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Volumn 143, Issue 9, 1997, Pages 3055-3061

Mutant studies of phosphofructo-2-kinases do not reveal an essential role of fructose-2,6-bisphosphate in the regulation of carbon fluxes in yeast cells

Author keywords

6 phosphofructo 1 kinase; Fructose 2,6 bisphosphate; Futile cycling; Glycolytic flux; Sarcharomyces cerevisiae

Indexed keywords

6 PHOSPHOFRUCTO 2 KINASE; 6 PHOSPHOFRUCTOKINASE; ALCOHOL; CARBON; CYCLIC AMP DEPENDENT PROTEIN KINASE; FRUCTOSE 2,6 BISPHOSPHATE; GLUCOSE; SERINE;

EID: 0038778727     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-9-3055     Document Type: Article
Times cited : (49)

References (43)
  • 1
    • 0028246641 scopus 로고
    • Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis
    • Arvanitidis, A. & Heinisch, J. (1994). Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis. J Biol Chem 269, 8911-8918.
    • (1994) J Biol Chem , vol.269 , pp. 8911-8918
    • Arvanitidis, A.1    Heinisch, J.2
  • 2
    • 0019905193 scopus 로고
    • Stimulation of yeast phosphofructokinase by fructose-2,6-bisphosphate
    • Bartrons, R., Van Schaftingen, E., Vissers, S. & Hers, H. G. (1982). Stimulation of yeast phosphofructokinase by fructose-2,6-bisphosphate. FEBS Lett 143, 137-140.
    • (1982) FEBS Lett , vol.143 , pp. 137-140
    • Bartrons, R.1    Van Schaftingen, E.2    Vissers, S.3    Hers, H.G.4
  • 4
    • 0029119846 scopus 로고
    • A rapid and highly efficient method for PCR-based site-directed mutagenesis using only one new primer
    • Boles, E. & Miosga, T. (1995). A rapid and highly efficient method for PCR-based site-directed mutagenesis using only one new primer. Curr Genet 28, 197-198.
    • (1995) Curr Genet , vol.28 , pp. 197-198
    • Boles, E.1    Miosga, T.2
  • 5
    • 0027537071 scopus 로고
    • Saccharomyces cerevisiae phosphoglucose isomerase and fructose bisphosphate aldolase can be functionally replaced by the corresponding enzymes of Escherichia coli and Drosophila melanogaster
    • Boles, E. & Zimmermann, F. K. (1993). Saccharomyces cerevisiae phosphoglucose isomerase and fructose bisphosphate aldolase can be functionally replaced by the corresponding enzymes of Escherichia coli and Drosophila melanogaster. Curr Genet 23, 187-191.
    • (1993) Curr Genet , vol.23 , pp. 187-191
    • Boles, E.1    Zimmermann, F.K.2
  • 6
    • 0027267942 scopus 로고
    • Different signals control the activation of glycolysis in the yeast Saccharomyces cerevisiae
    • Boles, E., Heinisch, J. & Zimmermann, F. K. (1993). Different signals control the activation of glycolysis in the yeast Saccharomyces cerevisiae. Yeast 9, 761-770.
    • (1993) Yeast , vol.9 , pp. 761-770
    • Boles, E.1    Heinisch, J.2    Zimmermann, F.K.3
  • 7
    • 0029991328 scopus 로고    scopus 로고
    • Cloning of a second gene encoding 6-phosphofructo-2-kinase in yeast and characterization of mutant strains without fructose-2,6-bisphosphate
    • Boles, E., Göhlmann, H. W. H. & Zimmermann, F. K. (1996). Cloning of a second gene encoding 6-phosphofructo-2-kinase in yeast and characterization of mutant strains without fructose-2,6-bisphosphate. Mol Microbiol 20, 65-76.
    • (1996) Mol Microbiol , vol.20 , pp. 65-76
    • Boles, E.1    Göhlmann, H.W.H.2    Zimmermann, F.K.3
  • 8
    • 0021125420 scopus 로고
    • Yeast mutants without phosphofructokinase activity can still perform glycolysis and alcoholic fermentation
    • Breitenbach-Schmitt, I., Heinisch, J., Schmitt, H. D. & Zimmermann, F. K. (1984). Yeast mutants without phosphofructokinase activity can still perform glycolysis and alcoholic fermentation. Mol Gen Genet 195, 530-535.
    • (1984) Mol Gen Genet , vol.195 , pp. 530-535
    • Breitenbach-Schmitt, I.1    Heinisch, J.2    Schmitt, H.D.3    Zimmermann, F.K.4
