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Volumn 175, Issue 3, 2008, Pages 247-254

Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant

Author keywords

ADP glucose; Heat stress; Maize; Random mutagenesis; Starch

Indexed keywords

BACTERIA (MICROORGANISMS); SOLANUM TUBEROSUM; ZEA MAYS;

EID: 47549083279     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2008.04.005     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 0000082157 scopus 로고
    • Thermal environment during endosperm cell division and grain filling in maize: effects on kernel growth and development in vitro
    • Jones R., Ouattar S., and Crookston R. Thermal environment during endosperm cell division and grain filling in maize: effects on kernel growth and development in vitro. Crop Sci. 24 (1984) 133-137
    • (1984) Crop Sci. , vol.24 , pp. 133-137
    • Jones, R.1    Ouattar, S.2    Crookston, R.3
  • 2
    • 0006575613 scopus 로고
    • Effects of photoperiod and temperature on vegetative and reproductive growth of maize (Zea mays) hybrid
    • Hunter R., Tollenaar M., and Breuer C. Effects of photoperiod and temperature on vegetative and reproductive growth of maize (Zea mays) hybrid. Can. J. Plant Sci. 57 (1977) 1127-1133
    • (1977) Can. J. Plant Sci. , vol.57 , pp. 1127-1133
    • Hunter, R.1    Tollenaar, M.2    Breuer, C.3
  • 3
    • 0000254060 scopus 로고
    • Effects of temperature on rate and duration of kernel dry matter accumulation of maize
    • Tollenaar M., and Bruulsema T. Effects of temperature on rate and duration of kernel dry matter accumulation of maize. Can. J. Plant Sci. 68 (1988) 935-940
    • (1988) Can. J. Plant Sci. , vol.68 , pp. 935-940
    • Tollenaar, M.1    Bruulsema, T.2
  • 4
    • 0000511670 scopus 로고
    • Heat stress during grain filling in maize: effects of carbohydrate storage and metabolism
    • Singletary G., Banisadr R., and Keeling P. Heat stress during grain filling in maize: effects of carbohydrate storage and metabolism. Aust. J. Plant Physiol. 21 (1994) 829-841
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 829-841
    • Singletary, G.1    Banisadr, R.2    Keeling, P.3
  • 5
    • 0000194970 scopus 로고
    • Differential responses to high temperatures of starch and nitrogen accumulation in the grain of four cultivars of wheat
    • Bhullar S.S., and Jenner C.F. Differential responses to high temperatures of starch and nitrogen accumulation in the grain of four cultivars of wheat. Aust. J. Plant Physiol. 12 (1985) 363-375
    • (1985) Aust. J. Plant Physiol. , vol.12 , pp. 363-375
    • Bhullar, S.S.1    Jenner, C.F.2
  • 6
    • 0031961128 scopus 로고    scopus 로고
    • Effect of high temperature during grain filling on starch synthesis in the developing barley grain
    • Wallwork M.A.B., Logue S.J., MacLeod L.C., and Jenner C.F. Effect of high temperature during grain filling on starch synthesis in the developing barley grain. Aust. J. Plant Physiol. 25 (1998) 173-181
    • (1998) Aust. J. Plant Physiol. , vol.25 , pp. 173-181
    • Wallwork, M.A.B.1    Logue, S.J.2    MacLeod, L.C.3    Jenner, C.F.4
  • 8
    • 0000057748 scopus 로고
    • Net photosynthetic rates, relative leaf growth rates, and leaf numbers of 22 races of maize grown at eight temperatures
    • Duncan W.G., and Hesketh J.D. Net photosynthetic rates, relative leaf growth rates, and leaf numbers of 22 races of maize grown at eight temperatures. Crop Sci. 8 (1968) 670-674
    • (1968) Crop Sci. , vol.8 , pp. 670-674
    • Duncan, W.G.1    Hesketh, J.D.2
  • 9
    • 0342759261 scopus 로고
    • Effects of temperature on the gas exchange of leaves in the light and dark
    • Hofstra G., and Hesketh J.D. Effects of temperature on the gas exchange of leaves in the light and dark. Planta 85 (1969) 228-237
    • (1969) Planta , vol.85 , pp. 228-237
    • Hofstra, G.1    Hesketh, J.D.2
  • 10
    • 0028797290 scopus 로고
    • Heat stress effects on sink activity of developing maize kernels grown in vitro
