메뉴 건너뛰기




Volumn 98, Issue 1-3, 2008, Pages 667-675

Directing the evolution of Rubisco and Rubisco activase: First impressions of a new tool for photosynthesis research

Author keywords

Activase; CO2 assimilation; Mutagenesis; Protein evolution; Rubisco; Sequence space

Indexed keywords

RCA PROTEIN, PLANT; RIBULOSEBISPHOSPHATE CARBOXYLASE; VEGETABLE PROTEIN;

EID: 57849104368     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-008-9324-z     Document Type: Review
Times cited : (71)

References (80)
  • 2
    • 0037561915 scopus 로고    scopus 로고
    • Structural framework for catalysis and regulation in ribulose-1,5- bisphosphate carboxylase/oxygenase
    • 10.1016/S0003-9861(03)00164-4
    • I Andersson TC Taylor 2003 Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase Arch Biochem Biophys 414 130 140 10.1016/S0003-9861(03)00164-4
    • (2003) Arch Biochem Biophys , vol.414 , pp. 130-140
    • Andersson, I.1    Taylor, T.C.2
  • 4
    • 0038576219 scopus 로고    scopus 로고
    • Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants
    • TJ Andrews SM Whitney 2003 Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants Arch Biochem Biophys 414 159 169
    • (2003) Arch Biochem Biophys , vol.414 , pp. 159-169
    • Andrews, T.J.1    Whitney, S.M.2
  • 5
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • 10.1021/ar960017f
    • FH Arnold 1998 Design by directed evolution Acc Chem Res 31 125 131 10.1021/ar960017f
    • (1998) Acc Chem Res , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 8
    • 0035252648 scopus 로고    scopus 로고
    • How enzymes adapt: Lessons from directed evolution
    • 10.1016/S0968-0004(00)01755-2
    • FH Arnold PL Wintrode K Miyazaki A Gershenson 2001 How enzymes adapt: lessons from directed evolution Trends Biochem Sci 26 100 106 10.1016/S0968-0004(00)01755-2
    • (2001) Trends Biochem Sci , vol.26 , pp. 100-106
    • Arnold, F.H.1    Wintrode, P.L.2    Miyazaki, K.3    Gershenson, A.4
  • 9
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between Rubisco-like protein of Bacillus and photosynthetic Rubisco
    • 10.1126/science.1086997
    • H Ashida Y Saito C Kojima K Kobayashi N Ogasawara A Yokota 2003 A functional link between Rubisco-like protein of Bacillus and photosynthetic Rubisco Science 302 286 290 10.1126/science.1086997
    • (2003) Science , vol.302 , pp. 286-290
    • Ashida, H.1    Saito, Y.2    Kojima, C.3    Kobayashi, K.4    Ogasawara, N.5    Yokota, A.6
  • 10
    • 20444419762 scopus 로고    scopus 로고
    • Was photosynthetic Rubisco recruited by acquisitive evolution from Rubisco-like proteins involved in sulfur metabolism?
    • 10.1016/j.resmic.2005.01.014
    • H Ashida A Danchin A Yokota 2005 Was photosynthetic Rubisco recruited by acquisitive evolution from Rubisco-like proteins involved in sulfur metabolism? Res Microbiol 156 611 618 10.1016/j.resmic.2005.01.014
    • (2005) Res Microbiol , vol.156 , pp. 611-618
    • Ashida, H.1    Danchin, A.2    Yokota, A.3
  • 12
    • 43049123356 scopus 로고    scopus 로고
    • Advances in laboratory evolution of enzymes
    • 10.1016/j.cbpa.2008.01.027
    • S Bershtein DS Tawfik 2008 Advances in laboratory evolution of enzymes Curr Opin Chem Biol 12 151 158 10.1016/j.cbpa.2008.01.027
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 151-158
    • Bershtein, S.1    Tawfik, D.S.2
  • 13
    • 2442668927 scopus 로고    scopus 로고
    • Discovery and directed evolution of a glyphosate tolerance gene
    • 10.1126/science.1096770
    • LA Castle DL Siehl R Gorton PA Patten YH Chen S Bertain 2004 Discovery and directed evolution of a glyphosate tolerance gene Science 304 1151 1154 10.1126/science.1096770
    • (2004) Science , vol.304 , pp. 1151-1154
    • Castle, L.A.1    Siehl, D.L.2    Gorton, R.3    Patten, P.A.4    Chen, Y.H.5    Bertain, S.6
  • 14
    • 0025719479 scopus 로고
    • 2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
    • 10.1021/bi00100a017
