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Volumn 155, Issue 4, 2011, Pages 1988-1998

Enzymatic activity of the soybean ecto-apyrase GS52 is essential for stimulation of nodulation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); GLYCINE MAX; RHIZOBIUM;

EID: 79953727553     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.110.170910     Document Type: Article
Times cited : (36)

References (55)
  • 1
    • 0034998287 scopus 로고    scopus 로고
    • Agrobacterium rhizogenes-transformed roots of Medicago truncatula for the study of nitrogen-fixing and endomycorrhizal symbiotic associations
    • Boisson-Dernier A, Chabaud M, Garcia F, Bécard G, Rosenberg C, Barker DG (2001) Agrobacterium rhizogenes-transformed roots of Medicago truncatula for the study of nitrogen-fixing and endomycorrhizal symbiotic associations. Mol Plant Microbe Interact 14: 695-700
    • (2001) Mol Plant Microbe Interact , vol.14 , pp. 695-700
    • Boisson-Dernier, A.1    Chabaud, M.2    Garcia, F.3    Bécard, G.4    Rosenberg, C.5    Barker, D.G.6
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 4
    • 0015189585 scopus 로고
    • Control of leghaemoglobin synthesis in snake beans
    • Broughton WJ, Dilworth MJ (1971) Control of leghaemoglobin synthesis in snake beans. Biochem J 125: 1075-1080
    • (1971) Biochem J , vol.125 , pp. 1075-1080
    • Broughton, W.J.1    Dilworth, M.J.2
  • 6
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single-site mutations using support vector machines
    • Cheng J, Randall A, Baldi P (2006) Prediction of protein stability changes for single-site mutations using support vector machines. Proteins 62: 1125-1132
    • (2006) Proteins , vol.62 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 9
    • 0034643922 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human endothelial cell ecto-ADPase/soluble CD39: Requirement of glutamate 174 and serine 218 for enzyme activity and inhibition of platelet recruitment
    • Drosopoulos JH, Broekman MJ, Islam N, Maliszewski CR, Gayle RB III, Marcus AJ (2000) Site-directed mutagenesis of human endothelial cell ecto-ADPase/soluble CD39: requirement of glutamate 174 and serine 218 for enzyme activity and inhibition of platelet recruitment. Biochemistry 39: 6936-6943
    • (2000) Biochemistry , vol.39 , pp. 6936-6943
    • Drosopoulos, J.H.1    Broekman, M.J.2    Islam, N.3    Maliszewski, C.R.4    Gayle, R.B.5    Marcus, A.J.6
  • 12
    • 0031885731 scopus 로고    scopus 로고
    • The role of ion fluxes in Nod factor signalling in Medicago sativa
    • Felle HH, Kondorosi E, Kondorosi A, Schultze M (1998) The role of ion fluxes in Nod factor signalling in Medicago sativa. Plant J 13: 455-463
    • (1998) Plant J , vol.13 , pp. 455-463
    • Felle, H.H.1    Kondorosi, E.2    Kondorosi, A.3    Schultze, M.4
  • 14
    • 58549105954 scopus 로고    scopus 로고
    • Molecular determinants of a symbiotic chronic infection
    • Gibson KE, Kobayashi H, Walker GC (2008) Molecular determinants of a symbiotic chronic infection. Annu Rev Genet 42: 413-441
    • (2008) Annu Rev Genet , vol.42 , pp. 413-441
    • Gibson, K.E.1    Kobayashi, H.2    Walker, G.C.3
  • 15
    • 49449102132 scopus 로고    scopus 로고
    • Evaluation of constitutive viral promoters in transgenic soybean roots and nodules
    • Govindarajulu M, Elmore JM, Fester T, Taylor CG (2008) Evaluation of constitutive viral promoters in transgenic soybean roots and nodules. Mol Plant Microbe Interact 21: 1027-1035
    • (2008) Mol Plant Microbe Interact , vol.21 , pp. 1027-1035
    • Govindarajulu, M.1    Elmore, J.M.2    Fester, T.3    Taylor, C.G.4
  • 17
    • 77955841193 scopus 로고    scopus 로고
    • Chitooligosaccharide sensing and downstream signaling: Contrasted outcomes in pathogenic and beneficial plant-microbe interactions
    • Hamel LP, Beaudoin N (2010) Chitooligosaccharide sensing and downstream signaling: contrasted outcomes in pathogenic and beneficial plant-microbe interactions. Planta 232: 787-806
