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Volumn 179, Issue 14, 1997, Pages 4513-4522

Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. Strain PCC 6803

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0030855218     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.14.4513-4522.1997     Document Type: Article
Times cited : (31)

References (52)
  • 1
    • 0025801445 scopus 로고
    • Light-activated heterotrophic growth of the cyanobacterium Synechocystis sp. PCC 6803: A blue-light-requiring process
    • Anderson, S. L., and L. McIntosh. 1991. Light-activated heterotrophic growth of the cyanobacterium Synechocystis sp. PCC 6803: a blue-light-requiring process. J. Bacteriol. 173:2761-2767.
    • (1991) J. Bacteriol. , vol.173 , pp. 2761-2767
    • Anderson, S.L.1    McIntosh, L.2
  • 3
    • 0003445896 scopus 로고
    • The influence of inorganic nitrogen supply on carbohydrate and related metabolism in the blue-green alga, Anabaena cylindrica Lemm
    • Batt, T., and D. H. Brown. 1974. The influence of inorganic nitrogen supply on carbohydrate and related metabolism in the blue-green alga, Anabaena cylindrica Lemm. Planta 116:197-206.
    • (1974) Planta , vol.116 , pp. 197-206
    • Batt, T.1    Brown, D.H.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0021033884 scopus 로고
    • Molecular cloning of the glyceraldehyde-3-phosphate dehydrogenase genes of Bacillus stearothermophilus and Escherichia coli, and their expression in Escherichia coli
    • Branlant, G., G. Flesch, and C. Branlant. 1983. Molecular cloning of the glyceraldehyde-3-phosphate dehydrogenase genes of Bacillus stearothermophilus and Escherichia coli, and their expression in Escherichia coli. Gene 25:1-7.
    • (1983) Gene , vol.25 , pp. 1-7
    • Branlant, G.1    Flesch, G.2    Branlant, C.3
  • 6
    • 0025311083 scopus 로고
    • Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences
    • Cai, Y., and C. P. Wolk. 1990. Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences. J. Bacteriol. 172:3138-3145.
    • (1990) J. Bacteriol. , vol.172 , pp. 3138-3145
    • Cai, Y.1    Wolk, C.P.2
  • 7
    • 0002381906 scopus 로고
    • Separation and purification of NAD- and NADP-linked glyceraldehyde-3-phosphate dehydrogenases from higher plants
    • M. Edelman, R. B. Hallik, and N. H. Chua (ed.), Elsevier Biomedical Press, Amsterdam, The Netherlands
    • Cerff, R. 1982. Separation and purification of NAD-and NADP-linked glyceraldehyde-3-phosphate dehydrogenases from higher plants, p. 683-694. In M. Edelman, R. B. Hallik, and N. H. Chua (ed.), Methods in chloroplast molecular biology. Elsevier Biomedical Press, Amsterdam, The Netherlands.
    • (1982) Methods in Chloroplast Molecular Biology , pp. 683-694
    • Cerff, R.1
  • 9
    • 0025789858 scopus 로고
    • Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II carbon dioxide fixation operon of Rhodobacter sphaeroides
    • Chen, J.-H., J. L. Gibson, L. A. McCue, and F. R. Tabita. 1991. Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II carbon dioxide fixation operon of Rhodobacter sphaeroides. J. Biol. Chem. 266:20447-20452.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20447-20452
    • Chen, J.-H.1    Gibson, J.L.2    McCue, L.A.3    Tabita, F.R.4
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynskí, P., and N. Sacchi. 1986. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1986) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynskí, P.1    Sacchi, N.2
  • 11
    • 0023465112 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene from Zymomonas mobilis: Cloning, sequencing, and identification of promoter region
    • Conway, T., G. W. Sewell, and L. O. Ingram. 1987. Glyceraldehyde-3-phosphate dehydrogenase gene from Zymomonas mobilis: cloning, sequencing, and identification of promoter region. J. Bacteriol. 169:5653-5662.
    • (1987) J. Bacteriol. , vol.169 , pp. 5653-5662
    • Conway, T.1    Sewell, G.W.2    Ingram, L.O.3
  • 12
    • 0025328922 scopus 로고
    • Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenase by site-directed mutagenesis
    • Corbier, C., S. Clermont, P. Billard, T. Skarzynski, C. Branlant, A. Wonacott, and G. Branlant. 1990. Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenase by site-directed mutagenesis. Biochemistry 29:7101-7106.
    • (1990) Biochemistry , vol.29 , pp. 7101-7106
    • Corbier, C.1    Clermont, S.2    Billard, P.3    Skarzynski, T.4    Branlant, C.5    Wonacott, A.6    Branlant, G.7
  • 13
    • 0011789735 scopus 로고
    • Light-regulation of enzyme activity in Anacystis nidulans (Richt.)