    • 2 specificity of chloroplast ribulose-1,5- bisphosphate carboxylase/oxygenase Biochemistry 30 8846 8850 10.1021/bi00100a017
    • (1991) Biochemistry , vol.30 , pp. 8846-8850
    • Chen, Z.1    Yu, W.2    Lee, J.-H.3    Diao, R.4    Spreitzer, R.J.5
  • 15
    • 0027744759 scopus 로고
    • Coexpression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli
    • 10.1007/BF00042362
    • LP Cloney DR Bekkaoui SM Hemmingsen 1993 Coexpression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli Plant Mol Biol 23 1285 1290 10.1007/BF00042362
    • (1993) Plant Mol Biol , vol.23 , pp. 1285-1290
    • Cloney, L.P.1    Bekkaoui, D.R.2    Hemmingsen, S.M.3
  • 17
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • 10.1038/34663
    • A Crameri SA Raillard E Bermudez WPC Stemmer 1998 DNA shuffling of a family of genes from diverse species accelerates directed evolution Nature 391 288 291 10.1038/34663
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 18
    • 34548018528 scopus 로고    scopus 로고
    • Mechanistic approaches to the study of evolution: The functional synthesis
    • 10.1038/nrg2160
    • AM Dean JW Thornton 2007 Mechanistic approaches to the study of evolution: the functional synthesis Nat Rev Genet 8 675 688 10.1038/nrg2160
    • (2007) Nat Rev Genet , vol.8 , pp. 675-688
    • Dean, A.M.1    Thornton, J.W.2
  • 20
    • 0034687777 scopus 로고    scopus 로고
    • RbcS suppressor mutations improve the thermal stability and CO2/O2 specificity of rbcL-mutant ribulose-1,5-bisphosphate carboxylase/oxygenase
    • 10.1073/pnas.260503997
    • YC Du SJ Hong RJ Spreitzer 2000 RbcS suppressor mutations improve the thermal stability and CO2/O2 specificity of rbcL-mutant ribulose-1,5- bisphosphate carboxylase/oxygenase Proc Natl Acad Sci USA 97 14206 14211 10.1073/pnas.260503997
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14206-14211
    • Du, Y.C.1    Hong, S.J.2    Spreitzer, R.J.3
  • 21
    • 0242573463 scopus 로고    scopus 로고
    • Nitrogen-regulated hypermutator strain of Synechococcus sp for use in in vivo artificial evolution
    • 10.1128/AEM.69.11.6427-6433.2003
    • D Emlyn-Jones GD Price TJ Andrews 2003 Nitrogen-regulated hypermutator strain of Synechococcus sp for use in in vivo artificial evolution Appl Environ Microbiol 69 6427 6433 10.1128/AEM.69.11.6427-6433.2003
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6427-6433
    • Emlyn-Jones, D.1    Price, G.D.2    Andrews, T.J.3
  • 22
    • 0037059460 scopus 로고    scopus 로고
    • Plant scientists see big potential in tiny plastids
    • 10.1126/science.295.5553.258
    • J Gewolb 2002 Plant scientists see big potential in tiny plastids Science 295 258 259 10.1126/science.295.5553.258
    • (2002) Science , vol.295 , pp. 258-259
    • Gewolb, J.1
  • 23
    • 34250700987 scopus 로고    scopus 로고
    • Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency
    • 10.1042/BJ20070071
    • DN Greene SM Whitney I Matsumura 2007 Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency Biochem J 404 517 524 10.1042/BJ20070071
    • (2007) Biochem J , vol.404 , pp. 517-524
    • Greene, D.N.1    Whitney, S.M.2    Matsumura, I.3
  • 24
    • 0037413687 scopus 로고    scopus 로고
    • Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization
    • 10.1093/emboj/cdg014
    • AD Griffiths DS Tawfik 2003 Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization EMBO J 22 24 35 10.1093/emboj/cdg014
    • (2003) EMBO J , vol.22 , pp. 24-35
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 26
    • 0035836695 scopus 로고    scopus 로고
    • A ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress
    • 10.1073/pnas.081610398
    • TE Hanson FR Tabita 2001 A ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress Proc Natl Acad Sci USA 98 4397 4402 10.1073/pnas.081610398
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 27
    • 0344518871 scopus 로고
    • Synthesis of spinach phosphoribulokinase and ribulose 1,5-bisphosphate in Escherichia coli
