메뉴 건너뛰기




Volumn 155, Issue 5, 2009, Pages 1602-1612

Glyceraldehyde-3-phosphate dehydrogenase of Xanthomonas campestris pv. campestris is required for extracellular polysaccharide production and full virulence

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE TRIPHOSPHATE; BACTERIAL POLYSACCHARIDE; FRUCTOSE; GALACTOSE; GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MANNOSE; PYRUVIC ACID; SUCROSE; BACTERIAL PROTEIN;

EID: 66849134758     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.023762-0     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 0242649169 scopus 로고    scopus 로고
    • Black rot of crucifers
    • Edited by A. J. Slusarenko, R. S. S. Fraser & L. C. van Loon. Dordrecht: Kluwer Academic Publications
    • Alvarez, A. M. (2000). Black rot of crucifers. In Mechanisms of Resistance to Plant Diseases, pp. 21-52. Edited by A. J. Slusarenko, R. S. S. Fraser & L. C. van Loon. Dordrecht: Kluwer Academic Publications.
    • (2000) Mechanisms of Resistance to Plant Diseases , pp. 21-52
    • Alvarez, A.M.1
  • 2
    • 0031688984 scopus 로고    scopus 로고
    • Xanthan gum biosynthesis and application: A biochemical/genetic perspective
    • Becker, A., Katzen, F., Pühler, A. & Ielpi, L. (1998). Xanthan gum biosynthesis and application: a biochemical/genetic perspective. Appl Microbiol Biotechnol 50, 145-152.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 145-152
    • Becker, A.1    Katzen, F.2    Pühler, A.3    Ielpi, L.4
  • 3
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through TonB-dependent receptors: A feature shared by phytopathogenic and aquatic bacteria
    • Blanvillain, S., Meyer, D., Boulanger, A., Lautier, M., Guynet, C., Denance, N., Vasse, J., Lauber, E. & Arlat, M. (2007). Plant carbohydrate scavenging through TonB-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS One 2, e224.
    • (2007) PLoS One , vol.2
    • Blanvillain, S.1    Meyer, D.2    Boulanger, A.3    Lautier, M.4    Guynet, C.5    Denance, N.6    Vasse, J.7    Lauber, E.8    Arlat, M.9
  • 4
    • 0032217157 scopus 로고    scopus 로고
    • Glc protein is involved in glucose-mediated activation of Escherichia coli gapA and gapB-pgk transcription
    • Glc protein is involved in glucose-mediated activation of Escherichia coli gapA and gapB-pgk transcription. J Bacteriol 180, 6476-6483.
    • (1998) J Bacteriol , vol.180 , pp. 6476-6483
    • Charpentier, B.1    Bardey, V.2    Robas, N.3    Branlant, C.4
  • 5
    • 0000834444 scopus 로고
    • Cloning of genes involved in pathogenicity of Xanthomonas campestris pv. campestris using the broad host range cosmid pLAFR1
    • Daniels, M. J., Barber, C. E., Turner, P. C., Sawczyc, M. K., Byrde, R. J. & Fielding, A. H. (1984). Cloning of genes involved in pathogenicity of Xanthomonas campestris pv. campestris using the broad host range cosmid pLAFR1. EMBO J 3, 3323-3328.
    • (1984) EMBO J , vol.3 , pp. 3323-3328
    • Daniels, M.J.1    Barber, C.E.2    Turner, P.C.3    Sawczyc, M.K.4    Byrde, R.J.5    Fielding, A.H.6
  • 6
    • 0026047506 scopus 로고
    • Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of the PTS operon, characterization of the fructose-specific enzymes
    • de Crécy-Lagard, V., Bouvet, O. M., Lejeune, P. & Danchin, A. (1991). Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of the PTS operon, characterization of the fructose-specific enzymes. J Biol Chem 266, 18154-18161.
    • (1991) J Biol Chem , vol.266 , pp. 18154-18161
    • de Crécy-Lagard, V.1    Bouvet, O.M.2    Lejeune, P.3    Danchin, A.4
  • 7
    • 0029187070 scopus 로고
    • Involvement of bacterial polysaccharides in plant pathogenesis
    • Denny, T. P. (1995). Involvement of bacterial polysaccharides in plant pathogenesis. Annu Rev Phytopathol 33, 173-197.