    • Cheikn N., and Jones R. Heat stress effects on sink activity of developing maize kernels grown in vitro. Physiol. Plant 95 (1995) 59-66
    • (1995) Physiol. Plant , vol.95 , pp. 59-66
    • Cheikn, N.1    Jones, R.2
  • 11
    • 3543053173 scopus 로고
    • Decreased starch synthesis in heat stressed maize kernels results from reduced ADPG-pyrophosphorylase and starch synthase activities
    • Singletary G., Banisadr R., and Keeling P. Decreased starch synthesis in heat stressed maize kernels results from reduced ADPG-pyrophosphorylase and starch synthase activities. Plant Physiol. Suppl. 102 (1993) 6
    • (1993) Plant Physiol. Suppl. , vol.102 , pp. 6
    • Singletary, G.1    Banisadr, R.2    Keeling, P.3
  • 12
    • 0001749204 scopus 로고
    • Multiple forms of maize endosperm ADP-glucose pyrophosphorylase and their control by Shrunken-2 and Brittle-2
    • Hannah L.C., Tuschall D., and Mans R. Multiple forms of maize endosperm ADP-glucose pyrophosphorylase and their control by Shrunken-2 and Brittle-2. Genetics 95 (1980) 961-970
    • (1980) Genetics , vol.95 , pp. 961-970
    • Hannah, L.C.1    Tuschall, D.2    Mans, R.3
  • 13
    • 0030187495 scopus 로고    scopus 로고
    • Effects of heat stress on enzyme activities and transcript levels in developing maize kernels grown in culture
    • Duke E., and Doehlert D. Effects of heat stress on enzyme activities and transcript levels in developing maize kernels grown in culture. Environ. Exp. Bot. 36 (1996) 199-208
    • (1996) Environ. Exp. Bot. , vol.36 , pp. 199-208
    • Duke, E.1    Doehlert, D.2
  • 14
    • 0033388536 scopus 로고    scopus 로고
    • Heat stress during grain filling in maize: effects on kernel growth and metabolism
    • Wilhelm E., Mullen R., Keeling P., and Singletary G. Heat stress during grain filling in maize: effects on kernel growth and metabolism. Crop Sci. 39 (1999) 1733-1741
    • (1999) Crop Sci. , vol.39 , pp. 1733-1741
    • Wilhelm, E.1    Mullen, R.2    Keeling, P.3    Singletary, G.4
  • 15
    • 0017151912 scopus 로고
    • Characterization of ADP-glucose pyrophosphorylase from shrunken-2 and brittle-2 mutants of maize
    • Hannah L.C., and Nelson Jr. O.E. Characterization of ADP-glucose pyrophosphorylase from shrunken-2 and brittle-2 mutants of maize. Biochem. Genet. 14 (1976) 547-560
    • (1976) Biochem. Genet. , vol.14 , pp. 547-560
    • Hannah, L.C.1    Nelson Jr., O.E.2
  • 16
    • 0014023725 scopus 로고
    • Starch deficient maize mutants lacking adenosine diphosphate glucose pyrophosphorylase activity
    • Tsai C.Y., and Nelson O.E. Starch deficient maize mutants lacking adenosine diphosphate glucose pyrophosphorylase activity. Science 151 (1966) 341-343
    • (1966) Science , vol.151 , pp. 341-343
    • Tsai, C.Y.1    Nelson, O.E.2
  • 18
    • 0032544014 scopus 로고    scopus 로고
    • Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics
    • Greene T.W., Kavakli I.H., Kahn M., and Okita T.W. Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 10322-10327
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10322-10327
    • Greene, T.W.1    Kavakli, I.H.2    Kahn, M.3    Okita, T.W.4
  • 20
    • 4644360565 scopus 로고
    • Engineering starch biosynthesis for increasing rice seed weight: the role of the cytoplasmic ADP-glucose pyrophosphorylase
    • Sakulsingharoja C., Choi S.B., Hwang S.K., Edwards G.E., Bork J., Meyer C.R., Preiss J., and Okita T.W. Engineering starch biosynthesis for increasing rice seed weight: the role of the cytoplasmic ADP-glucose pyrophosphorylase. Plant Sci. 167 (1994) 1323-1333
    • (1994) Plant Sci. , vol.167 , pp. 1323-1333
    • Sakulsingharoja, C.1    Choi, S.B.2    Hwang, S.K.3    Edwards, G.E.4    Bork, J.5    Meyer, C.R.6    Preiss, J.7    Okita, T.W.8
  • 21
    • 0026458333 scopus 로고
    • Regulation of the amount of starch in plant tissues by ADP-glucose pyrophosphorylase