  • 9
    • 0018391488 scopus 로고
    • Physiological effects of seven different blocks in glycolysis in Saccharomyces cerevisiae
    • Ciriacy, M. & Breitenbach, I. (1979). Physiological effects of seven different blocks in glycolysis in Saccharomyces cerevisiae. J Bacteriol 139, 152-160.
    • (1979) J Bacteriol , vol.139 , pp. 152-160
    • Ciriacy, M.1    Breitenbach, I.2
  • 10
    • 0026653206 scopus 로고
    • Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae
    • Davies, S. E. C. & Brindle, K. M. (1992). Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae. Biochemistry 31, 4729-4735.
    • (1992) Biochemistry , vol.31 , pp. 4729-4735
    • Davies, S.E.C.1    Brindle, K.M.2
  • 11
    • 0026457028 scopus 로고
    • Regulation of sugar utilization by Saccharomyces cerevisiae
    • Entian, K.-D. & Barnett, J. A. (1992). Regulation of sugar utilization by Saccharomyces cerevisiae. Trends Biochem Sci 17, 506-510.
    • (1992) Trends Biochem Sci , vol.17 , pp. 506-510
    • Entian, K.-D.1    Barnett, J.A.2
  • 12
    • 0029094167 scopus 로고
    • Physiological control of flux: The requirement for multisite modulation
    • Fell, D. A. & Thomas, S. (1995). Physiological control of flux: the requirement for multisite modulation. Biochem J 311, 35-39.
    • (1995) Biochem J , vol.311 , pp. 35-39
    • Fell, D.A.1    Thomas, S.2
  • 13
    • 0021764588 scopus 로고
    • The mechanism by which glucose increases fructose-2,6-bisphosphate concentration in Saccharomyces cerevisiae
    • François, J., Van Schaftingen, E. & Hers, H. G. (1984). The mechanism by which glucose increases fructose-2,6-bisphosphate concentration in Saccharomyces cerevisiae. Eur J Biochem 145, 187-193.
    • (1984) Eur J Biochem , vol.145 , pp. 187-193
    • François, J.1    Van Schaftingen, E.2    Hers, H.G.3
  • 14
    • 0023193659 scopus 로고
    • Changes in the concentrations of cAMP, fructose-2,6-bisphosphate and related metabolites and enzymes in Saccharomyces cerevisiae during growth on glucose
    • François, J., Eraso, P. & Gancedo, C. (1987). Changes in the concentrations of cAMP, fructose-2,6-bisphosphate and related metabolites and enzymes in Saccharomyces cerevisiae during growth on glucose. Eur J Biochem 164, 369-373.
    • (1987) Eur J Biochem , vol.164 , pp. 369-373
    • François, J.1    Eraso, P.2    Gancedo, C.3
  • 15
    • 0024288058 scopus 로고
    • The control of glycogen metabolism in yeast
    • François, J., Villanueva, M. E. & Hers, H. G. (1988). The control of glycogen metabolism in yeast. Eur J Biochem 174, 551-559.
    • (1988) Eur J Biochem , vol.174 , pp. 551-559
    • François, J.1    Villanueva, M.E.2    Hers, H.G.3
  • 16
    • 0014977781 scopus 로고
    • Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeast
    • Gancedo, J. M. & Gancedo, C. (1971). Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeast. Arch Microbiol 76, 132-138.
    • (1971) Arch Microbiol , vol.76 , pp. 132-138
    • Gancedo, J.M.1    Gancedo, C.2
  • 17
    • 0020362744 scopus 로고
    • Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae
    • Gancedo, J. M., Mazon, M. J. & Gancedo, C. (1982). Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae. Arch Biochem Biophys 218, 478-482.
    • (1982) Arch Biochem Biophys , vol.218 , pp. 478-482
    • Gancedo, J.M.1    Mazon, M.J.2    Gancedo, C.3
  • 18
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six base-pair restriction sites
    • Gietz, R. D. & Sugino, A. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six base-pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 19
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C. & Fink, E. R. (1991). Guide to yeast genetics and molecular biology. Methods Enzymol 194, 1-933.
