) analysis showed that gcr2 and gcr1 affect ENO1 mRNA levels.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Baker H. V. Glycolytic gene expression in Saccharomyces cerevisiae: nucleotide sequence of GCR1, null mutants, and evidence for expression. Mol Cell Biol. 1986 Nov;6(11):3774–3784. doi: 10.1128/mcb.6.11.3774. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Buchman A. R., Lue N. F., Kornberg R. D. Connections between transcriptional activators, silencers, and telomeres as revealed by functional analysis of a yeast DNA-binding protein. Mol Cell Biol. 1988 Dec;8(12):5086–5099. doi: 10.1128/mcb.8.12.5086. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Capieaux E., Vignais M. L., Sentenac A., Goffeau A. The yeast H+-ATPase gene is controlled by the promoter binding factor TUF. J Biol Chem. 1989 May 5;264(13):7437–7446. [PubMed] [Google Scholar]
- Chambers A., Tsang J. S., Stanway C., Kingsman A. J., Kingsman S. M. Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAP1. Mol Cell Biol. 1989 Dec;9(12):5516–5524. doi: 10.1128/mcb.9.12.5516. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Clifton D., Fraenkel D. G. The gcr (glycolysis regulation) mutation of Saccharomyces cerevisiae. J Biol Chem. 1981 Dec 25;256(24):13074–13078. [PubMed] [Google Scholar]
- Clifton D., Weinstock S. B., Fraenkel D. G. Glycolysis mutants in Saccharomyces cerevisiae. Genetics. 1978 Jan;88(1):1–11. doi: 10.1093/genetics/88.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen R., Yokoi T., Holland J. P., Pepper A. E., Holland M. J. Transcription of the constitutively expressed yeast enolase gene ENO1 is mediated by positive and negative cis-acting regulatory sequences. Mol Cell Biol. 1987 Aug;7(8):2753–2761. doi: 10.1128/mcb.7.8.2753. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen S. N., Chang A. C., Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2110–2114. doi: 10.1073/pnas.69.8.2110. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fraenkel D. G. On ras gene function in yeast. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4740–4744. doi: 10.1073/pnas.82.14.4740. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol. 1983 Jun 5;166(4):557–580. doi: 10.1016/s0022-2836(83)80284-8. [DOI] [PubMed] [Google Scholar]
- Hess B., Boiteux A., Krüger J. Cooperation of glycolytic enzymes. Adv Enzyme Regul. 1969;7:149–167. doi: 10.1016/0065-2571(69)90016-8. [DOI] [PubMed] [Google Scholar]
- Hill J. E., Myers A. M., Koerner T. J., Tzagoloff A. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast. 1986 Sep;2(3):163–167. doi: 10.1002/yea.320020304. [DOI] [PubMed] [Google Scholar]
- Hoffman C. S., Winston F. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene. 1987;57(2-3):267–272. doi: 10.1016/0378-1119(87)90131-4. [DOI] [PubMed] [Google Scholar]
- Holland M. J., Yokoi T., Holland J. P., Myambo K., Innis M. A. The GCR1 gene encodes a positive transcriptional regulator of the enolase and glyceraldehyde-3-phosphate dehydrogenase gene families in Saccharomyces cerevisiae. Mol Cell Biol. 1987 Feb;7(2):813–820. doi: 10.1128/mcb.7.2.813. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huet J., Cottrelle P., Cool M., Vignais M. L., Thiele D., Marck C., Buhler J. M., Sentenac A., Fromageot P. A general upstream binding factor for genes of the yeast translational apparatus. EMBO J. 1985 Dec 16;4(13A):3539–3547. doi: 10.1002/j.1460-2075.1985.tb04114.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huet J., Sentenac A. TUF, the yeast DNA-binding factor specific for UASrpg upstream activating sequences: identification of the protein and its DNA-binding domain. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3648–3652. doi: 10.1073/pnas.84.11.3648. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol. 1983 Jan;153(1):163–168. doi: 10.1128/jb.153.1.163-168.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kawasaki G., Fraenkel D. G. Cloning of yeast glycolysis genes by complementation. Biochem Biophys Res Commun. 1982 Oct 15;108(3):1107–1122. doi: 10.1016/0006-291x(82)92114-3. [DOI] [PubMed] [Google Scholar]
- Lindquist S. Regulation of protein synthesis during heat shock. Nature. 1981 Sep 24;293(5830):311–314. doi: 10.1038/293311a0. [DOI] [PubMed] [Google Scholar]
- Machida M., Uemura H., Jigami Y., Tanaka H. The protein factor which binds to the upstream activating sequence of Saccharomyces cerevisiae ENO1 gene. Nucleic Acids Res. 1988 Feb 25;16(4):1407–1422. doi: 10.1093/nar/16.4.1407. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maitra P. K., Lobo Z. A kinetic study of glycolytic enzyme synthesis in yeast. J Biol Chem. 1971 Jan 25;246(2):475–488. [PubMed] [Google Scholar]
- Mortimer R. K., Hawthorne D. C. Genetic mapping in yeast. Methods Cell Biol. 1975;11:221–233. doi: 10.1016/s0091-679x(08)60325-8. [DOI] [PubMed] [Google Scholar]
- Nishiwaki K., Hayashi N., Irie S., Chung D. H., Harashima S., Oshima Y. Structure of the yeast HIS5 gene responsive to general control of amino acid biosynthesis. Mol Gen Genet. 1987 Jun;208(1-2):159–167. doi: 10.1007/BF00330437. [DOI] [PubMed] [Google Scholar]
- Nishizawa M., Araki R., Teranishi Y. Identification of an upstream activating sequence and an upstream repressible sequence of the pyruvate kinase gene of the yeast Saccharomyces cerevisiae. Mol Cell Biol. 1989 Feb;9(2):442–451. doi: 10.1128/mcb.9.2.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
- RICHARDS O. C., RUTTER W. J. Preparation and properties of yeast aldolase. J Biol Chem. 1961 Dec;236:3177–3184. [PubMed] [Google Scholar]
- Rose M. D., Novick P., Thomas J. H., Botstein D., Fink G. R. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene. 1987;60(2-3):237–243. doi: 10.1016/0378-1119(87)90232-0. [DOI] [PubMed] [Google Scholar]
- Runge K. W., Zakian V. A. Introduction of extra telomeric DNA sequences into Saccharomyces cerevisiae results in telomere elongation. Mol Cell Biol. 1989 Apr;9(4):1488–1497. doi: 10.1128/mcb.9.4.1488. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shore D., Nasmyth K. Purification and cloning of a DNA binding protein from yeast that binds to both silencer and activator elements. Cell. 1987 Dec 4;51(5):721–732. doi: 10.1016/0092-8674(87)90095-x. [DOI] [PubMed] [Google Scholar]
- Uemura H., Shiba T., Paterson M., Jigami Y., Tanaka H. Identification of a sequence containing the positive regulatory region of Saccharomyces cerevisiae gene ENO1. Gene. 1986;45(1):67–75. doi: 10.1016/0378-1119(86)90133-2. [DOI] [PubMed] [Google Scholar]