    • GS Hudson MK Morell YBC Arvidsson TJ Andrews 1992 Synthesis of spinach phosphoribulokinase and ribulose 1,5-bisphosphate in Escherichia coli Aust J Plant Physiol 19 213 221
    • (1992) Aust J Plant Physiol , vol.19 , pp. 213-221
    • Hudson, G.S.1    Morell, M.K.2    Arvidsson, Y.B.C.3    Andrews, T.J.4
  • 28
    • 33744512606 scopus 로고    scopus 로고
    • Directed evolution of enzymes and biosynthetic pathways
    • 10.1016/j.mib.2006.03.003
    • TW Johannes HM Zhao 2006 Directed evolution of enzymes and biosynthetic pathways Curr Opin Microbiol 9 261 267 10.1016/j.mib.2006.03.003
    • (2006) Curr Opin Microbiol , vol.9 , pp. 261-267
    • Johannes, T.W.1    Zhao, H.M.2
  • 29
    • 3342882580 scopus 로고    scopus 로고
    • 2 production by Rubisco
    • 10.1016/j.febslet.2004.06.064
    • 2 production by Rubisco FEBS Lett 571 124 128 10.1016/j.febslet.2004.06.064
    • (2004) FEBS Lett , vol.571 , pp. 124-128
    • Kim, K.1    Portis, A.R.2
  • 30
    • 37249051287 scopus 로고    scopus 로고
    • Enhanced thermostability of Arabidopsis Rubisco activase improves photosynthesis and growth rates under moderate heat stress
    • 10.1105/tpc.107.054171
    • I Kurek TK Chang SM Bertain A Madrigal L Liu MW Lassner 2007 Enhanced thermostability of Arabidopsis Rubisco activase improves photosynthesis and growth rates under moderate heat stress Plant Cell 19 3230 3241 10.1105/tpc.107.054171
    • (2007) Plant Cell , vol.19 , pp. 3230-3241
    • Kurek, I.1    Chang, T.K.2    Bertain, S.M.3    Madrigal, A.4    Liu, L.5    Lassner, M.W.6
  • 31
    • 0037011406 scopus 로고    scopus 로고
    • Screening and selection methods for large-scale analysis of protein function
    • HN Lin VW Cornish 2002 Screening and selection methods for large-scale analysis of protein function Angew Chem Int Ed 41 4403 4425
    • (2002) Angew Chem Int Ed , vol.41 , pp. 4403-4425
    • Lin, H.N.1    Cornish, V.W.2
  • 32
    • 33645023824 scopus 로고    scopus 로고
    • Can improvement in photosynthesis increase crop yields?
    • 10.1111/j.1365-3040.2005.01493.x
    • SP Long XG Zhu SL Naidu DR Ort 2006 Can improvement in photosynthesis increase crop yields? Plant Cell Environ 29 315 330 10.1111/j.1365-3040.2005. 01493.x
    • (2006) Plant Cell Environ , vol.29 , pp. 315-330
    • Long, S.P.1    Zhu, X.G.2    Naidu, S.L.3    Ort, D.R.4
  • 33
    • 0034490454 scopus 로고    scopus 로고
    • Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp PCC7002 (Cyanobacteria), and evidence that CcmM is essential for carboxysome assembly
    • 10.1046/j.1529-8817.2000.00028.x
    • M Ludwig D Sultemeyer GD Price 2000 Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp PCC7002 (Cyanobacteria), and evidence that CcmM is essential for carboxysome assembly J Phycol 36 1109 1118 10.1046/j.1529-8817.2000.00028.x
    • (2000) J Phycol , vol.36 , pp. 1109-1118
    • Ludwig, M.1    Sultemeyer, D.2    Price, G.D.3
  • 34
    • 0033555016 scopus 로고    scopus 로고
    • Genetic engineers aim to soup up crop photosynthesis
    • 10.1126/science.283.5400.314
    • CC Mann 1999 Genetic engineers aim to soup up crop photosynthesis Science 283 314 316 10.1126/science.283.5400.314
    • (1999) Science , vol.283 , pp. 314-316
    • Mann, C.C.1
  • 35
    • 2542536523 scopus 로고    scopus 로고
    • Mutagenic PCR of protein-coding genes for in vitro evolution
    • Humana Press Totowa
    • Matsumura I, Ellington AD (2002) Mutagenic PCR of protein-coding genes for in vitro evolution. In: Braman J (ed) Methods in molecular biology, vol 182. Humana Press, Totowa, pp 261-269
    • (2002) Methods in Molecular Biology , vol.182 , pp. 261-269
    • Matsumura, I.1    Ellington, A.D.2    Braman, J.3
  • 36
    • 0014935646 scopus 로고
    • Natural selection and concept of a protein space
    • 10.1038/225563a0
    • J Maynard Smith 1970 Natural selection and concept of a protein space Nature 225 563 564 10.1038/225563a0
    • (1970) Nature , vol.225 , pp. 563-564
    • Maynard Smith, J.1
  • 38
    • 84971054454 scopus 로고
    • Rubisco: Maladapted or misunderstood?
