메뉴 건너뛰기




Volumn 164, Issue 12, 2007, Pages 1564-1571

Chloroplast protein synthesis elongation factor, EF-Tu, reduces thermal aggregation of rubisco activase

Author keywords

Chaperones; Chloroplast EF Tu; Heat tolerance; Protein aggregation; Rubisco activase

Indexed keywords

BIOSYNTHESIS; CROPS; ENZYME ACTIVITY; PHOTOSYNTHESIS;

EID: 36048970701     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2007.07.008     Document Type: Article
Times cited : (39)

References (44)
  • 1
    • 0001667761 scopus 로고
    • Differential stomatal response between C3 and C4 species to atmospheric CO2 concentration and light
    • Akita S., and Moss D.N. Differential stomatal response between C3 and C4 species to atmospheric CO2 concentration and light. Crop Sci 12 (1972) 789-793
    • (1972) Crop Sci , vol.12 , pp. 789-793
    • Akita, S.1    Moss, D.N.2
  • 2
    • 0030021532 scopus 로고    scopus 로고
    • The bait in the Rubisco mousetrap
    • Andrews T.J. The bait in the Rubisco mousetrap. Nat Struct Mol Biol 3 (1996) 3-7
    • (1996) Nat Struct Mol Biol , vol.3 , pp. 3-7
    • Andrews, T.J.1
  • 3
    • 0019315437 scopus 로고
    • Dissociation of supramolecular complexes in chloroplast membranes: a manifestation of heat damage to the photosynthetic apparatus
    • Armond P.A., Björkman O., and Staehelin L.A. Dissociation of supramolecular complexes in chloroplast membranes: a manifestation of heat damage to the photosynthetic apparatus. Biochim Biophys Acta 601 (1980) 433-442
    • (1980) Biochim Biophys Acta , vol.601 , pp. 433-442
    • Armond, P.A.1    Björkman, O.2    Staehelin, L.A.3
  • 4
    • 0025238551 scopus 로고
    • Evolutionary transfer of the chloroplast tufA gene to the nucleus
    • Baldauf S.L., and Palmer J.D. Evolutionary transfer of the chloroplast tufA gene to the nucleus. Nature 344 (1990) 262-265
    • (1990) Nature , vol.344 , pp. 262-265
    • Baldauf, S.L.1    Palmer, J.D.2
  • 5
    • 2142768810 scopus 로고    scopus 로고
    • Chaperone activity of cytosolic small heat shock proteins from wheat
    • Basha E., Lee G.J., Demeler B., and Vierling E. Chaperone activity of cytosolic small heat shock proteins from wheat. Eur J Biochem 271 (2004) 1426-1436
    • (2004) Eur J Biochem , vol.271 , pp. 1426-1436
    • Basha, E.1    Lee, G.J.2    Demeler, B.3    Vierling, E.4
  • 6
    • 0000191368 scopus 로고
    • Photosynthetic response and adaptation to temperature in higher plants
    • Berry J.A., and Björkman O. Photosynthetic response and adaptation to temperature in higher plants. Annu Rev Plant Physiol 31 (1980) 491-543
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 491-543
    • Berry, J.A.1    Björkman, O.2
  • 7
    • 0035123743 scopus 로고    scopus 로고
    • Heat-stress induced synthesis of chloroplast protein synthesis elongation factor (EF-Tu) in a heat-tolerant maize line
    • Bhadula S.K., Elthon T.E., Habben J.E., Helentjaris T.G., Jiao S., and Ristic Z. Heat-stress induced synthesis of chloroplast protein synthesis elongation factor (EF-Tu) in a heat-tolerant maize line. Planta 212 (2001) 359-366
    • (2001) Planta , vol.212 , pp. 359-366
    • Bhadula, S.K.1    Elthon, T.E.2    Habben, J.E.3    Helentjaris, T.G.4    Jiao, S.5    Ristic, Z.6
  • 8
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor
    • Caldas T.D., Yaagoubi A.E., and Richarme G. Chaperone properties of bacterial elongation factor. J Biol Chem 273 (1998) 11478-11482
    • (1998) J Biol Chem , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    Yaagoubi, A.E.2    Richarme, G.3
  • 9
    • 0033969301 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2
    • Caldas T.D., Laalami S., and Richarme G. Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. J Biol Chem 275 (2000) 855-860
    • (2000) J Biol Chem , vol.275 , pp. 855-860