    • Duggan, J. X., and L. Anderson. 1974. Light-regulation of enzyme activity in Anacystis nidulans (Richt.). Planta 122:293-297.
    • (1974) Planta , vol.122 , pp. 293-297
    • Duggan, J.X.1    Anderson, L.2
  • 14
    • 0027373083 scopus 로고
    • Strong and regulated promoters in the cyanobacterium Anabaena PCC 7120
    • Elhai, J. 1993. Strong and regulated promoters in the cyanobacterium Anabaena PCC 7120. FEMS Microbiol. Lett. 114:179-184.
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 179-184
    • Elhai, J.1
  • 15
    • 0022607058 scopus 로고
    • Interaction of fructose with the glucose permease of the cyanobacterium Synechocystis sp. strain PCC 6803
    • Flores, E., and G. Schmetterer. 1986. Interaction of fructose with the glucose permease of the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 166:693-696.
    • (1986) J. Bacteriol. , vol.166 , pp. 693-696
    • Flores, E.1    Schmetterer, G.2
  • 18
    • 0025065382 scopus 로고
    • Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: Effects on stability
    • Ganter, C., and A. Plückthun. 1990. Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: effects on stability. Biochemistry 29:9395-9402.
    • (1990) Biochemistry , vol.29 , pp. 9395-9402
    • Ganter, C.1    Plückthun, A.2
  • 19
    • 1842303872 scopus 로고
    • Genetics Computer Group. Madison, Wis.
    • 18a. Genetics Computer Group. 1995. GCG software program manual. Genetics Computer Group. Madison, Wis.
    • (1995) GCG Software Program Manual
  • 20
    • 0018569125 scopus 로고
    • Regulation of phosphate accumulation in the unicellular cyanobacterium Synechococcus
    • Grillo, J. F., and J. Gibson. 1979. Regulation of phosphate accumulation in the unicellular cyanobacterium Synechococcus. J. Bacteriol. 140:508-517.
    • (1979) J. Bacteriol. , vol.140 , pp. 508-517
    • Grillo, J.F.1    Gibson, J.2
  • 21
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory. Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual, p. 53-138. Cold Spring Harbor Laboratory. Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual , pp. 53-138
    • Harlow, E.1    Lane, D.2
  • 22
    • 0029047354 scopus 로고
    • A nuclear gene of eubacterial origin in Euglena gracilis reflects a cryptic endosymbiosis during protist evolution
    • Henze, K., A. Badr, M. Wettern, R. Cerff, and W. Martin. 1995. A nuclear gene of eubacterial origin in Euglena gracilis reflects a cryptic endosymbiosis during protist evolution. Proc. Natl. Acad. Sci. USA 92:9122-9126.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9122-9126
    • Henze, K.1    Badr, A.2    Wettern, M.3    Cerff, R.4    Martin, W.5
  • 23
    • 0016714846 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase mutants of Escherichia coli
    • Hillman, J. D., and D. G. Fraenkel. 1975. Glyceraldehyde-3-phosphate dehydrogenase mutants of Escherichia coli. J. Bacteriol. 122:1175-1179.
    • (1975) J. Bacteriol. , vol.122 , pp. 1175-1179
    • Hillman, J.D.1    Fraenkel, D.G.2
  • 24
    • 1842285767 scopus 로고
    • Association of NAD and NADP linked glyceraldehyde-3-phosphate dehydrogenase in the blue-green alga, Anabaena variabilis
    • Hood, W., and N. G. Carr. 1969. Association of NAD and NADP linked glyceraldehyde-3-phosphate dehydrogenase in the blue-green alga, Anabaena variabilis. Planta 86:250-258.
    • (1969) Planta , vol.86 , pp. 250-258
    • Hood, W.1    Carr, N.G.2
  • 25
    • 0018180463 scopus 로고
    • Cyanobacteria grown under photoautotrophic, photoheterotrophic, and heterotrophic regimes: Sugar metabolism and carbon dioxide fixation
    • Joset-Espardellier, F., C. Astier, E. H. Evans, and N. G. Carr. 1978. Cyanobacteria grown under photoautotrophic, photoheterotrophic, and heterotrophic regimes: sugar metabolism and carbon dioxide fixation. FEMS Microbiol. Lett. 4:261-264.