    • 10.1071/BT9920431
    • MK Morell K Paul HJ Kane TJ Andrews 1992 Rubisco: maladapted or misunderstood? Aust J Bot 40 431 441 10.1071/BT9920431
    • (1992) Aust J Bot , vol.40 , pp. 431-441
    • Morell, M.K.1    Paul, K.2    Kane, H.J.3    Andrews, T.J.4
  • 39
    • 50949090470 scopus 로고    scopus 로고
    • Evolving improved Synechococcus Rubisco functional expression in Escherichia coli
    • doi: 10.1042/BJ20080668
    • Mueller-Cajar O, Whitney SM (2008) Evolving improved Synechococcus Rubisco functional expression in Escherichia coli. Biochem J (May):19. doi: 10.1042/BJ20080668
    • (2008) Biochem J , Issue.MAY , pp. 19
    • Mueller-Cajar, O.1    Whitney, S.M.2
  • 40
    • 37049033685 scopus 로고    scopus 로고
    • Directed evolution of Rubisco in Escherichia coli reveals a specificity-determining hydrogen bond in the form II enzyme
    • 10.1021/bi700820a
    • O Mueller-Cajar M Morell SM Whitney 2007 Directed evolution of Rubisco in Escherichia coli reveals a specificity-determining hydrogen bond in the form II enzyme Biochemistry 46 14067 14074 10.1021/bi700820a
    • (2007) Biochemistry , vol.46 , pp. 14067-14074
    • Mueller-Cajar, O.1    Morell, M.2    Whitney, S.M.3
  • 41
    • 2542563521 scopus 로고    scopus 로고
    • Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution
    • 10.1093/nar/gkh315
    • C Neylon 2004 Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution Nucleic Acids Res 32 1448 1459 10.1093/nar/gkh315
    • (2004) Nucleic Acids Res , vol.32 , pp. 1448-1459
    • Neylon, C.1
  • 42
    • 0041859262 scopus 로고    scopus 로고
    • Affixing the O to Rubisco: Discovering the source of photorespiratory glycolate and its regulation
    • 10.1023/A:1024913925002
    • WL Ogren 2003 Affixing the O to Rubisco: discovering the source of photorespiratory glycolate and its regulation Photosynth Res 76 53 63 10.1023/A:1024913925002
    • (2003) Photosynth Res , vol.76 , pp. 53-63
    • Ogren, W.L.1
  • 43
    • 0031876149 scopus 로고    scopus 로고
    • Physiological control and regulation of the Rhodobacter capsulatus cbb operons
    • GC Paoli P Vichivanives FR Tabita 1998 Physiological control and regulation of the Rhodobacter capsulatus cbb operons J Bacteriol 180 4258 4269
    • (1998) J Bacteriol , vol.180 , pp. 4258-4269
    • Paoli, G.C.1    Vichivanives, P.2    Tabita, F.R.3
  • 44
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase
    • 10.1016/j.jmb.2005.07.020
    • MR Parikh I Matsumura 2005 Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase J Mol Biol 352 621 628 10.1016/j.jmb.2005.07.020
    • (2005) J Mol Biol , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 45
    • 33644980943 scopus 로고    scopus 로고
    • Directed evolution of Rubisco hypermorphs through genetic selection in engineered E. coli
    • 10.1093/protein/gzj010
    • MR Parikh DN Greene KK Woods I Matsumura 2006 Directed evolution of Rubisco hypermorphs through genetic selection in engineered E. coli Protein Eng Des Sel 19 113 119 10.1093/protein/gzj010
    • (2006) Protein Eng des Sel , vol.19 , pp. 113-119
    • Parikh, M.R.1    Greene, D.N.2    Woods, K.K.3    Matsumura, I.4
  • 46
    • 0037725392 scopus 로고    scopus 로고
    • Manipulation of Rubisco: The amount, activity, function and regulation
    • 10.1093/jxb/erg141
    • MAJ Parry PJ Andralojc RAC Mitchell PJ Madgwick AJ Keys 2003 Manipulation of Rubisco: the amount, activity, function and regulation J Exp Bot 54 1321 1333 10.1093/jxb/erg141
    • (2003) J Exp Bot , vol.54 , pp. 1321-1333