    • Stark D.M., Timmerman K.P., Barry G., Preiss J., and Kishore G.M. Regulation of the amount of starch in plant tissues by ADP-glucose pyrophosphorylase. Science 258 (1992) 287-292
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.P.2    Barry, G.3    Preiss, J.4    Kishore, G.M.5
  • 22
    • 33846282391 scopus 로고    scopus 로고
    • Increasing maize seed weight by enhancing the cytoplasmic ADP-glucose pyrophosphorylase activity in transgenic plants
    • Wang Z., Chen X., Wang J., Liu T., Liu Y., Zhao L., and Wang G. Increasing maize seed weight by enhancing the cytoplasmic ADP-glucose pyrophosphorylase activity in transgenic plants. Plant Cell Tissue Organ Cult. 88 (2007) 83-92
    • (2007) Plant Cell Tissue Organ Cult. , vol.88 , pp. 83-92
    • Wang, Z.1    Chen, X.2    Wang, J.3    Liu, T.4    Liu, Y.5    Zhao, L.6    Wang, G.7
  • 23
    • 0032573220 scopus 로고    scopus 로고
    • Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
    • Greene T.W., and Hannah L.C. Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 13342-13347
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13342-13347
    • Greene, T.W.1    Hannah, L.C.2
  • 25
    • 0038654262 scopus 로고    scopus 로고
    • Seed yield and plant biomass increases in rice are conferred by deregulation of endosperm ADP-glucose pyrophosphorylase
    • Smidansky E.D., Martin J.M., Hannah L.C., Fischer A.M., and Giroux M.J. Seed yield and plant biomass increases in rice are conferred by deregulation of endosperm ADP-glucose pyrophosphorylase. Planta 216 (2003) 656-664
    • (2003) Planta , vol.216 , pp. 656-664
    • Smidansky, E.D.1    Martin, J.M.2    Hannah, L.C.3    Fischer, A.M.4    Giroux, M.J.5
  • 27
    • 27244442142 scopus 로고    scopus 로고
    • Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics
    • Boehlein S.K., Sewell A.K., Cross J., Stewart J.D., and Hannah L.C. Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics. Plant Physiol. 138 (2005) 1552-1562
    • (2005) Plant Physiol. , vol.138 , pp. 1552-1562
    • Boehlein, S.K.1    Sewell, A.K.2    Cross, J.3    Stewart, J.D.4    Hannah, L.C.5
  • 29
    • 0029866101 scopus 로고    scopus 로고
    • Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation
    • Greene T.W., Chantler S.E., Kahn M.L., Barry G.F., Preiss J., and Okita T.W. Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 1509-1513
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1509-1513
    • Greene, T.W.1    Chantler, S.E.2    Kahn, M.L.3    Barry, G.F.4    Preiss, J.5    Okita, T.W.6
  • 30
    • 0032007679 scopus 로고    scopus 로고
    • Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase
    • Laughlin M.J., Payne J.W., and Okita T.W. Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase. Phytochemistry 47 (1998) 621-629
    • (1998) Phytochemistry , vol.47 , pp. 621-629
    • Laughlin, M.J.1    Payne, J.W.2    Okita, T.W.3
  • 32
    • 3543150163 scopus 로고    scopus 로고
    • The maize Sh2r6hs ADP-glucose pyrophosphorylase (AGP) large subunit confers enhanced AGP properties in transgenic wheat (Triticum aestivum)
    • Meyer F.D., Smidansky E.D., Beecher B., Greene T.W., and Giroux M.J. The maize Sh2r6hs ADP-glucose pyrophosphorylase (AGP) large subunit confers enhanced AGP properties in transgenic wheat (Triticum aestivum). Plant Sci. 167 (2004) 899-911
    • (2004) Plant Sci. , vol.167 , pp. 899-911
    • Meyer, F.D.1    Smidansky, E.D.2    Beecher, B.3    Greene, T.W.4    Giroux, M.J.5
  • 33
    • 0014470221 scopus 로고
    • Isolation of mutants of Escherichia coli B altered in their ability to synthesize glycogen
    • Govons S., Vinopal R., Ingraham J., and Preiss J. Isolation of mutants of Escherichia coli B altered in their ability to synthesize glycogen. J. Bacteriol. 97 (1969) 970-972
    • (1969) J. Bacteriol. , vol.97 , pp. 970-972
    • Govons, S.1    Vinopal, R.2    Ingraham, J.3    Preiss, J.4
  • 34
    • 0003037055 scopus 로고
    • Chemical composition