    • (1978) FEMS Microbiol. Lett. , vol.4 , pp. 261-264
    • Joset-Espardellier, F.1    Astier, C.2    Evans, E.H.3    Carr, N.G.4
  • 27
    • 0028226319 scopus 로고
    • The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus
    • Liaud, M.-F., C. Valentin, W. Martin, F.-Y. Bouget, B. Kloareg, and R. Cerff. 1994. The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus. J. Mol. Evol. 38:319-327.
    • (1994) J. Mol. Evol. , vol.38 , pp. 319-327
    • Liaud, M.-F.1    Valentin, C.2    Martin, W.3    Bouget, F.-Y.4    Kloareg, B.5    Cerff, R.6
  • 29
    • 0027169132 scopus 로고
    • Evidence for a chimeric nature of nuclear genomes: Eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes
    • Martin, W., H. Brinkmann, C. Savona, and R. Cerff. 1993. Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes. Proc. Natl. Acad. Sci USA 90:8692-8696.
    • (1993) Proc. Natl. Acad. Sci USA , vol.90 , pp. 8692-8696
    • Martin, W.1    Brinkmann, H.2    Savona, C.3    Cerff, R.4
  • 30
    • 0001291049 scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in photosynthetic organisms
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in photosynthetic organisms. Plant Sci. 84:163-170.
    • (1992) Plant Sci. , vol.84 , pp. 163-170
    • Mateos, M.I.1    Serrano, A.2
  • 32
    • 0029111278 scopus 로고
    • The NADP- Linked glyceraldehyde-3-phosphate dehydrogenases of Anabaena variabilis and Synechocystis sp. PCC 6803, which lack one of the cysteines found in the higher plant enzyme, are not reductively activated
    • Pacold, M. E., F. J. Stevens, D. Li, and L. E. Anderson. 1995. The NADP-linked glyceraldehyde-3-phosphate dehydrogenases of Anabaena variabilis and Synechocystis sp. PCC 6803, which lack one of the cysteines found in the higher plant enzyme, are not reductively activated. Photosynth. Res. 43:125-130.
    • (1995) Photosynth. Res. , vol.43 , pp. 125-130
    • Pacold, M.E.1    Stevens, F.J.2    Li, D.3    Anderson, L.E.4
  • 33
    • 0014383038 scopus 로고
    • The incorporation and metabolism of glucose by Anabaena variabilis
    • Pearce, J., and N. G. Carr. 1969. The incorporation and metabolism of glucose by Anabaena variabilis. J. Gen. Microbiol. 54:451-462.
    • (1969) J. Gen. Microbiol. , vol.54 , pp. 451-462
    • Pearce, J.1    Carr, N.G.2
  • 34
    • 0015441506 scopus 로고
    • Metabolism of glucose by unicellular blue-green algae
    • Pelroy, R. A., R. Rippka, and R. Y. Stanier. 1972. Metabolism of glucose by unicellular blue-green algae. Arch. Mikrobiol. 87:303-322.
    • (1972) Arch. Mikrobiol. , vol.87 , pp. 303-322
    • Pelroy, R.A.1    Rippka, R.2    Stanier, R.Y.3
  • 35
    • 0018409915 scopus 로고
    • Generic assignment, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., J. Deruelles, J. B. Waterbury, M. Herman, and R. Y. Stanier 1979. Generic assignment, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111:1-61.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herman, M.4    Stanier, R.Y.5
  • 36
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in a vertical polyacrylamide minigel system
    • Robertson, E. F., H. K. Dannelly, P. J. Malloy, and H. C. Reeves. 1987. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167:290-294.
    • (1987) Anal. Biochem. , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 39
    • 0001110695 scopus 로고
    • Cyanobacterial respiration
    • D. A. Bryant (ed.), Kluwer Academic Pubushers, Dordrecht, The Netherlands
    • Schmetterer, G. 1994. Cyanobacterial respiration, p. 409-435. In D. A. Bryant (ed.), The molecular biology of cyanobacteria. Kluwer Academic Pubushers, Dordrecht, The Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 409-435
    • Schmetterer, G.1
  • 40
    • 0027983497 scopus 로고
    • Identification of two different glyceraldehyde-3-phosphate dehydrogenases (phosphorylating) in the pholosynthetic protist Cyanophora paradoxa
    • Serrano, A., and W. Löffelhardt. 1994. Identification of two different glyceraldehyde-3-phosphate dehydrogenases (phosphorylating) in the pholosynthetic protist Cyanophora paradoxa. Arch. Microbiol. 162:14-19.