    • Caldas, T.D.1    Laalami, S.2    Richarme, G.3
  • 11
    • 0034700153 scopus 로고    scopus 로고
    • Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2
    • Crafts-Brandner S.J., and Salvucci M.E. Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2. Proc Natl Acad Sci USA 97 (2000) 13430-13435
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13430-13435
    • Crafts-Brandner, S.J.1    Salvucci, M.E.2
  • 12
    • 0037008209 scopus 로고    scopus 로고
    • Sensitivity of photosynthesis in a C4 plant, maize, to heat stress
    • Crafts-Brandner S.J., and Salvucci M.E. Sensitivity of photosynthesis in a C4 plant, maize, to heat stress. Plant Physiol 129 (2002) 1773-1780
    • (2002) Plant Physiol , vol.129 , pp. 1773-1780
    • Crafts-Brandner, S.J.1    Salvucci, M.E.2
  • 13
    • 0031400786 scopus 로고    scopus 로고
    • The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature
    • Crafts-Brandner S.J., van de Loo F.J., and Salvucci M.E. The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature. Plant Physiol 114 (1997) 439-444
    • (1997) Plant Physiol , vol.114 , pp. 439-444
    • Crafts-Brandner, S.J.1    van de Loo, F.J.2    Salvucci, M.E.3
  • 14
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • Diamant S., Peres Ben-Zvi A., Bukau B., and Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem 275 (2000) 21107-21113
    • (2000) J Biol Chem , vol.275 , pp. 21107-21113
    • Diamant, S.1    Peres Ben-Zvi, A.2    Bukau, B.3    Goloubinoff, P.4
  • 15
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
    • Feder M.E., and Hofmann G.E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 61 (1999) 243-282
    • (1999) Annu Rev Physiol , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 16
    • 0001569341 scopus 로고    scopus 로고
    • Moderately high temperatures inhibit Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco
    • Feller U., Crafts-Brandner S.J., and Salvucci M.E. Moderately high temperatures inhibit Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco. Plant Physiol 116 (1998) 539-546
    • (1998) Plant Physiol , vol.116 , pp. 539-546
    • Feller, U.1    Crafts-Brandner, S.J.2    Salvucci, M.E.3
  • 17
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat shock proteins
    • Hendrick J.P., and Hartl F.U. Molecular chaperone functions of heat shock proteins. Annu Rev Biochem 62 (1993) 349-384
    • (1993) Annu Rev Biochem , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 18
    • 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
  • 19
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • Lee G.J., and Vierling E. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol 122 (2000) 189-197
    • (2000) Plant Physiol , vol.122 , pp. 189-197
    • Lee, G.J.1    Vierling, E.2
  • 20
    • 0012253997 scopus 로고    scopus 로고
    • Gene expression of chloroplast translation elongation factor Tu during maize chloroplast biogenesis
    • Lee J.H., Kang I.H., Choi K.L., Sim W.S., and Kim J.K. Gene expression of chloroplast translation elongation factor Tu during maize chloroplast biogenesis. J Plant Biol 40 (1997) 227-233
    • (1997) J Plant Biol , vol.40 , pp. 227-233
    • Lee, J.H.1    Kang, I.H.2    Choi, K.L.3    Sim, W.S.4    Kim, J.K.5
  • 24
    • 0030599940 scopus 로고    scopus 로고
    • The tuf gene family of soybean: structure and differential transcription
    • Maurer F., Maximilien M., and Stutz E. The tuf gene family of soybean: structure and differential transcription. Plant Sci 117 (1996) 83-93
    • (1996) Plant Sci , vol.117 , pp. 83-93
    • Maurer, F.1    Maximilien, M.2    Stutz, E.3
  • 25
    • 1642527081 scopus 로고    scopus 로고
    • Localization and abundance of chloroplast protein synthesis elongation factor (EF-Tu) and heat stability of chloroplast stromal proteins in maize