    • Parry, M.A.J.1    Andralojc, P.J.2    Mitchell, R.A.C.3    Madgwick, P.J.4    Keys, A.J.5
  • 47
    • 33847030362 scopus 로고    scopus 로고
    • Prospects from increasing photosynthesis by overcoming the limitations of Rubisco
    • 10.1017/S0021859606006666
    • MAJ Parry PJ Madgwick JFC Carvalho PJ Andralojc 2007 Prospects from increasing photosynthesis by overcoming the limitations of Rubisco J Agric Sci 145 31 43 10.1017/S0021859606006666
    • (2007) J Agric Sci , vol.145 , pp. 31-43
    • Parry, M.A.J.1    Madgwick, P.J.2    Carvalho, J.F.C.3    Andralojc, P.J.4
  • 48
    • 36749020130 scopus 로고    scopus 로고
    • Protein engineers turned evolutionists
    • 10.1038/nmeth1207-991
    • SG Peisajovich DS Tawfik 2007 Protein engineers turned evolutionists Nat Methods 4 991 994 10.1038/nmeth1207-991
    • (2007) Nat Methods , vol.4 , pp. 991-994
    • Peisajovich, S.G.1    Tawfik, D.S.2
  • 49
    • 0024713252 scopus 로고
    • A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe
    • 10.1073/pnas.86.15.5753
    • J Pierce TJ Carlson JGK Williams 1989 A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe Proc Natl Acad Sci USA 86 5753 5757 10.1073/pnas.86.15.5753
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5753-5757
    • Pierce, J.1    Carlson, T.J.2    Williams, J.G.K.3
  • 50
    • 33846551980 scopus 로고    scopus 로고
    • Empirical fitness landscapes reveal accessible evolutionary paths
    • 10.1038/nature05451
    • FJ Poelwijk DJ Kiviet DM Weinreich SJ Tans 2007 Empirical fitness landscapes reveal accessible evolutionary paths Nature 445 383 386 10.1038/nature05451
    • (2007) Nature , vol.445 , pp. 383-386
    • Poelwijk, F.J.1    Kiviet, D.J.2    Weinreich, D.M.3    Tans, S.J.4
  • 51
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase - Rubisco's catalytic chaperone
    • 10.1023/A:1022458108678
    • AR Portis 2003 Rubisco activase - Rubisco's catalytic chaperone Photosynth Res 75 11 27 10.1023/A:1022458108678
    • (2003) Photosynth Res , vol.75 , pp. 11-27
    • Portis, A.R.1
  • 52
    • 44649180011 scopus 로고    scopus 로고
    • i transporters, diversity, genetic regulation and prospects for engineering into plants
    • Epub 10.1093/jx b/erm112: erm112
    • i transporters, diversity, genetic regulation and prospects for engineering into plants. J Exp Bot Epub 10.1093/jx b/erm112: erm112
    • (2008) J Exp Bot
    • Price, G.D.1    Badger, M.R.2    Woodger, F.J.3    Long, B.M.4
  • 53
    • 13844281394 scopus 로고    scopus 로고
    • Directed evolution of proteins for heterologous expression and stability
    • 10.1016/j.sbi.2005.01.001
    • C Roodveldt A Aharoni DS Tawfik 2005 Directed evolution of proteins for heterologous expression and stability Curr Opin Struct Biol 15 50 56 10.1016/j.sbi.2005.01.001
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 50-56
    • Roodveldt, C.1    Aharoni, A.2    Tawfik, D.S.3
  • 54
    • 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
    • 10.1104/pp. 103.038323
    • ME Salvucci SJ Crafts-Brandner 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 1470 10.1104/pp. 103.038323
    • (2004) Plant Physiol , vol.134 , pp. 1460-1470
    • Salvucci, M.E.1    Crafts-Brandner, S.J.2
  • 55
    • 34250112628 scopus 로고
    • A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase oxygenase activation in vivo
    • 10.1007/BF00037012
    • ME Salvucci AR Portis Jr WL Ogren 1985 A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase oxygenase activation in vivo Photosynth Res 7 193 201 10.1007/BF00037012