    • (1995) Annu Rev Phytopathol , vol.33 , pp. 173-197
    • Denny, T.P.1
  • 8
    • 0037344870 scopus 로고    scopus 로고
    • Regulation of the central glycolytic genes in Bacillus subtilis: Binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate
    • Doan, T. & Aymerich, S. (2003). Regulation of the central glycolytic genes in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol Microbiol 47, 1709-1721.
    • (2003) Mol Microbiol , vol.47 , pp. 1709-1721
    • Doan, T.1    Aymerich, S.2
  • 9
    • 0141814627 scopus 로고    scopus 로고
    • Biofilm dispersal in Xanthomonas campestris is controlled by cell-cell signaling and is required for full virulence to plants
    • Dow, J. M., Crossman, L., Findlay, K., He, Y.-Q., Feng, J.-X. & Tang, J.-L. (2003). Biofilm dispersal in Xanthomonas campestris is controlled by cell-cell signaling and is required for full virulence to plants. Proc Natl Acad Sci U S A 100, 10995-11000.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10995-11000
    • Dow, J.M.1    Crossman, L.2    Findlay, K.3    He, Y.-Q.4    Feng, J.-X.5    Tang, J.-L.6
  • 10
    • 0034640272 scopus 로고    scopus 로고
    • Two glyceraldehyde 3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
    • Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G. & Aymerich, S. (2000). Two glyceraldehyde 3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037.
    • (2000) J Biol Chem , vol.275 , pp. 14031-14037
    • Fillinger, S.1    Boschi-Muller, S.2    Azza, S.3    Dervyn, E.4    Branlant, G.5    Aymerich, S.6
  • 11
    • 0025065382 scopus 로고
    • Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: Effects on stability
    • Ganter, C. & Plückthun, A. (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
  • 13
    • 0019036678 scopus 로고
    • D-Glyceraldehyde-3-phosphate dehydrogenase. The purification and characterisation of the enzyme from the thermophiles Bacillus stearothermophilus and Thermus aquaticus
    • Harris, J. I., Hocking, J. D., Runswick, M. J., Suzuki, K. & Walker, J. E. (1980). D-Glyceraldehyde-3-phosphate dehydrogenase. The purification and characterisation of the enzyme from the thermophiles Bacillus stearothermophilus and Thermus aquaticus. Eur J Biochem 108, 535-547.
    • (1980) Eur J Biochem , vol.108 , pp. 535-547
    • Harris, J.I.1    Hocking, J.D.2    Runswick, M.J.3    Suzuki, K.4    Walker, J.E.5
  • 14
    • 0002180234 scopus 로고
    • The host of Xanthomonas
    • Edited by J. G. Swings & E. L. Civerolo. London: Chapman & Hall
    • Hayward, A. C. (1993). The host of Xanthomonas. In Xanthomonas, pp. 51-54. Edited by J. G. Swings & E. L. Civerolo. London: Chapman & Hall.
    • (1993) Xanthomonas , pp. 51-54
    • Hayward, A.C.1
  • 16
    • 0038301902 scopus 로고    scopus 로고
    • Characterization of xanthan gum biosynthesis in a centrifugal, packed-bed reactor using metabolic flux analysis
    • Hsu, C.-H. & Lo, Y.-M. (2003). Characterization of xanthan gum biosynthesis in a centrifugal, packed-bed reactor using metabolic flux analysis. Process Biochem 38, 1617-1625.
    • (2003) Process Biochem , vol.38 , pp. 1617-1625
    • Hsu, C.-H.1    Lo, Y.-M.2
  • 17
    • 0021368737 scopus 로고
    • Energy requirements for microbial exopolysaccharide synthesis
    • Jarman, T. R. & Pace, G. W. (1984). Energy requirements for microbial exopolysaccharide synthesis. Arch Microbiol 137, 231-235.
    • (1984) Arch Microbiol , vol.137 , pp. 231-235
    • Jarman, T.R.1    Pace, G.W.2
  • 18
    • 0021662240 scopus 로고
    • Production, properties and applications of xanthan
    • Kennedy, J. F. & Bradshaw, I. J. (1984). Production, properties and applications of xanthan. Prog Ind Microbiol 19, 319-371.