    • (2010) Planta , vol.232 , pp. 787-806
    • Hamel, L.P.1    Beaudoin, N.2
  • 18
    • 0029948487 scopus 로고    scopus 로고
    • The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism
    • Hurley JH (1996) The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism. Annu Rev Biophys Biomol Struct 25: 137-162
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 137-162
    • Hurley, J.H.1
  • 19
    • 33645980001 scopus 로고    scopus 로고
    • Cloning and characterization of pea apyrases: Involvement of PsAPY1 in response to signal molecules from the pea pathogen Mycosphaerella pinodes
    • Kawahara T, Toyoda K, Kiba A, Miura A, Ohgawara T, Yamamoto M, Inagaki Y, Ichinose Y, Shiraishi T (2003) Cloning and characterization of pea apyrases: involvement of PsAPY1 in response to signal molecules from the pea pathogen Mycosphaerella pinodes. J Gen Plant Pathol 69: 33-38
    • (2003) J Gen Plant Pathol , vol.69 , pp. 33-38
    • Kawahara, T.1    Toyoda, K.2    Kiba, A.3    Miura, A.4    Ohgawara, T.5    Yamamoto, M.6    Inagaki, Y.7    Ichinose, Y.8    Shiraishi, T.9
  • 21
    • 33751088273 scopus 로고    scopus 로고
    • Extracellular ATP in plants: Visualization, localization, and analysis of physiological significance in growth and signaling
    • Kim SY, Sivaguru M, Stacey G (2006) Extracellular ATP in plants: visualization, localization, and analysis of physiological significance in growth and signaling. Plant Physiol 142: 984-992
    • (2006) Plant Physiol , vol.142 , pp. 984-992
    • Kim, S.Y.1    Sivaguru, M.2    Stacey, G.3
  • 22
    • 33845702620 scopus 로고    scopus 로고
    • The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by muta-genic and computational modeling analyses
    • Kirley TL, Crawford PA, Smith TM (2006) The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by muta-genic and computational modeling analyses. Purinergic Signal 2: 379-389
    • (2006) Purinergic Signal , vol.2 , pp. 379-389
    • Kirley, T.L.1    Crawford, P.A.2    Smith, T.M.3
  • 23
    • 22244483744 scopus 로고    scopus 로고
    • A rapid and efficient PCR-based mutagenesis method applicable to cell physiology study
    • Ko JK, Ma J (2005) A rapid and efficient PCR-based mutagenesis method applicable to cell physiology study. Am J Physiol Cell Physiol 288: C1273-C1278
    • (2005) Am J Physiol Cell Physiol , vol.288
    • Ko, J.K.1    Ma, J.2
  • 24
    • 0030003556 scopus 로고    scopus 로고
    • Comparative studies on animal and plant apy-rases (ATP diphosphohydrolase EC 3.6.1.5) with application of immu-nological techniques and various ATPase inhibitors
    • Komoszyński MA (1996) Comparative studies on animal and plant apy-rases (ATP diphosphohydrolase EC 3.6.1.5) with application of immu-nological techniques and various ATPase inhibitors. Comp Biochem Physiol B Biochem Mol Biol 113: 581-591
    • (1996) Comp Biochem Physiol B Biochem Mol Biol , vol.113 , pp. 581-591
    • Komoszyński, M.A.1
  • 25
    • 41549132525 scopus 로고    scopus 로고
    • Modeling studies of potato nucleoside triphosphate diphospho-hydrolase NTPDase1: An insight into the catalytic mechanism
    • Kozakiewicz A, Neumann P, Banach M, Komoszyński M, Wojtczak A (2008) Modeling studies of potato nucleoside triphosphate diphospho-hydrolase NTPDase1: an insight into the catalytic mechanism. Acta Biochim Pol 55: 141-150
    • (2008) Acta Biochim Pol , vol.55 , pp. 141-150
    • Kozakiewicz, A.1    Neumann, P.2    Banach, M.3    Komoszyński, M.4    Wojtczak, A.5
  • 28
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • Machida S, Ogawa S, Xiaohua S, Takaha T, Fujii K, Hayashi K (2000) Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett 486: 131-135
    • (2000) FEBS Lett , vol.486 , pp. 131-135
    • Machida, S.1    Ogawa, S.2    Xiaohua, S.3    Takaha, T.4    Fujii, K.5    Hayashi, K.6
  • 29
    • 49549159486 scopus 로고
