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Volumn 684, Issue , 2011, Pages 363-374

Purification of Rubisco Activase from Leaves or after Expression in Escherichia coli

Author keywords

AAA+ protein; Arabidopsis thaliana; ATP; Calvin Cycle; CO2 fixation; Molecular chaperone; Rubisco activase

Indexed keywords

AMMONIUM SULFATE; RCA PROTEIN, PLANT; VEGETABLE PROTEIN;

EID: 79952116203     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-60761-925-3_28     Document Type: Chapter
Times cited : (17)

References (20)
  • 1
    • 34250112628 scopus 로고
    • A soluble chloroplast protein catalyses ribulose-bisphosphate carboxylase/ oxygenase activation in vivo
    • Salvucci, M. E., Portis, A. R. Jr., and Ogren, W. L. (1985) A soluble chloroplast protein catalyses ribulose-bisphosphate carboxylase/ oxygenase activation in vivo. Photosynth Res 7, 193–201.
    • (1985) Photosynth Res , vol.7 , pp. 193-201
    • Salvucci, M.E.1    Portis, A.R.2    Ogren, W.L.3
  • 2
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase – Rubisco’s catalytic chaperone
    • Portis, A. R. Jr. (2003) Rubisco activase – Rubisco’s catalytic chaperone. Photosynth Res 75, 11–27.
    • (2003) Photosynth Res , vol.75 , pp. 11-27
    • Portis, A.R.1
  • 3
    • 0030021532 scopus 로고    scopus 로고
    • The bait in the Rubisco mousetrap
    • Andrews, T. J. (1996) The bait in the Rubisco mousetrap. Nat Struct Biol 3, 3–7.
    • (1996) Nat Struct Biol , vol.3 , pp. 3-7
    • Andrews, T.J.1
  • 4
    • 44649135348 scopus 로고    scopus 로고
    • Regulation of Rubisco activase and its interaction with Rubisco
    • Portis, A. R. Jr., Li, C. S., Wang, D. F., and Salvucci, M. E. (2008) Regulation of Rubisco activase and its interaction with Rubisco. J Exp Bot 59, 1597–604.
    • (2008) J Exp Bot , vol.59 , pp. 1597-1604
    • Portis, A.R.1    Li, C.S.2    Wang, D.F.3    Salvucci, M.E.4
  • 5
    • 0000907139 scopus 로고
    • Dissociation of ribulose-1,5-bisphosphate bound to ribulose-1,5-bisphosphate carboxylase oxygenase and its enhancement by ribulose-1,5-bisphosphate carboxylase oxygenase activase mediated hydrolysis of ATP
    • Wang, Z. Y. and Portis, A. R. Jr. (1992) Dissociation of ribulose-1,5-bisphosphate bound to ribulose-1,5-bisphosphate carboxylase oxygenase and its enhancement by ribulose-1,5-bisphosphate carboxylase oxygenase activase mediated hydrolysis of ATP. Plant Physiol 99, 1348–53.
    • (1992) Plant Physiol , vol.99 , pp. 1348-1353
    • Wang, Z.Y.1    Portis, A.R.2
  • 6
    • 0000134277 scopus 로고
    • 2 response of ribu-lose-1,5-bisphosphate carboxylase/oxygenase activation in Arabidopsis leaves
    • 2 response of ribu-lose-1,5-bisphosphate carboxylase/oxygenase activation in Arabidopsis leaves. Plant Physiol 80, 655–59.
    • (1986) Plant Physiol , vol.80 , pp. 655-659
    • Salvucci, M.E.1    Portis, A.R.2    Ogren, W.L.3
  • 7
    • 0000435087 scopus 로고    scopus 로고
    • Regulation of ribu-lose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: Insights from studies of antisense plants containing reduced amounts of Rubisco activase
    • Hammond, E. T., Andrews, T. J., and Woodrow, I. E. (1998) Regulation of ribu-lose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: Insights from studies of antisense plants containing reduced amounts of Rubisco activase. Plant Physiol 118, 1463–71.
    • (1998) Plant Physiol , vol.118 , pp. 1463-1471
    • Hammond, E.T.1    Andrews, T.J.2    Woodrow, I.E.3
  • 9
    • 0013365725 scopus 로고
    • Stimulation of thylakoid energization and ribulose-bisphosphate carboxylase/oxygenase activation in Arabidopsis leaves by methyl viologen
    • Salvucci, M. E., Portis, A. R. Jr., Heber, U., and Ogren, W. L. (1987) Stimulation of thylakoid energization and ribulose-bisphosphate carboxylase/oxygenase activation in Arabidopsis leaves by methyl viologen. FEBS Lett 221, 215–20.
    • (1987) FEBS Lett , vol.221 , pp. 215-220
    • Salvucci, M.E.1    Portis, A.R.2    Heber, U.3    Ogren, W.L.4
  • 10
    • 1942533656 scopus 로고    scopus 로고