    • (1984) Prog Ind Microbiol , vol.19 , pp. 319-371
    • Kennedy, J.F.1    Bradshaw, I.J.2
  • 19
    • 0016573116 scopus 로고
    • Assay of picomole amounts of ATP, ADP, and AMP using the luciferase enzyme system
    • Kimmich, G. A., Randles, J. & Brand, J. S. (1975). Assay of picomole amounts of ATP, ADP, and AMP using the luciferase enzyme system. Anal Biochem 69, 187-206.
    • (1975) Anal Biochem , vol.69 , pp. 187-206
    • Kimmich, G.A.1    Randles, J.2    Brand, J.S.3
  • 20
    • 0031909505 scopus 로고    scopus 로고
    • Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803
    • Koksharova, O., Schubert, M., Shestakov, S. & Cerff, R. (1998). Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 36, 183-194.
    • (1998) Plant Mol Biol , vol.36 , pp. 183-194
    • Koksharova, O.1    Schubert, M.2    Shestakov, S.3    Cerff, R.4
  • 21
    • 0030660130 scopus 로고    scopus 로고
    • Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (gap) is developmentally regulated and induced by glucose
    • Kormanec, J., Lempel'ová, A., Nováková, R., Rezuchová, B. & Homérová, D. (1997). Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (gap) is developmentally regulated and induced by glucose. Microbiology 143, 3555-3561.
    • (1997) Microbiology , vol.143 , pp. 3555-3561
    • Kormanec, J.1    Lempel'ová, A.2    Nováková, R.3    Rezuchová, B.4    Homérová, D.5
  • 22
    • 0025865480 scopus 로고
    • The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes
    • Lambeir, A. M., Loiseau, A. M., Kuntz, D. A., Vellieux, F. M., Michels, P. A. & Opperdoes, F. R. (1991). The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes. Eur J Biochem 198, 429-435.
    • (1991) Eur J Biochem , vol.198 , pp. 429-435
    • Lambeir, A.M.1    Loiseau, A.M.2    Kuntz, D.A.3    Vellieux, F.M.4    Michels, P.A.5    Opperdoes, F.R.6
  • 23
    • 0020479380 scopus 로고
    • Heme biosynthesis in Rhizobium: Identification of a cloned gene coding for δ-aminolevulinic acid synthetase from Rhizobium meliloti
    • Leong, S. A., Ditta, G. S. & Helinski, D. R. (1982). Heme biosynthesis in Rhizobium: identification of a cloned gene coding for δ-aminolevulinic acid synthetase from Rhizobium meliloti. J Biol Chem 257, 8724-8730.
    • (1982) J Biol Chem , vol.257 , pp. 8724-8730
    • Leong, S.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 24
    • 0035007045 scopus 로고    scopus 로고
    • Kinetic analysis of growth and xanthan gum production with Xanthomonas campestris on sucrose, using sequentially consumed nitrogen sources
    • Letisse, F., Chevallereau, P., Simon, J. L. & Lindley, N. D. (2001). Kinetic analysis of growth and xanthan gum production with Xanthomonas campestris on sucrose, using sequentially consumed nitrogen sources. Appl Microbiol Biotechnol 55, 417-422.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 417-422
    • Letisse, F.1    Chevallereau, P.2    Simon, J.L.3    Lindley, N.D.4
  • 25
    • 33947411941 scopus 로고    scopus 로고
    • A novel locus involved in extracellular polysaccharide production and virulence of Xanthomonas campestris pathovar campestris
    • Lu, G.-T., Ma, Z.-F., Hu, J.-R., Tang, D.-J., He, Y.-Q., Feng, J.-X. & Tang, J.-L. (2007a). A novel locus involved in extracellular polysaccharide production and virulence of Xanthomonas campestris pathovar campestris. Microbiology 153, 737-746.