    • (1991) Methods Enzymol , vol.194 , pp. 1-933
    • Guthrie, C.1    Fink, E.R.2
  • 20
    • 0022595650 scopus 로고
    • Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast
    • Heinisch, J. (1986). Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Mol Gen Genet 202, 75-82.
    • (1986) Mol Gen Genet , vol.202 , pp. 75-82
    • Heinisch, J.1
  • 22
    • 0030037752 scopus 로고    scopus 로고
    • A yeast phosphofructokinase insensitive to the allosteric activator fructose-2,6-bisphosphate
    • Heinisch, J. J., Boles, E. & Timpel, C. (1996). A yeast phosphofructokinase insensitive to the allosteric activator fructose-2,6-bisphosphate. J Biol Chem 271, 15928-15933.
    • (1996) J Biol Chem , vol.271 , pp. 15928-15933
    • Heinisch, J.J.1    Boles, E.2    Timpel, C.3
  • 23
    • 0020483680 scopus 로고
    • Fructose-2,6-bisphosphate 2 years after its discovery
    • Hers, H. G. & Van Schaftingen, E. (1982). Fructose-2,6-bisphosphate 2 years after its discovery. Biochem J 206, 1-12.
    • (1982) Biochem J , vol.206 , pp. 1-12
    • Hers, H.G.1    Van Schaftingen, E.2
  • 24
    • 0030596963 scopus 로고    scopus 로고
    • 644 is important for catalytic activity but is not involved in cAMP-dependent phosphorylation of yeast 6-phosphofructo-2-kinase
    • 644 is important for catalytic activity but is not involved in cAMP-dependent phosphorylation of yeast 6-phosphofructo-2-kinase. FEBS Lett 395, 225-227.
    • (1996) FEBS Lett , vol.395 , pp. 225-227
    • Keßler, R.1    Eschrich, K.2
  • 25
    • 0026314763 scopus 로고
    • Yeast 6-phosphofructo-2-kinase: Sequence and mutant
    • Kretschmer, M. & Fraenkel, D. G. (1991). Yeast 6-phosphofructo-2-kinase: sequence and mutant. Biochemistry 30, 10663-10672.
    • (1991) Biochemistry , vol.30 , pp. 10663-10672
    • Kretschmer, M.1    Fraenkel, D.G.2
  • 26
    • 0025876586 scopus 로고
    • Identification and cloning of yeast phosphofructokinase 2
    • Kretschmer, M., Tempest, P. & Fraenkel, D. G. (1991). Identification and cloning of yeast phosphofructokinase 2. Eur J Biochem 197, 367-372.
    • (1991) Eur J Biochem , vol.197 , pp. 367-372
    • Kretschmer, M.1    Tempest, P.2    Fraenkel, D.G.3
  • 28
    • 0019187844 scopus 로고
    • Reserve carbohydrate metabolism in Saccharomyces cerevisiae: Responses to nutrient limitation
    • Lillie, S. H. & Pringle, J. R. (1980). Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J Bacteriol 143, 1384-1394.
    • (1980) J Bacteriol , vol.143 , pp. 1384-1394
    • Lillie, S.H.1    Pringle, J.R.2
  • 30
    • 0029996341 scopus 로고    scopus 로고
    • A two-hybrid system analysis shows interactions between 6-phosphofructo-1-kinase and 6-phosphofructo-2-kinase but not between other glycolytic enzymes of the yeast Saccharomyces cerevisiae
    • Müller, S., Boles, E. & Zimmermann, F. K. (1996). A two-hybrid system analysis shows interactions between 6-phosphofructo-1-kinase and 6-phosphofructo-2-kinase but not between other glycolytic enzymes of the yeast Saccharomyces cerevisiae. Eur J Biochem 236, 626-631.
    • (1996) Eur J Biochem , vol.236 , pp. 626-631
    • Müller, S.1    Boles, E.2    Zimmermann, F.K.3
  • 31
    • 0029874904 scopus 로고    scopus 로고
    • The regulatory characteristics of yeast fructose-1,6-bisphosphatase confer only a small selective advantage
    • Navas, M. A. & Gancedo, J. M. (1996). The regulatory characteristics of yeast fructose-1,6-bisphosphatase confer only a small selective advantage. J Bacteriol 178, 1809-1812.
    • (1996) J Bacteriol , vol.178 , pp. 1809-1812
    • Navas, M.A.1    Gancedo, J.M.2
  • 32
    • 0027453012 scopus 로고
    • Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth on glucose