    • (1985) Photosynth Res , vol.7 , pp. 193-201
    • Salvucci, M.E.1    Portis Jr., A.R.2    Ogren, W.L.3
  • 56
    • 33845251165 scopus 로고    scopus 로고
    • Effect of activase level and isoform on the thermotolerance of photosynthesis in Arabidopsis 10.1093/jxb/erl140
    • ME Salvucci BP DeRidder AR Portis Jr 2006 Effect of activase level and isoform on the thermotolerance of photosynthesis in Arabidopsis 10.1093/jxb/erl140 J Exp Bot 57 3793 3799
    • (2006) J Exp Bot , vol.57 , pp. 3793-3799
    • Salvucci, M.E.1    Deridder, B.P.2    Portis Jr., A.R.3
  • 57
    • 34250017377 scopus 로고    scopus 로고
    • Structure and Function of RbcX, an assembly chaperone for hexadecameric Rubisco
    • 10.1016/j.cell.2007.04.025
    • S Saschenbrecker A Bracher KV Rao BV Rao FU Hartl M Hayer-Hartl 2007 Structure and Function of RbcX, an assembly chaperone for hexadecameric Rubisco Cell 129 1189 1200 10.1016/j.cell.2007.04.025
    • (2007) Cell , vol.129 , pp. 1189-1200
    • Saschenbrecker, S.1    Bracher, A.2    Rao, K.V.3    Rao, B.V.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 58
    • 0033120651 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes
    • 10.1016/S0167-7799(98)01283-9
    • C Schmidt-Dannert FH Arnold 1999 Directed evolution of industrial enzymes Trends Biotechnol 17 135 136 10.1016/S0167-7799(98)01283-9
    • (1999) Trends Biotechnol , vol.17 , pp. 135-136
    • Schmidt-Dannert, C.1    Arnold, F.H.2
  • 59
    • 14644404385 scopus 로고    scopus 로고
    • Effects of moderate heat stress on photosynthesis: Importance of thylakoid reactions, rubisco deactivation, reactive oxygen species, and thermotolerance provided by isoprene
    • 10.1111/j.1365-3040.2005.01324.x
    • TD Sharkey 2005 Effects of moderate heat stress on photosynthesis: importance of thylakoid reactions, rubisco deactivation, reactive oxygen species, and thermotolerance provided by isoprene Plant Cell Environ 28 269 277 10.1111/j.1365-3040.2005.01324.x
    • (2005) Plant Cell Environ , vol.28 , pp. 269-277
    • Sharkey, T.D.1
  • 60
    • 0041663412 scopus 로고    scopus 로고
    • Positive and negative selection of mutant forms of prokaryotic (cyanobacterial) ribulose-1,5-bisphosphate carboxylase/oxygenase
    • 10.1016/S0022-2836(03)00786-1
    • SA Smith FR Tabita 2003 Positive and negative selection of mutant forms of prokaryotic (cyanobacterial) ribulose-1,5-bisphosphate carboxylase/oxygenase J Mol Biol 331 557 569 10.1016/S0022-2836(03)00786-1
    • (2003) J Mol Biol , vol.331 , pp. 557-569
    • Smith, S.A.1    Tabita, F.R.2
  • 61
    • 0000044510 scopus 로고
    • Genetic modification of photorespiration
    • 10.1016/0968-0004(82)90130-X
    • CR Somerville WL Ogren 1982 Genetic modification of photorespiration Trends Biochem Sci 7 171 174 10.1016/0968-0004(82)90130-X
    • (1982) Trends Biochem Sci , vol.7 , pp. 171-174
    • Somerville, C.R.1    Ogren, W.L.2
  • 62
    • 0001596719 scopus 로고
    • A mutant of Arabidopsis thaliana which lacks activation of RuBP carboxylase in vivo
    • CR Somerville AR Portis Jr WL Ogren 1982 A mutant of Arabidopsis thaliana which lacks activation of RuBP carboxylase in vivo Plant Physiol 70 381 387
    • (1982) Plant Physiol , vol.70 , pp. 381-387
    • Somerville, C.R.1    Portis Jr., A.R.2    Ogren, W.L.3
  • 63
    • 0001297575 scopus 로고
    • Genetic dissection of Rubisco structure and function
    • 10.1146/annurev.pp. 44.060193.002211
    • RJ Spreitzer 1993 Genetic dissection of Rubisco structure and function Annu Rev Plant Physiol Plant Mol Biol 44 411 434 10.1146/annurev.pp. 44.060193.002211