    • (2007) Microbiology , vol.153 , pp. 737-746
    • Lu, G.-T.1    Ma, Z.-F.2    Hu, J.-R.3    Tang, D.-J.4    He, Y.-Q.5    Feng, J.-X.6    Tang, J.-L.7
  • 26
    • 37449027198 scopus 로고    scopus 로고
    • The role of glucose kinase in carbohydrate utilization and extracellular polysaccharide production in Xanthomonas campestris pathovar campestris
    • Lu, G.-T., Yang, Z.-J., Peng, F.-Y., Tan, Y.-N., Tang, Y.-Q., Feng, J.-X., Tang, D.-J., He, Y.-Q. & Tang, J.-L. (2007b). The role of glucose kinase in carbohydrate utilization and extracellular polysaccharide production in Xanthomonas campestris pathovar campestris. Microbiology 153, 4284-4294.
    • (2007) Microbiology , vol.153 , pp. 4284-4294
    • Lu, G.-T.1    Yang, Z.-J.2    Peng, F.-Y.3    Tan, Y.-N.4    Tang, Y.-Q.5    Feng, J.-X.6    Tang, D.-J.7    He, Y.-Q.8    Tang, J.-L.9
  • 27
    • 0020657307 scopus 로고
    • Characterization of two glyceraldehyde-3-phosphate dehydrogenase isoenzymes from the pentalenolactone producer Streptomyces arenae
    • Maurer, K. H., Pfeiffer, F., Zehender, H. & Mecke, D. (1983). Characterization of two glyceraldehyde-3-phosphate dehydrogenase isoenzymes from the pentalenolactone producer Streptomyces arenae. J Bacteriol 153, 930-936.
    • (1983) J Bacteriol , vol.153 , pp. 930-936
    • Maurer, K.H.1    Pfeiffer, F.2    Zehender, H.3    Mecke, D.4
  • 28
  • 29
    • 0000111355 scopus 로고
    • Black rot of crucifers
    • Edited by H. S. Chaube, J. Kumar, A. N. Mukhopadhyay & U. S. Singh. Englewood Cliffs, NJ: Prentice Hall
    • Onsando, J. M. (1992). Black rot of crucifers. In Plant Diseases of International Importance II: Diseases of Vegetable and Oil Seed Crops, pp. 243-252. Edited by H. S. Chaube, J. Kumar, A. N. Mukhopadhyay & U. S. Singh. Englewood Cliffs, NJ: Prentice Hall.
    • (1992) Plant Diseases of International Importance II: Diseases of Vegetable and Oil Seed Crops , pp. 243-252
    • Onsando, J.M.1
  • 30
    • 0024256012 scopus 로고
    • Glucose metabolism in Xanthomonas campestris and influence of methionine on the carbon flow
    • Pielken, P., Schmiz, K. L., Eggeling, L. & Sahm, H. (1988). Glucose metabolism in Xanthomonas campestris and influence of methionine on the carbon flow. Can J Microbiol 34, 1333-1337.
    • (1988) Can J Microbiol , vol.34 , pp. 1333-1337
    • Pielken, P.1    Schmiz, K.L.2    Eggeling, L.3    Sahm, H.4
  • 31
    • 22344455805 scopus 로고    scopus 로고
    • Qian, W., Jia, Y., Ren, S.-X., He, Y.-Q., Feng, J.-X., Lu, L.-F., Sun, Q., Ying, G., Tang, D.-J. & other authors (2005). Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris. Genome Res 15, 757-767.
    • Qian, W., Jia, Y., Ren, S.-X., He, Y.-Q., Feng, J.-X., Lu, L.-F., Sun, Q., Ying, G., Tang, D.-J. & other authors (2005). Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris. Genome Res 15, 757-767.
  • 33
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., Tauch, A., Jäger, W., Kalinowski, J., Thierbach, G. & Pühler, A. (1994). Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145, 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 34
    • 1542319732 scopus 로고    scopus 로고
    • Relationship between growth rate and ATP concentration in Escherichia coli: A bioassay for available cellular ATP
    • Schneider, D. A. & Gourse, R. L. (2004). Relationship between growth rate and ATP concentration in Escherichia coli: A bioassay for available cellular ATP. J Biol Chem 279, 8262-8268.
    • (2004) J Biol Chem , vol.279 , pp. 8262-8268
    • Schneider, D.A.1    Gourse, R.L.2
  • 35
    • 0030855259 scopus 로고    scopus 로고
    • Characterization of Esherichia coli strains with gapA and gapB genes deleted
    • Seta, F. D., Boschi-Muller, S., Vignails, M. L. & Branlant, G. (1997). Characterization of Esherichia coli strains with gapA and gapB genes deleted. J Bacteriol 179, 5218-5221.