    • Navas, M. A., Cerdán, S. & Gancedo, J. M. (1993). Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth on glucose. Proc Nat! Acad Sci USA 90, 1290-1294.
    • (1993) Proc Nat! Acad Sci USA , vol.90 , pp. 1290-1294
    • Navas, M.A.1    Cerdán, S.2    Gancedo, J.M.3
  • 33
    • 0021223202 scopus 로고
    • Characterization of fructose-1,6-bisphosphatase from bakers' yeast
    • Noda, T., Hoffschulte, H. & Holzer, H. (1984). Characterization of fructose-1,6-bisphosphatase from bakers' yeast. J Biol Chem 259, 7191-7197.
    • (1984) J Biol Chem , vol.259 , pp. 7191-7197
    • Noda, T.1    Hoffschulte, H.2    Holzer, H.3
  • 34
    • 0026671190 scopus 로고
    • The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase
    • Paravicini, G. & Kretschmer, M. (1992). The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase. Biochemistry 31, 7126-7133.
    • (1992) Biochemistry , vol.31 , pp. 7126-7133
    • Paravicini, G.1    Kretschmer, M.2
  • 36
    • 0024694679 scopus 로고
    • Over-production of glycolytic enzymes in yeast
    • Schaaff, I., Heinisch, J. & Zimmermann, F. K. (1989). Over-production of glycolytic enzymes in yeast. Yeast 5, 285-290.
    • (1989) Yeast , vol.5 , pp. 285-290
    • Schaaff, I.1    Heinisch, J.2    Zimmermann, F.K.3
  • 37
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells by single stranded nucleic acids as carrier
    • Schiestl, R. H. & Gietz, R. D. (1989). High efficiency transformation of intact yeast cells by single stranded nucleic acids as carrier. Curr Genet 16, 339-346.
    • (1989) Curr Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 38
    • 0025879946 scopus 로고
    • Fermentable sugars and intracellular acidification as specific activators of the RAS-adenylate cyclase signalling pathway in yeast: The relationship to nutrient-induced cell cycle control
    • Thevelein, J. M. (1991). Fermentable sugars and intracellular acidification as specific activators of the RAS-adenylate cyclase signalling pathway in yeast: the relationship to nutrient-induced cell cycle control. Mol Microbiol 5, 1301-1307.
    • (1991) Mol Microbiol , vol.5 , pp. 1301-1307
    • Thevelein, J.M.1
  • 39
    • 0030574067 scopus 로고    scopus 로고
    • Design of metabolic control for large flux changes
    • Thomas, S. & Fell, D. A. (1996). Design of metabolic control for large flux changes. J Theor Biol 182, 285-298.
    • (1996) J Theor Biol , vol.182 , pp. 285-298
    • Thomas, S.1    Fell, D.A.2
  • 41
    • 0020438908 scopus 로고
    • A kinetic study of pyrophosphate : Fructose-6-phosphate phosphotransferase from potato tubers
    • Van Schaftingen, E., Lederer, B., Bartrons, R. & Hers, H. G. (1982). A kinetic study of pyrophosphate : fructose-6-phosphate phosphotransferase from potato tubers. Eur J Biochem 129, 191-195.
    • (1982) Eur J Biochem , vol.129 , pp. 191-195
    • Van Schaftingen, E.1    Lederer, B.2    Bartrons, R.3    Hers, H.G.4
  • 42
    • 0027255819 scopus 로고
    • The pde2 gene of Saccharomyces cerevisiae is allelic to real and encodes a phosphodiesterase which protects the cell from extracellular cAMP
    • Wilson, R. B., Renault, G., Jacquet, M. & Tatchell, K. (1993). The pde2 gene of Saccharomyces cerevisiae is allelic to real and encodes a phosphodiesterase which protects the cell from extracellular cAMP. FEBS Lett 325, 191-195.
    • (1993) FEBS Lett , vol.325 , pp. 191-195
    • Wilson, R.B.1    Renault, G.2    Jacquet, M.3    Tatchell, K.4
  • 43
    • 77957005673 scopus 로고
    • Preparation and assay of deoxyribonucleic acids from animal tissue
    • Zamenhoff, S. (1957). Preparation and assay of deoxyribonucleic acids from animal tissue. Methods Enzymol 3, 696-704.
    • (1957) Methods Enzymol , vol.3 , pp. 696-704
    • Zamenhoff, S.1


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