    • Delayed luminescence analysis (DLA) of purine and pyrimidine ribose and deoxyribose nucleotide triphosphates in picomole quantities
    • Manandhar MSP, Van Dyke K (1974) Delayed luminescence analysis (DLA) of purine and pyrimidine ribose and deoxyribose nucleotide triphosphates in picomole quantities. Microchem J 19: 42-51
    • (1974) Microchem J , vol.19 , pp. 42-51
    • Manandhar, M.S.P.1    van Dyke, K.2
  • 30
    • 0037381237 scopus 로고    scopus 로고
    • Metabolic control of excessive extracellular nucleotide accumulation by CD39/ecto-nucleotidase-1: Implications for ischemic vascular diseases
    • Marcus AJ, Broekman MJ, Drosopoulos JH, Islam N, Pinsky DJ, Sesti C, Levi R (2003) Metabolic control of excessive extracellular nucleotide accumulation by CD39/ecto-nucleotidase-1: implications for ischemic vascular diseases. J Pharmacol Exp Ther 305: 9-16
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 9-16
    • Marcus, A.J.1    Broekman, M.J.2    Drosopoulos, J.H.3    Islam, N.4    Pinsky, D.J.5    Sesti, C.6    Levi, R.7
  • 32
    • 20444484191 scopus 로고    scopus 로고
    • Transgenic expression of the soybean apyrase in Lotus japonicus enhances nodulation
    • McAlvin CB, Stacey G (2005) Transgenic expression of the soybean apyrase in Lotus japonicus enhances nodulation. Plant Physiol 137: 1456-1462
    • (2005) Plant Physiol , vol.137 , pp. 1456-1462
    • McAlvin, C.B.1    Stacey, G.2
  • 33
    • 3042701572 scopus 로고    scopus 로고
    • Calcium, kinases and nodulation signalling in legumes
    • Oldroyd GE, Downie JA (2004) Calcium, kinases and nodulation signalling in legumes. Nat Rev Mol Cell Biol 5: 566-576
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 566-576
    • Oldroyd, G.E.1    Downie, J.A.2
  • 34
    • 44649141367 scopus 로고    scopus 로고
    • Coordinating nodule morphogenesis with rhizobial infection in legumes
    • Oldroyd GE, Downie JA (2008) Coordinating nodule morphogenesis with rhizobial infection in legumes. Annu Rev Plant Biol 59: 519-546
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 519-546
    • Oldroyd, G.E.1    Downie, J.A.2
  • 35
    • 0000456575 scopus 로고
    • Effects of vanadate on the plasma membrane ATPase of red beet and corn
    • O'Neill SD, Spanswick RM (1984) Effects of vanadate on the plasma membrane ATPase of red beet and corn. Plant Physiol 75: 586-591
    • (1984) Plant Physiol , vol.75 , pp. 586-591
    • O'Neill, S.D.1    Spanswick, R.M.2
  • 37
    • 0028967657 scopus 로고
    • Ecto-ATPases: Identities and functions
    • Plesner L (1995) Ecto-ATPases: identities and functions. Int Rev Cytol 158: 141-214
    • (1995) Int Rev Cytol , vol.158 , pp. 141-214
    • Plesner, L.1
  • 38
    • 0033524467 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a human brain ecto-apyrase: Evidence that the E-type ATPases are related to the actin/ heat shock 70/sugar kinase superfamily
    • Smith TM, Kirley TL (1999) Site-directed mutagenesis of a human brain ecto-apyrase: evidence that the E-type ATPases are related to the actin/ heat shock 70/sugar kinase superfamily. Biochemistry 38: 321-328
    • (1999) Biochemistry , vol.38 , pp. 321-328
    • Smith, T.M.1    Kirley, T.L.2
  • 39
    • 23144452044 scopus 로고    scopus 로고
    • The HHPred interactive server for protein homology detection and structure prediction
    • Söding J, Biegert A, Lupas AN (2005) The HHPred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33: W244-W248
    • (2005) Nucleic Acids Res , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 40
    • 0034496345 scopus 로고    scopus 로고
    • Molecular and biochemical comparison of two different apyrases from Arabidopsis thaliana
    • Steinebrunner I, Jeter C, Song C, Roux SJ (2000) Molecular and biochemical comparison of two different apyrases from Arabidopsis thaliana. Plant Physiol Biochem 38: 913-922
    • (2000) Plant Physiol Biochem , vol.38 , pp. 913-922
    • Steinebrunner, I.1    Jeter, C.2    Song, C.3    Roux, S.J.4
  • 41