    • Momcilovic I., and Ristic Z. Localization and abundance of chloroplast protein synthesis elongation factor (EF-Tu) and heat stability of chloroplast stromal proteins in maize. Plant Sci 166 (2004) 81-88
    • (2004) Plant Sci , vol.166 , pp. 81-88
    • Momcilovic, I.1    Ristic, Z.2
  • 26
    • 0012533273 scopus 로고    scopus 로고
    • The Rubisco activase-Rubisco system: an ATPase-dependent association that regulates photosynthesis
    • McManus M.T., Laing W.L., and Allen A.C. (Eds), Sheffield Academic Press, Sheffield, UK
    • Portis A.R. The Rubisco activase-Rubisco system: an ATPase-dependent association that regulates photosynthesis. In: McManus M.T., Laing W.L., and Allen A.C. (Eds). Protein-protein interactions in plant biology Vol. 7 (2002), Sheffield Academic Press, Sheffield, UK 30-52
    • (2002) Protein-protein interactions in plant biology , vol.7 , pp. 30-52
    • Portis, A.R.1
  • 27
    • 4544318828 scopus 로고    scopus 로고
    • Chaperone activity of recombinant maize chloroplast protein synthesis elongation factor, EF-Tu
    • Rao D., Momcilovic I., Kobayashi S., Callegari E., and Ristic Z. Chaperone activity of recombinant maize chloroplast protein synthesis elongation factor, EF-Tu. Eur J Biochem 271 (2004) 3684-3692
    • (2004) Eur J Biochem , vol.271 , pp. 3684-3692
    • Rao, D.1    Momcilovic, I.2    Kobayashi, S.3    Callegari, E.4    Ristic, Z.5
  • 28
    • 0001543107 scopus 로고
    • Chloroplast structure after water and high temperature stress in two lines of maize that differ in endogenous levels of abscisic acid
    • Ristic Z., and Cass D.D. Chloroplast structure after water and high temperature stress in two lines of maize that differ in endogenous levels of abscisic acid. Int J Plant Sci 153 (1992) 186-196
    • (1992) Int J Plant Sci , vol.153 , pp. 186-196
    • Ristic, Z.1    Cass, D.D.2
  • 29
    • 0027136527 scopus 로고
    • Dehydration avoidance and damage to the plasma and thylakoid membranes in lines of maize differing in endogenous levels of abscisic acid
    • Ristic Z., and Cass D.D. Dehydration avoidance and damage to the plasma and thylakoid membranes in lines of maize differing in endogenous levels of abscisic acid. J Plant Physiol 142 (1993) 759-764
    • (1993) J Plant Physiol , vol.142 , pp. 759-764
    • Ristic, Z.1    Cass, D.D.2
  • 30
    • 0029862011 scopus 로고    scopus 로고
    • Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates
    • Ristic Z., Williams G., Yang G., Martin B., and Fullerton S. Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates. J Plant Physiol 149 (1996) 424-432
    • (1996) J Plant Physiol , vol.149 , pp. 424-432
    • Ristic, Z.1    Williams, G.2    Yang, G.3    Martin, B.4    Fullerton, S.5
  • 31
    • 4544266397 scopus 로고    scopus 로고
    • A maize mutant with decreased capacity to accumulate chloroplast protein synthesis elongation factor (EF-Tu) displays reduced tolerance to heat stress
    • Ristic Z., Wilson K., Nelsen C., Momcilovic I., Kobayashi S., Meeley R., et al. A maize mutant with decreased capacity to accumulate chloroplast protein synthesis elongation factor (EF-Tu) displays reduced tolerance to heat stress. Plant Sci 167 (2004) 1367-1374
    • (2004) Plant Sci , vol.167 , pp. 1367-1374
    • Ristic, Z.1    Wilson, K.2    Nelsen, C.3    Momcilovic, I.4    Kobayashi, S.5    Meeley, R.6
  • 32
    • 37549014854 scopus 로고    scopus 로고
    • Ristic Z, Bukovnik U, Momcilovic I, Fu J, Prasad PVV. Heat-induced accumulation of chloroplast protein synthesis elongation factor, EF-Tu, in winter wheat. J Plant Physiol 2007; doi:10.1016/j.jplph.2007.03.003.
  • 33
    • 0026460010 scopus 로고
    • Subunit interactions of Rubisco activase: polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with Rubisco
