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Volumn 18, Issue 12, 2013, Pages 688-694

The complexity of chloroplast chaperonins

Author keywords

Chaperone; Chaperonin; Chloroplast; Protein folding; Rubisco

Indexed keywords

CHAPERONE; CHAPERONIN; CHLOROPLAST PROTEIN; ISOPROTEIN; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 84888432741     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2013.08.001     Document Type: Review
Times cited : (47)

References (81)
  • 1
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts
    • Barraclough R., Ellis R.J. Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim. Biophys. Acta 1980, 608:19-31.
    • (1980) Biochim. Biophys. Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 2
    • 0024755607 scopus 로고
    • Rubisco assembly: a model system for studying the mechanism of chaperonin action
    • Roy H. Rubisco assembly: a model system for studying the mechanism of chaperonin action. Plant Cell 1989, 1:1035-1042.
    • (1989) Plant Cell , vol.1 , pp. 1035-1042
    • Roy, H.1
  • 3
    • 0025667365 scopus 로고
    • Molecular chaperones: the plant connection
    • Ellis R.J. Molecular chaperones: the plant connection. Science 1990, 250:954-959.
    • (1990) Science , vol.250 , pp. 954-959
    • Ellis, R.J.1
  • 4
    • 0023900525 scopus 로고
    • Homologous plant and bacterial proteins chaperone oligomeric protein assembly
    • Hemmingsen S.M., et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 1988, 333:330-334.
    • (1988) Nature , vol.333 , pp. 330-334
    • Hemmingsen, S.M.1
  • 5
    • 0025251691 scopus 로고
    • Chaperone function: the assembly of ribulose bisphosphate carboxylase-oxygenase
    • Gatenby A.A., Ellis R.J. Chaperone function: the assembly of ribulose bisphosphate carboxylase-oxygenase. Annu. Rev. Cell Biol. 1990, 6:125-149.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 125-149
    • Gatenby, A.A.1    Ellis, R.J.2
  • 6
    • 0026014687 scopus 로고
    • The universally conserved GroE (Hsp60) chaperonins
    • Zeilstra-Ryalls J., et al. The universally conserved GroE (Hsp60) chaperonins. Annu. Rev. Microbiol. 1991, 45:301-325.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 301-325
    • Zeilstra-Ryalls, J.1
  • 7
    • 0024578552 scopus 로고
    • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff P., et al. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 1989, 337:44-47.
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1
  • 8
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J.P., Hartl F.U. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 1993, 62:349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 9
    • 0031684079 scopus 로고    scopus 로고
    • Structure and function in GroEL-mediated protein folding
    • Sigler P.B., et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 1998, 67:581-608.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 581-608
    • Sigler, P.B.1
  • 10
    • 36949033246 scopus 로고    scopus 로고
    • Two families of chaperonin: physiology and mechanism
    • Horwich A.L., et al. Two families of chaperonin: physiology and mechanism. Annu. Rev. Cell Dev. Biol. 2007, 23:115-145.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 115-145
    • Horwich, A.L.1
  • 11
    • 0029066222 scopus 로고
    • Functional characterization of the higher plant chloroplast chaperonins
    • Viitanen P.V., et al. Functional characterization of the higher plant chloroplast chaperonins. J. Biol. Chem. 1995, 270:18158-18164.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18158-18164
    • Viitanen, P.V.1
  • 12
    • 0024850774 scopus 로고
    • Cloning and characterization of the yeast chaperonin HSP60 gene
    • Johnson R.B., et al. Cloning and characterization of the yeast chaperonin HSP60 gene. Gene 1989, 84:295-302.
    • (1989) Gene , vol.84 , pp. 295-302
    • Johnson, R.B.1
  • 13
    • 0023657522 scopus 로고
    • Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits
    • Musgrove J.E., et al. Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits. Eur. J. Biochem. 1987, 163:529-534.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 529-534
    • Musgrove, J.E.1
  • 14
    • 0025200907 scopus 로고
    • Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent
    • Martel R., et al. Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent. Gene 1990, 94:181-187.
    • (1990) Gene , vol.94 , pp. 181-187
    • Martel, R.1
  • 15
    • 0033590077 scopus 로고    scopus 로고
    • Chloroplast chaperonins: evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer
    • Nishio K., et al. Chloroplast chaperonins: evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer. Biochem. Biophys. Res. Commun. 1999, 266:584-587.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 584-587
    • Nishio, K.1
  • 16
    • 0028431010 scopus 로고
    • Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides
    • Cloney L.P., et al. Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides. Plant Physiol. 1994, 105:233-241.