    • Gerhandt P., et al. (Ed), American Society for Microbiology, Washington, DC
    • Hanson R.S., and Phillips J.A. Chemical composition. In: Gerhandt P., et al. (Ed). Manual of Methods for General Bacteriology (1981), American Society for Microbiology, Washington, DC 328-364
    • (1981) Manual of Methods for General Bacteriology , pp. 328-364
    • Hanson, R.S.1    Phillips, J.A.2
  • 35
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit, a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit, a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41 (1999) 95-98
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 36
    • 0033571484 scopus 로고    scopus 로고
    • Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi
    • Deng Z., Roberts D., Wang X., and Kemp R.G. Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi. Arch. Biochem. Biophys. 371 (1999) 326-331
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 326-331
    • Deng, Z.1    Roberts, D.2    Wang, X.3    Kemp, R.G.4
  • 37
    • 40749101539 scopus 로고    scopus 로고
    • Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined
    • Boehlein S.K., Shaw J.R., Stewart J.D., and Hannah L.C. Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined. Plant Physiol. 146 (2008) 289-299
    • (2008) Plant Physiol. , vol.146 , pp. 289-299
    • Boehlein, S.K.1    Shaw, J.R.2    Stewart, J.D.3    Hannah, L.C.4
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22 (2006) 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 41
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 42
    • 0025398721 scopus 로고
    • What If-a molecular modeling and drug design program
    • Vriend G. What If-a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 43
    • 0026610767 scopus 로고
    • Assessment of protein models with 3-dimensional profiles
    • Luthy R., Bowie J.U., and Eisenberg D. Assessment of protein models with 3-dimensional profiles. Nature 356 (1992) 83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 44
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11 (1998) 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 45
    • 0031772789 scopus 로고    scopus 로고
    • Assembly of maize endosperm ADP-glucose pyrophosphorylase requires motifs located throughout the large and small subunit units
    • Greene T.W., and Hannah L.C. Assembly of maize endosperm ADP-glucose pyrophosphorylase requires motifs located throughout the large and small subunit units. Plant Cell 10 (1998) 1295-1306
    • (1998) Plant Cell , vol.10 , pp. 1295-1306
    • Greene, T.W.1    Hannah, L.C.2
  • 46
    • 34347388786 scopus 로고    scopus 로고
    • The two AGPase subunits evolve at different rates in angiosperm, yet they are equally sensitive to activity altering amino acid changes when expressed in bacteria
    • Georgelis N., Braun E.L., Shaw J.R., and Hannah L.C. The two AGPase subunits evolve at different rates in angiosperm, yet they are equally sensitive to activity altering amino acid changes when expressed in bacteria. Plant Cell 19 (2007) 1458-1472
    • (2007) Plant Cell , vol.19 , pp. 1458-1472
    • Georgelis, N.1    Braun, E.L.2    Shaw, J.R.3    Hannah, L.C.4
  • 47
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y., Gojobori T., and Ikemura T. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acids Res. 28 (2000) 292
    • (2000) Nucleic Acids Res. , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 48
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuber ADP-glucose pyrophosphorylase
    • Jin X., Ballicora M.A., Preiss J., and Geiger J.H. Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO J. 24 (2005) 694-704
    • (2005) EMBO J. , vol.24 , pp. 694-704
    • Jin, X.1    Ballicora, M.A.2    Preiss, J.3    Geiger, J.H.4
  • 49
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform. 5 (2004) 150-163
    • (2004) Brief Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3


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