    • (1993) Annu Rev Plant Physiol Plant Mol Biol , vol.44 , pp. 411-434
    • Spreitzer, R.J.1
  • 65
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • 10.1146/annurev.arplant.53.100301.135233
    • RJ Spreitzer ME Salvucci 2002 Rubisco: structure, regulatory interactions, and possibilities for a better enzyme Annu Rev Plant Biol 53 449 475 10.1146/annurev.arplant.53.100301.135233
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 66
    • 28044454726 scopus 로고    scopus 로고
    • Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco
    • 10.1073/pnas.0508042102
    • RJ Spreitzer SR Peddi S Satagopan 2005 Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco Proc Natl Acad Sci USA 102 17225 17230 10.1073/pnas.0508042102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17225-17230
    • Spreitzer, R.J.1    Peddi, S.R.2    Satagopan, S.3
  • 67
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly - In-vitro recombination for molecular evolution
    • 10.1073/pnas.91.22.10747
    • WPC Stemmer 1994 DNA shuffling by random fragmentation and reassembly - in-vitro recombination for molecular evolution Proc Natl Acad Sci USA 91 10747 10751 10.1073/pnas.91.22.10747
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 68
    • 44649191875 scopus 로고    scopus 로고
    • Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships
    • erm361
    • Tabita FR, Satagopan S, Hanson TE, Kreel NE, Scott SS (2008) Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships. J Exp Bot 59(7):1515-1524. erm361
    • (2008) J Exp Bot , vol.59 , Issue.7 , pp. 1515-1524
    • Tabita, F.R.1    Satagopan, S.2    Hanson, T.E.3    Kreel, N.E.4    Scott, S.S.5
  • 69
    • 33646583168 scopus 로고    scopus 로고
    • Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
    • 10.1073/pnas.0600605103
    • GB Tcherkez GD Farquhar TJ Andrews 2006 Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized Proc Natl Acad Sci USA 103 7246 7251 10.1073/pnas.0600605103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7246-7251
    • Tcherkez, G.B.1    Farquhar, G.D.2    Andrews, T.J.3
  • 70
    • 0028336813 scopus 로고
    • Complementing substitutions within loop regions 2 and 3 of the α/β-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
    • 10.1021/bi00183a014
    • G Thow G Zhu RJ Spreitzer 1994 Complementing substitutions within loop regions 2 and 3 of the α/β-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase Biochemistry 33 5109 5114 10.1021/bi00183a014
    • (1994) Biochemistry , vol.33 , pp. 5109-5114
    • Thow, G.1    Zhu, G.2    Spreitzer, R.J.3
  • 71
    • 0033770580 scopus 로고    scopus 로고
    • Rational evolutionary design: The theory of in vitro protein evolution
    • CA Voigt S Kauffman ZG Wang 2001 Rational evolutionary design: the theory of in vitro protein evolution Adv Protein Chem 55 79 160
    • (2001) Adv Protein Chem , vol.55 , pp. 79-160
    • Voigt, C.A.1    Kauffman, S.2    Wang, Z.G.3
  • 72
    • 0037304389 scopus 로고    scopus 로고
    • Genetic screens and directed evolution for protein solubility
    • 10.1016/S1367-5931(02)00017-0
    • GS Waldo 2003 Genetic screens and directed evolution for protein solubility Curr Opin Chem Biol 7 33 38 10.1016/S1367-5931(02)00017-0
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 33-38
    • Waldo, G.S.1
  • 73
    • 0031024440 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A molecule for phylogenetic and enzymological investigation
    • 10.1111/j.1574-6968.1997.tb10165.x