    • (1994) Plant Physiol. , vol.105 , pp. 233-241
    • Cloney, L.P.1
  • 17
    • 0034809742 scopus 로고    scopus 로고
    • Arabidopsis thaliana type I and II chaperonins
    • Hill J.E., Hemmingsen S.M. Arabidopsis thaliana type I and II chaperonins. Cell Stress Chaperones 2001, 6:190-200.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 190-200
    • Hill, J.E.1    Hemmingsen, S.M.2
  • 18
    • 0028933373 scopus 로고
    • In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP
    • Lissin N.M. In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP. FEBS Lett. 1995, 361:55-60.
    • (1995) FEBS Lett. , vol.361 , pp. 55-60
    • Lissin, N.M.1
  • 19
    • 0034697297 scopus 로고    scopus 로고
    • Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding
    • Dickson R., et al. Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding. J. Biol. Chem. 2000, 275:11829-11835.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11829-11835
    • Dickson, R.1
  • 20
    • 70350517984 scopus 로고    scopus 로고
    • Differential effects of co-chaperonin homologs on cpn60 oligomers
    • Bonshtien A.L., et al. Differential effects of co-chaperonin homologs on cpn60 oligomers. Cell Stress Chaperones 2009, 14:509-519.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 509-519
    • Bonshtien, A.L.1
  • 21
    • 0027363793 scopus 로고
    • Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES
    • Rospert S., et al. Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES. FEBS Lett. 1993, 335:358-360.
    • (1993) FEBS Lett. , vol.335 , pp. 358-360
    • Rospert, S.1
  • 22
    • 0037208893 scopus 로고    scopus 로고
    • Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter
    • Hansen J.J., et al. Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. Hum. Genet. 2003, 112:71-77.
    • (2003) Hum. Genet. , vol.112 , pp. 71-77
    • Hansen, J.J.1
  • 23
    • 0035839528 scopus 로고    scopus 로고
    • Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana
    • Koumoto Y., et al. Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana. J. Biol. Chem. 2001, 276:29688-29694.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29688-29694
    • Koumoto, Y.1
  • 24
    • 1242341391 scopus 로고    scopus 로고
    • On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20
    • Sharkia R., et al. On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20. Biochim. Biophys. Acta 2003, 1651:76-84.
    • (2003) Biochim. Biophys. Acta , vol.1651 , pp. 76-84
    • Sharkia, R.1
  • 25
    • 0026744722 scopus 로고
    • Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants
    • Bertsch U., et al. Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:8696-8700.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8696-8700
    • Bertsch, U.1
  • 26
    • 0028921271 scopus 로고
    • Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60
    • Baneyx F., et al. Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60. J. Biol. Chem. 1995, 270:10695-10702.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10695-10702
    • Baneyx, F.1
  • 27
    • 0033103962 scopus 로고    scopus 로고
    • Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana
    • Koumoto Y., et al. Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana. Plant J. 1999, 17:467-477.
    • (1999) Plant J. , vol.17 , pp. 467-477
    • Koumoto, Y.1
  • 28
    • 84872248851 scopus 로고    scopus 로고
    • P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli
    • Vitlin Gruber A., et al. P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. PLoS ONE 2013, 8:e53909.
    • (2013) PLoS ONE , vol.8
    • Vitlin Gruber, A.1
  • 29
    • 84862025119 scopus 로고    scopus 로고
    • Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes
    • Tsai Y.C., et al. Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes. J. Biol. Chem. 2012, 287:20471-20481.
    • (2012) J. Biol. Chem. , vol.287 , pp. 20471-20481
    • Tsai, Y.C.1
  • 30
    • 33947516022 scopus 로고    scopus 로고
    • Significance of the N-terminal domain for the function of chloroplast cpn20 chaperonin
    • Bonshtien A.L., et al. Significance of the N-terminal domain for the function of chloroplast cpn20 chaperonin. J. Biol. Chem. 2007, 282:4463-4469.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4463-4469
    • Bonshtien, A.L.1
  • 31
    • 84884973475 scopus 로고    scopus 로고
    • Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions
    • Henderson B., et al. Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions. Biol. Rev. Camb. Philos. Soc. 2013, 10.1111/brv.12037.
    • (2013) Biol. Rev. Camb. Philos. Soc.
    • Henderson, B.1
  • 32
    • 66749187185 scopus 로고    scopus 로고
    • Multiple chaperonins in bacteria-why so many?