    • (1994) Arch. Microbiol. , vol.162 , pp. 14-19
    • Serrano, A.1    Löffelhardt, W.2
  • 42
    • 0027729858 scopus 로고
    • ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenases (phosphorylating and non-phosphorylating) model system
    • Serrano, A., M. I. Mateos, and M. Losada. 1993. ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenases (phosphorylating and non-phosphorylating) model system. Biochem. Biophys. Res. Commun. 193:1348-3356.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 1348-3356
    • Serrano, A.1    Mateos, M.I.2    Losada, M.3
  • 43
    • 0023046216 scopus 로고
    • Evidence in favor of the symbiotic origin of chloroplasts: Primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenases
    • Shin, M.-C., G. Lazar, and H. M. Goodman. 1986. Evidence in favor of the symbiotic origin of chloroplasts: primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenases. Cell 47:73-80.
    • (1986) Cell , vol.47 , pp. 73-80
    • Shin, M.-C.1    Lazar, G.2    Goodman, H.M.3
  • 44
    • 0002467809 scopus 로고
    • Modes of Cyanobacterial carbon metabolism
    • N. G. Carr and B. A. Whitton (ed.). Blackwell Scientific Publication, Oxford. England
    • Smith, A. J. 1982. Modes of Cyanobacterial carbon metabolism, p. 47-85. In N. G. Carr and B. A. Whitton (ed.). The biology of cyanobacteria. Blackwell Scientific Publication, Oxford. England.
    • (1982) The Biology of Cyanobacteria , pp. 47-85
    • Smith, A.J.1
  • 45
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri, A., A. Mougin, C. Corbier, A. Wonacott, C. Branlant, and G. Branlant. 1989. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry 28: 2585-2592.
    • (1989) Biochemistry , vol.28 , pp. 2585-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.4    Branlant, C.5    Branlant, G.6
  • 46
    • 0028787216 scopus 로고
    • Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strahl ATCC 29133
    • Summers, M. L., J. G. Wallis, E. L. Campbell, and J. C. Meeks. 1995. Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strahl ATCC 29133. J. Bacteriol. 177:6184-6194.
    • (1995) J. Bacteriol. , vol.177 , pp. 6184-6194
    • Summers, M.L.1    Wallis, J.G.2    Campbell, E.L.3    Meeks, J.C.4
  • 47
    • 0000111789 scopus 로고
    • The biochemistry and molecular regulation of carbon dioxide metabolism in cyanobacteria
    • D. A. Bryant (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Tabita, F. R. 1994. The biochemistry and molecular regulation of carbon dioxide metabolism in cyanobacteria, p. 437-467. In D. A. Bryant (ed.), The molecular biology of cyanobacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 437-467
    • Tabita, F.R.1
  • 48
    • 0029175426 scopus 로고
    • Resistance of photosynthesis to hydrogen peroxide in algae
    • Takeda, T., A. Yokota, and S. Shigeoka. 1995. Resistance of photosynthesis to hydrogen peroxide in algae. Plant Cell Physiol. 36:1089-1095.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1089-1095
    • Takeda, T.1    Yokota, A.2    Shigeoka, S.3
  • 49
    • 0029999407 scopus 로고    scopus 로고
    • Enzymic and molecular characterization of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942: Resistance of the enzyme to hydrogen peroxide
    • Tamoi, M., T. Ishikawa, T. Takeda, and S. Shigeoka. 1996. Enzymic and molecular characterization of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942: resistance of the enzyme to hydrogen peroxide. Biochem. J. 316:685-690.
    • (1996) Biochem. J. , vol.316 , pp. 685-690
    • Tamoi, M.1    Ishikawa, T.2    Takeda, T.3    Shigeoka, S.4
  • 50
    • 85036488690 scopus 로고    scopus 로고
    • Valverde, F., M. Losada, and A. Serrano. Unpublished data
    • Valverde, F., M. Losada, and A. Serrano. Unpublished data.
  • 51
    • 0027053219 scopus 로고
    • Analysis of the gene encoding the RNA subunit of the ribonuclease P from cyanobacteria
    • Vioque, A. 1992. Analysis of the gene encoding the RNA subunit of the ribonuclease P from cyanobacteria. Nucleic Acids Res. 20:6331-6337.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6331-6337
    • Vioque, A.1
  • 52
    • 0025089914 scopus 로고
    • Cloning and expression of chromosomally and plasmid-encoded glyceraldehyde-3-phosphate dehydrogenase genes from the chemoautotroph Alcaligenes eutrophus
    • Windhövel, U., and B. Bowien. 1993. Cloning and expression of chromosomally and plasmid-encoded glyceraldehyde-3-phosphate dehydrogenase genes from the chemoautotroph Alcaligenes eutrophus. FEMS Microbiol. Lett. 66:29-34.
    • (1993) FEMS Microbiol. Lett. , vol.66 , pp. 29-34
    • Windhövel, U.1    Bowien, B.2


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