    • GMF Watson FR Tabita 1997 Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: a molecule for phylogenetic and enzymological investigation FEMS Microbiol Lett 146 13 22 10.1111/j.1574-6968.1997.tb10165.x
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 13-22
    • Watson, G.M.F.1    Tabita, F.R.2
  • 74
    • 33947534842 scopus 로고    scopus 로고
    • Linked Rubisco subunits can assemble into functional oligomers without impeding catalytic performance
    • 10.1074/jbc.M610479200
    • SM Whitney RE Sharwood 2007 Linked Rubisco subunits can assemble into functional oligomers without impeding catalytic performance J Biol Chem 282 3809 3818 10.1074/jbc.M610479200
    • (2007) J Biol Chem , vol.282 , pp. 3809-3818
    • Whitney, S.M.1    Sharwood, R.E.2
  • 75
    • 0034914259 scopus 로고    scopus 로고
    • Form I Rubiscos from non-green algae are expressed abundantly but not assembled in tobacco chloroplasts
    • 10.1046/j.1365-313x.2001.01056.x
    • SM Whitney P Baldet GS Hudson TJ Andrews 2001 Form I Rubiscos from non-green algae are expressed abundantly but not assembled in tobacco chloroplasts Plant J 26 535 547 10.1046/j.1365-313x.2001.01056.x
    • (2001) Plant J , vol.26 , pp. 535-547
    • Whitney, S.M.1    Baldet, P.2    Hudson, G.S.3    Andrews, T.J.4
  • 76
    • 0034730971 scopus 로고    scopus 로고
    • Photorespiration: Metabolic pathways and their role in stress protection
    • 10.1098/rstb.2000.0712
    • A Wingler PJ Lea WP Quick RC Leegood 2000 Photorespiration: metabolic pathways and their role in stress protection Philos Trans R Soc Lond B Biol Sci 355 1517 1529 10.1098/rstb.2000.0712
    • (2000) Philos Trans R Soc Lond B Biol Sci , vol.355 , pp. 1517-1529
    • Wingler, A.1    Lea, P.J.2    Quick, W.P.3    Leegood, R.C.4
  • 77
    • 2342562489 scopus 로고    scopus 로고
    • Deciphering enzymes - Genetic selection as a probe of structure and mechanism
    • 10.1111/j.1432-1033.2004.04073.x
    • KJ Woycechowsky D Hilvert 2004 Deciphering enzymes - genetic selection as a probe of structure and mechanism Eur J Biochem 271 1630 1637 10.1111/j.1432-1033.2004.04073.x
    • (2004) Eur J Biochem , vol.271 , pp. 1630-1637
    • Woycechowsky, K.J.1    Hilvert, D.2
  • 78
    • 33646178621 scopus 로고    scopus 로고
    • Designed divergent evolution of enzyme function
    • 10.1038/nature04607
    • Y Yoshikuni TE Ferrin JD Keasling 2006 Designed divergent evolution of enzyme function Nature 440 1078 1082 10.1038/nature04607
    • (2006) Nature , vol.440 , pp. 1078-1082
    • Yoshikuni, Y.1    Ferrin, T.E.2    Keasling, J.D.3
  • 79
    • 24944455200 scopus 로고    scopus 로고
    • Laboratory-directed protein evolution
    • 10.1128/MMBR.69.3.373-392.2005
    • L Yuan I Kurek J English R Keenan 2005 Laboratory-directed protein evolution Microbiol Mol Biol Rev 69 373 10.1128/MMBR.69.3.373-392.2005
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 373
    • Yuan, L.1    Kurek, I.2    English, J.3    Keenan, R.4
  • 80
    • 1242344163 scopus 로고    scopus 로고
    • 3 crop plants with foreign Rubisco increase productivity? a computational analysis extrapolating from kinetic properties to canopy photosynthesis
    • 10.1046/j.1365-3040.2004.01142.x
    • 3 crop plants with foreign Rubisco increase productivity? A computational analysis extrapolating from kinetic properties to canopy photosynthesis Plant Cell Environ 27 155 165 10.1046/j.1365-3040.2004.01142.x
    • (2004) Plant Cell Environ , vol.27 , pp. 155-165
    • Zhu, X.G.1    Portis, A.R.2    Long, S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.