    • Lund P.A. Multiple chaperonins in bacteria-why so many?. FEMS Microbiol. Rev. 2009, 33:785-800.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 785-800
    • Lund, P.A.1
  • 33
    • 0030194514 scopus 로고    scopus 로고
    • Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus
    • Bonk M., et al. Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus. Plant Physiol. 1996, 111:931-939.
    • (1996) Plant Physiol. , vol.111 , pp. 931-939
    • Bonk, M.1
  • 34
    • 0001643571 scopus 로고
    • Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein
    • Hemmingsen S.M., Ellis R.J. Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein. Plant Physiol. 1986, 80:269-276.
    • (1986) Plant Physiol. , vol.80 , pp. 269-276
    • Hemmingsen, S.M.1    Ellis, R.J.2
  • 35
    • 0026481083 scopus 로고
    • Expression of plant chaperonin-60 genes in Escherichia coli
    • Cloney L.P., et al. Expression of plant chaperonin-60 genes in Escherichia coli. J. Biol. Chem. 1992, 267:23327-23332.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23327-23332
    • Cloney, L.P.1
  • 36
    • 0026478888 scopus 로고
    • Assessment of plant chaperonin-60 gene function in Escherichia coli
    • Cloney L.P., et al. Assessment of plant chaperonin-60 gene function in Escherichia coli. J. Biol. Chem. 1992, 267:23333-23336.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23333-23336
    • Cloney, L.P.1
  • 37
    • 80051900180 scopus 로고    scopus 로고
    • Chloroplast beta chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro
    • Vitlin A., et al. Chloroplast beta chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro. Plant Mol. Biol. 2011, 77:105-115.
    • (2011) Plant Mol. Biol. , vol.77 , pp. 105-115
    • Vitlin, A.1
  • 38
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential for folding of a specific substrate
    • Peng L., et al. A chaperonin subunit with unique structures is essential for folding of a specific substrate. PLoS Biol. 2011, 9:e1001040.
    • (2011) PLoS Biol. , vol.9
    • Peng, L.1
  • 39
    • 0034598920 scopus 로고    scopus 로고
    • Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
    • Farr G.W., et al. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. Cell 2000, 100:561-573.
    • (2000) Cell , vol.100 , pp. 561-573
    • Farr, G.W.1
  • 40
    • 65249090789 scopus 로고    scopus 로고
    • Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for plastid division in Arabidopsis thaliana
    • Suzuki K., et al. Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for plastid division in Arabidopsis thaliana. BMC Plant Biol. 2009, 9:38.
    • (2009) BMC Plant Biol. , vol.9 , pp. 38
    • Suzuki, K.1
  • 41
    • 0034979913 scopus 로고    scopus 로고
    • The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60α gene
    • Apuya N.R., et al. The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60α gene. Plant Physiol. 2001, 126:717-730.
    • (2001) Plant Physiol. , vol.126 , pp. 717-730
    • Apuya, N.R.1
  • 42
    • 0037364978 scopus 로고    scopus 로고
    • Deletion of a chaperonin 60 beta gene leads to cell death in the Arabidopsis lesion initiation 1 mutant
    • Ishikawa A., et al. Deletion of a chaperonin 60 beta gene leads to cell death in the Arabidopsis lesion initiation 1 mutant. Plant Cell Physiol. 2003, 44:255-261.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 255-261
    • Ishikawa, A.1
  • 43
    • 58549113565 scopus 로고    scopus 로고
    • Cpn20: siamese twins of the chaperonin world
    • Weiss C., et al. Cpn20: siamese twins of the chaperonin world. Plant Mol. Biol. 2009, 69:227-238.
    • (2009) Plant Mol. Biol. , vol.69 , pp. 227-238
    • Weiss, C.1
  • 44
    • 44649175852 scopus 로고    scopus 로고
    • Association of Rubisco activase with chaperonin-60β: a possible mechanism for protecting photosynthesis during heat stress
    • Salvucci M.E. Association of Rubisco activase with chaperonin-60β: a possible mechanism for protecting photosynthesis during heat stress. J. Exp. Bot. 2008, 59:1923-1933.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1923-1933
    • Salvucci, M.E.1
  • 45
    • 0028105690 scopus 로고
    • Expression of one of the members of the Arabidopsis chaperonin 60 beta gene family is developmentally regulated and wound-repressible
    • Zabaleta E., et al. Expression of one of the members of the Arabidopsis chaperonin 60 beta gene family is developmentally regulated and wound-repressible. Plant Mol. Biol. 1994, 24:195-202.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 195-202
    • Zabaleta, E.1
  • 46
    • 79951681576 scopus 로고    scopus 로고
    • Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
    • Finka A., et al. Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 2011, 16:15-31.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 15-31
    • Finka, A.1
  • 47
    • 84884502211 scopus 로고    scopus 로고
    • Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis
    • Zhang X.F., et al. Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis. Plant Mol. Biol. 2013, 10.1007/s11103-013-0082-8.