    • (1997) J Bacteriol , vol.179 , pp. 5218-5221
    • Seta, F.D.1    Boschi-Muller, S.2    Vignails, M.L.3    Branlant, G.4
  • 36
    • 0023506006 scopus 로고
    • Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea
    • Staskawicz, B., Dahlbeck, D., Keen, N. & Napoli, C. (1987). Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea. J Bacteriol 169, 5789-5794.
    • (1987) J Bacteriol , vol.169 , pp. 5789-5794
    • Staskawicz, B.1    Dahlbeck, D.2    Keen, N.3    Napoli, C.4
  • 37
    • 0015757283 scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. Kinetics and physicochemical studies
    • Suzuki, K. & Imahori, K. (1973). Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. Kinetics and physicochemical studies. J Biochem 74, 955-970.
    • (1973) J Biochem , vol.74 , pp. 955-970
    • Suzuki, K.1    Imahori, K.2
  • 38
    • 0025869929 scopus 로고
    • Genetic and molecular analysis of a cluster of rpf genes involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris
    • Tang, J.-L., Liu, Y.-N., Barber, C. E., Dow, J. M., Wootton, J. C. & Daniels, M. J. (1991). Genetic and molecular analysis of a cluster of rpf genes involved in positive regulation of synthesis of extracellular enzymes and polysaccharide in Xanthomonas campestris pathovar campestris. Mol Gen Genet 226, 409-417.
    • (1991) Mol Gen Genet , vol.226 , pp. 409-417
    • Tang, J.-L.1    Liu, Y.-N.2    Barber, C.E.3    Dow, J.M.4    Wootton, J.C.5    Daniels, M.J.6
  • 39
    • 24344437709 scopus 로고    scopus 로고
    • Xanthomonas campestris pv. campestris possesses a single gluconeogenic pathway that is required for virulence
    • Tang, D.-J., He, Y.-Q., Feng, J.-X., He, B.-R., Jiang, B.-L., Lu, G.-T., Chen, B. & Tang, J.-L. (2005). Xanthomonas campestris pv. campestris possesses a single gluconeogenic pathway that is required for virulence. J Bacteriol 187, 6231-6237.
    • (2005) J Bacteriol , vol.187 , pp. 6231-6237
    • Tang, D.-J.1    He, Y.-Q.2    Feng, J.-X.3    He, B.-R.4    Jiang, B.-L.5    Lu, G.-T.6    Chen, B.7    Tang, J.-L.8
  • 41
    • 0345633540 scopus 로고    scopus 로고
    • Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis
    • Tobisch, S., Zuhlke, D., Bernhardt, J., Stulke, J. & Hecker, M. (1999). Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis. J Bacteriol 181, 6996-7004.
    • (1999) J Bacteriol , vol.181 , pp. 6996-7004
    • Tobisch, S.1    Zuhlke, D.2    Bernhardt, J.3    Stulke, J.4    Hecker, M.5
  • 42
    • 0021261403 scopus 로고
    • Behavior of the transposons Tn5 and Tn7 in Xanthomonas campestris pv. campestris
    • Turner, P., Barber, C. & Daniels, M. J. (1984). Behavior of the transposons Tn5 and Tn7 in Xanthomonas campestris pv. campestris. Mol Gen Genet 195, 101-107.
    • (1984) Mol Gen Genet , vol.195 , pp. 101-107
    • Turner, P.1    Barber, C.2    Daniels, M.J.3
  • 44
    • 0034672395 scopus 로고    scopus 로고
    • Rapid gene inactivation in Pseudomonas aeruginosa
    • Windgassen, M., Urban, A. & Jaeger, K. E. (2000). Rapid gene inactivation in Pseudomonas aeruginosa. FEMS Microbiol Lett 193, 201-205.
    • (2000) FEMS Microbiol Lett , vol.193 , pp. 201-205
    • Windgassen, M.1    Urban, A.2    Jaeger, K.E.3
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 47
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng, L., Roeder, R. G. & Luo, Y. (2003). S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114, 255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.