    • Relationship between the heat tolerance of photosynthesis and the thermal stability of Rubisco activase in plants from contrasting thermal environments
    • Salvucci, M. E. and Crafts-Brandner, S. J. (2004) Relationship between the heat tolerance of photosynthesis and the thermal stability of Rubisco activase in plants from contrasting thermal environments. Plant Physiol 134, 1460–70.
    • (2004) Plant Physiol , vol.134 , pp. 1460-1470
    • Salvucci, M.E.1    Crafts-Brandner, S.J.2
  • 11
    • 0000446241 scopus 로고
    • Purification and species distribution of Rubisco activase
    • Salvucci, M. E., Werneke, J. M., Ogren, W. L., and Portis, A. R. Jr. (1987) Purification and species distribution of Rubisco activase. Plant Physiol 84, 930–6.
    • (1987) Plant Physiol , vol.84 , pp. 930-936
    • Salvucci, M.E.1    Werneke, J.M.2    Ogren, W.L.3    Portis, A.R.4
  • 12
    • 0001206497 scopus 로고
    • Rubisco activase mediates ATP-dependent activation of ribulose bisphosphate carboxylase
    • Streusand, V. J. and Portis, A. R. Jr. (1987) Rubisco activase mediates ATP-dependent activation of ribulose bisphosphate carboxylase. Plant Physiol 85, 152–4.
    • (1987) Plant Physiol , vol.85 , pp. 152-154
    • Streusand, V.J.1    Portis, A.R.2
  • 13
    • 0024485948 scopus 로고
    • Adenosine-triphosphate hydrolysis by purified Rubisco activase
    • Robinson, S. P. and Portis, A. R. Jr. (1989) Adenosine-triphosphate hydrolysis by purified Rubisco activase. Arch Biochem Biophys 268, 93–9.
    • (1989) Arch Biochem Biophys , vol.268 , pp. 93-99
    • Robinson, S.P.1    Portis, A.R.2
  • 15
    • 0025738366 scopus 로고
    • Expression of the two isoforms of spinach ribulose 1,5-bisphosphate carboxylase activase and essentiality of the conserved lysine in the consensus nucleotide-binding domain
    • Shen, J. B., Orozco, E. M., and Ogren, W. L. (1991) Expression of the two isoforms of spinach ribulose 1,5-bisphosphate carboxylase activase and essentiality of the conserved lysine in the consensus nucleotide-binding domain. J Biol Chem 266, 8963–8.
    • (1991) J Biol Chem , vol.266 , pp. 8963-8968
    • Shen, J.B.1    Orozco, E.M.2    Ogren, W.L.3
  • 16
    • 0027267295 scopus 로고
    • Photoaffinity labeling of ribulose-1.5-bispho-sphate carboxylase/oxygenase activase with ATP g-benzophenone. Identification of the ATP g-phosphate binding domain
    • Salvucci, M. E., Rajagopalan, K., Sievert, G., Haley, B. E., and Watt, D. S. (1993) Photoaffinity labeling of ribulose-1.5-bispho-sphate carboxylase/oxygenase activase with ATP g-benzophenone. Identification of the ATP g-phosphate binding domain. J Biol Chem 268, 14239–44.
    • (1993) J Biol Chem , vol.268 , pp. 14239-14244
    • Salvucci, M.E.1    Rajagopalan, K.2    Sievert, G.3    Haley, B.E.4    Watt, D.S.5
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal Biochem 72, 248–59.
    • (1976) Anal Biochem , vol.72 , pp. 248-259
    • Bradford, M.M.1
  • 18
    • 0000269022 scopus 로고
    • Electrophoretic analysis of chloroplast proteins
    • Chua, N.-H. (1980) Electrophoretic analysis of chloroplast proteins. Methods Enzymol 69, 434–46.
    • (1980) Methods Enzymol , vol.69 , pp. 434-446
    • Chua, N.-H.1
  • 19
    • 0030056076 scopus 로고    scopus 로고
    • Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) involves Rubisco activase Trp16
    • van de Loo, F. J. and Salvucci, M. E. (1996) Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) involves Rubisco activase Trp16. Biochemistry 35, 8143–48.
    • (1996) Biochemistry , vol.35 , pp. 8143-8148
    • van de Loo, F.J.1    Salvucci, M.E.2
  • 20
    • 0027305570 scopus 로고
    • 2+ and ATP or adenosine 5¢-[g-thio]-triphosphate (ATP-g-S) enhances intrinsic fluorescence and induces aggregation which increases the activity of spinach Rubisco activase
    • 2+ and ATP or adenosine 5¢-[g-thio]-triphosphate (ATP-g-S) enhances intrinsic fluorescence and induces aggregation which increases the activity of spinach Rubisco activase. Biochim Biophys Acta 1202, 47–55.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 47-55
    • Wang, Z.Y.1    Ramage, R.T.2    Portis, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.