    • (2013) Plant Mol. Biol.
    • Zhang, X.F.1
  • 48
    • 84873546706 scopus 로고    scopus 로고
    • Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD)
    • Kuo W.Y., et al. Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD). Plant Signal. Behav. 2013, 8:e23074.
    • (2013) Plant Signal. Behav. , vol.8
    • Kuo, W.Y.1
  • 49
    • 84870249599 scopus 로고    scopus 로고
    • CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts
    • Kuo W.Y., et al. CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts. New Phytol. 2012, 197:99-110.
    • (2012) New Phytol. , vol.197 , pp. 99-110
    • Kuo, W.Y.1
  • 50
    • 0034726456 scopus 로고    scopus 로고
    • Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein
    • Yang T., Poovaiah B.W. Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein. Biochem. Biophys. Res. Commun. 2000, 275:601-607.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 601-607
    • Yang, T.1    Poovaiah, B.W.2
  • 51
    • 0027142232 scopus 로고
    • Newly imported Rieske iron-sulfur protein associates with both Cpn60 and Hsp70 in the chloroplast stroma
    • Madueno F., et al. Newly imported Rieske iron-sulfur protein associates with both Cpn60 and Hsp70 in the chloroplast stroma. Plant Cell 1993, 5:1865-1876.
    • (1993) Plant Cell , vol.5 , pp. 1865-1876
    • Madueno, F.1
  • 52
    • 0027536925 scopus 로고
    • + reductase upon its import into chloroplasts
    • + reductase upon its import into chloroplasts. FEBS Lett. 1993, 320:198-202.
    • (1993) FEBS Lett. , vol.320 , pp. 198-202
    • Tsugeki, R.1    Nishimura, M.2
  • 53
    • 0024773203 scopus 로고
    • Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone
    • Lubben T.H., et al. Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone. Plant Cell 1989, 1:1223-1230.
    • (1989) Plant Cell , vol.1 , pp. 1223-1230
    • Lubben, T.H.1
  • 54
    • 0027970292 scopus 로고
    • Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multisubunit coupling factor CF1 core
    • Chen G.G., Jagendorf A.T. Chloroplast molecular chaperone-assisted refolding and reconstitution of an active multisubunit coupling factor CF1 core. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:11497-11501.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11497-11501
    • Chen, G.G.1    Jagendorf, A.T.2
  • 55
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries of the chloroplast
    • Kessler F., Blobel G. Interaction of the protein import and folding machineries of the chloroplast. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:7684-7689.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 56
    • 0030849191 scopus 로고    scopus 로고
    • Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly
    • Bonk M., et al. Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly. Eur. J. Biochem. 1997, 247:942-950.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 942-950
    • Bonk, M.1
  • 57
    • 0026508705 scopus 로고
    • Isolation and characterization of genes encoding chaperonin 60 beta from Arabidopsis thaliana
    • Zabaleta E., et al. Isolation and characterization of genes encoding chaperonin 60 beta from Arabidopsis thaliana. Gene 1992, 111:175-181.
    • (1992) Gene , vol.111 , pp. 175-181
    • Zabaleta, E.1
  • 58
    • 0030462854 scopus 로고    scopus 로고
    • Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions
    • Schmitz G., et al. Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions. Planta 1996, 200:326-336.
    • (1996) Planta , vol.200 , pp. 326-336
    • Schmitz, G.1
  • 59
    • 34447295076 scopus 로고    scopus 로고
    • Silencing of chaperonin 21, that was differentially expressed in inflorescence of seedless and seeded grapes, promoted seed abortion in tobacco and tomato fruits
    • Hanania U., et al. Silencing of chaperonin 21, that was differentially expressed in inflorescence of seedless and seeded grapes, promoted seed abortion in tobacco and tomato fruits. Transgenic Res. 2007, 16:515-525.