    • 0037391711 scopus 로고    scopus 로고
    • Disruption of apyrases inhibits pollen germination in Arabidopsis
    • Steinebrunner I, Wu J, Sun Y, Corbett A, Roux SJ (2003) Disruption of apyrases inhibits pollen germination in Arabidopsis. Plant Physiol 131: 1638-1647
    • (2003) Plant Physiol , vol.131 , pp. 1638-1647
    • Steinebrunner, I.1    Wu, J.2    Sun, Y.3    Corbett, A.4    Roux, S.J.5
  • 44
    • 77957744767 scopus 로고    scopus 로고
    • Extracellular nucleo-tides elicit cytosolic free calcium oscillations in Arabidopsis
    • Tanaka K, Swanson SJ, Gilroy S, Stacey G (2010b) Extracellular nucleo-tides elicit cytosolic free calcium oscillations in Arabidopsis. Plant Physiol 154: 705-719
    • (2010) Plant Physiol , vol.154 , pp. 705-719
    • Tanaka, K.1    Swanson, S.J.2    Gilroy, S.3    Stacey, G.4
  • 45
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphorus
    • Taussky HH, Shorr E (1953) A microcolorimetric method for the determination of inorganic phosphorus. J Biol Chem 202: 675-685
    • (1953) J Biol Chem , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 47
    • 76049111641 scopus 로고    scopus 로고
    • Crystal structure of a Legionella pneumophila ecto-triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases
    • Vivian JP, Riedmaier P, Ge H, Le Nours J, Sansom FM, Wilce MC, Byres E, Dias M, Schmidberger JW, Cowan PJ, et al (2010) Crystal structure of a Legionella pneumophila ecto-triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases. Structure 18: 228-238
    • (2010) Structure , vol.18 , pp. 228-238
    • Vivian, J.P.1    Riedmaier, P.2    Ge, H.3    le Nours, J.4    Sansom, F.M.5    Wilce, M.C.6    Byres, E.7    Dias, M.8    Schmidberger, J.W.9    Cowan, P.J.10
  • 49
    • 66149156968 scopus 로고    scopus 로고
    • Evaluating the absolute quality of a single protein model using structural features and support vector machines
    • Wang Z, Tegge AN, Cheng J (2009) Evaluating the absolute quality of a single protein model using structural features and support vector machines. Proteins 75: 638-647
    • (2009) Proteins , vol.75 , pp. 638-647
    • Wang, Z.1    Tegge, A.N.2    Cheng, J.3
  • 50
    • 0037382949 scopus 로고    scopus 로고
    • Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana
    • Windsor B, Roux SJ, Lloyd A (2003) Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana. Nat Biotechnol 21: 428-433
    • (2003) Nat Biotechnol , vol.21 , pp. 428-433
    • Windsor, B.1    Roux, S.J.2    Lloyd, A.3
  • 52
    • 0035799316 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of residues in the apyrase conserved regions
    • Yang F, Hicks-Berger CA, Smith TM, Kirley TL (2001) Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry 40: 3943-3950
    • (2001) Biochemistry , vol.40 , pp. 3943-3950
    • Yang, F.1    Hicks-Berger, C.A.2    Smith, T.M.3    Kirley, T.L.4
  • 53
    • 35448935001 scopus 로고    scopus 로고
    • Characterization of rat NTPDase1, -2, and -3 ectodomains refolded from bacterial inclusion bodies
    • Zebisch M, Sträter N (2007) Characterization of rat NTPDase1, -2, and -3 ectodomains refolded from bacterial inclusion bodies. Biochemistry 46: 11945-11956
    • (2007) Biochemistry , vol.46 , pp. 11945-11956
    • Zebisch, M.1    Sträter, N.2
  • 54
    • 44349101227 scopus 로고    scopus 로고
    • Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling
    • Zebisch M, Sträter N (2008) Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling. Proc Natl Acad Sci USA 105: 6882-6887
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6882-6887
    • Zebisch, M.1    Sträter, N.2
  • 55
    • 0042622381 scopus 로고    scopus 로고
    • LGA: A method for finding 3D similarities in protein structures
    • Zemla A (2003) LGA: a method for finding 3D similarities in protein structures. Nucleic Acids Res 31: 3370-3374
    • (2003) Nucleic Acids Res , vol.31 , pp. 3370-3374
    • Zemla, A.1


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