    • Salvucci M.E. Subunit interactions of Rubisco activase: polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with Rubisco. Arch Biochem Biophys 298 (1992) 688-696
    • (1992) Arch Biochem Biophys , vol.298 , pp. 688-696
    • Salvucci, M.E.1
  • 34
    • 0035193658 scopus 로고    scopus 로고
    • Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo
    • Salvucci M.E., Osteryoung K.W., Crafts-Brandner S.J., and Vierling E. Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo. Plant Physiol 127 (2001) 1053-1064
    • (2001) Plant Physiol , vol.127 , pp. 1053-1064
    • Salvucci, M.E.1    Osteryoung, K.W.2    Crafts-Brandner, S.J.3    Vierling, E.4
  • 35
    • 0037529201 scopus 로고    scopus 로고
    • Two isoforms of Rubisco activase in cotton, the products of separate genes not alternative splicing
    • Salvucci M.E., van de Loo F.J., and Stecher D. Two isoforms of Rubisco activase in cotton, the products of separate genes not alternative splicing. Planta 216 (2003) 736-744
    • (2003) Planta , vol.216 , pp. 736-744
    • Salvucci, M.E.1    van de Loo, F.J.2    Stecher, D.3
  • 36
    • 0032133306 scopus 로고    scopus 로고
    • Regulation of the heat shock response
    • Schöffl F., Prändl R., and Reindl A. Regulation of the heat shock response. Plant Physiol 117 (1998) 1135-1141
    • (1998) Plant Physiol , vol.117 , pp. 1135-1141
    • Schöffl, F.1    Prändl, R.2    Reindl, A.3
  • 37
    • 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. Nucl Acids Res 31 (2003) 3381-3385
    • (2003) Nucl Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 38
    • 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. 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 (1991) 8963-8968
    • (1991) J Biol Chem , vol.266 , pp. 8963-8968
    • Shen, J.B.1    Orozco, E.M.2    Ogren, W.L.3
  • 39
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: interactions, associations and the possibilities of a better enzyme
    • Spreitzer R.J., and Salvucci M.E. Rubisco: interactions, associations and the possibilities of a better enzyme. Annu Rev Plant Biol 53 (2002) 449-475
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 40
    • 0027976415 scopus 로고
    • Discrimination against misacylated tRNA by chloroplast elongation factor Tu
    • Stanzel M., Schon A., and Sprinzl M. Discrimination against misacylated tRNA by chloroplast elongation factor Tu. Eur J Biochem 219 (1994) 435-439
    • (1994) Eur J Biochem , vol.219 , pp. 435-439
    • Stanzel, M.1    Schon, A.2    Sprinzl, M.3
  • 41
    • 0028097838 scopus 로고
    • Structure and differential expression of two distinct genes encoding chloroplast elongation factor Tu in tobacco
    • Sugita M., Murayama Y., and Sugiura M. Structure and differential expression of two distinct genes encoding chloroplast elongation factor Tu in tobacco. Curr Genet 25 (1994) 164-168
    • (1994) Curr Genet , vol.25 , pp. 164-168
    • Sugita, M.1    Murayama, Y.2    Sugiura, M.3
  • 42
    • 33947518803 scopus 로고    scopus 로고
    • Chaperone properties of mammalian mitochondrial translation elongation factor Tu
    • Suzuki H., Ueda T., Taguchi H., and Takeuchi N. Chaperone properties of mammalian mitochondrial translation elongation factor Tu. J Biol Chem 282 (2007) 4076-4084
    • (2007) J Biol Chem , vol.282 , pp. 4076-4084
    • Suzuki, H.1    Ueda, T.2    Taguchi, H.3    Takeuchi, N.4
  • 43
    • 0027137079 scopus 로고
    • Cloning and nucleotide sequence of a tobacco chloroplast translational elongation factor, EF-Tu
    • Ursin V.M., Becker C.K., and Shewmaker C.K. Cloning and nucleotide sequence of a tobacco chloroplast translational elongation factor, EF-Tu. Plant Physiol 101 (1993) 333-334
    • (1993) Plant Physiol , vol.101 , pp. 333-334
    • Ursin, V.M.1    Becker, C.K.2    Shewmaker, C.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.