    • (2007) Transgenic Res. , vol.16 , pp. 515-525
    • Hanania, U.1
  • 60
    • 0028843014 scopus 로고
    • Rubisco synthesis, assembly, mechanism, and regulation
    • Gutteridge S., Gatenby A.A. Rubisco synthesis, assembly, mechanism, and regulation. Plant Cell 1995, 7:809-819.
    • (1995) Plant Cell , vol.7 , pp. 809-819
    • Gutteridge, S.1    Gatenby, A.A.2
  • 61
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston R.S., et al. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 1996, 32:191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1
  • 62
    • 84867032700 scopus 로고    scopus 로고
    • Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize
    • Feiz L., et al. Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize. Plant Cell 2012, 24:3435-3446.
    • (2012) Plant Cell , vol.24 , pp. 3435-3446
    • Feiz, L.1
  • 63
    • 0030970919 scopus 로고    scopus 로고
    • Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene
    • Li L.A., Tabita F.R. Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene. J. Bacteriol. 1997, 179:3793-3796.
    • (1997) J. Bacteriol. , vol.179 , pp. 3793-3796
    • Li, L.A.1    Tabita, F.R.2
  • 64
    • 9244232372 scopus 로고    scopus 로고
    • The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli
    • Onizuka T., et al. The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli. Plant Cell Physiol. 2004, 45:1390-1395.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1390-1395
    • Onizuka, T.1
  • 65
    • 33845698888 scopus 로고    scopus 로고
    • RbcX can function as a rubisco chaperonin, but is non-essential in Synechococcus PCC7942
    • Emlyn-Jones D., et al. RbcX can function as a rubisco chaperonin, but is non-essential in Synechococcus PCC7942. Plant Cell Physiol. 2006, 47:1630-1640.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1630-1640
    • Emlyn-Jones, D.1
  • 66
    • 34250017377 scopus 로고    scopus 로고
    • Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco
    • Saschenbrecker S., et al. Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco. Cell 2007, 129:1189-1200.
    • (2007) Cell , vol.129 , pp. 1189-1200
    • Saschenbrecker, S.1
  • 67
    • 79961027721 scopus 로고    scopus 로고
    • Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco
    • Bracher A., et al. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat. Struct. Mol. Biol. 2011, 18:875-880.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 875-880
    • Bracher, A.1
  • 68
    • 74549200552 scopus 로고    scopus 로고
    • Coupled chaperone action in folding and assembly of hexadecameric Rubisco
    • Liu C., et al. Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature 2010, 463:197-202.
    • (2010) Nature , vol.463 , pp. 197-202
    • Liu, C.1
  • 69
    • 80054020146 scopus 로고    scopus 로고
    • Initial characteristics of RbcX proteins from Arabidopsis thaliana
    • Kolesinski P., et al. Initial characteristics of RbcX proteins from Arabidopsis thaliana. Plant Mol. Biol. 2011, 77:447-459.
    • (2011) Plant Mol. Biol. , vol.77 , pp. 447-459
    • Kolesinski, P.1
  • 70
    • 84873738356 scopus 로고    scopus 로고
    • Insights into eukaryotic Rubisco assembly - crystal structures of RbcX chaperones from Arabidopsis thaliana
    • Kolesinski P., et al. Insights into eukaryotic Rubisco assembly - crystal structures of RbcX chaperones from Arabidopsis thaliana. Biochim. Biophys. Acta 2013, 1830:2899-2906.
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 2899-2906
    • Kolesinski, P.1
  • 71
    • 0033133350 scopus 로고    scopus 로고
    • BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize
    • Brutnell T.P., et al. BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize. Plant Cell 1999, 11:849-864.
    • (1999) Plant Cell , vol.11 , pp. 849-864
    • Brutnell, T.P.1
  • 72
    • 0028057089 scopus 로고
    • Antisense expression of chaperonin 60 beta in transgenic tobacco plants leads to abnormal phenotypes and altered distribution of photoassimilates
    • Zabaleta E., et al. Antisense expression of chaperonin 60 beta in transgenic tobacco plants leads to abnormal phenotypes and altered distribution of photoassimilates. Plant J. 1994, 6:425-432.
    • (1994) Plant J. , vol.6 , pp. 425-432
    • Zabaleta, E.1
  • 73
    • 0001829914 scopus 로고
    • Nuclear mutants of maize with defects in chloroplast polysome assembly have altered chloroplast RNA metabolism
    • Barkan A. Nuclear mutants of maize with defects in chloroplast polysome assembly have altered chloroplast RNA metabolism. Plant Cell 1993, 5:389-402.
    • (1993) Plant Cell , vol.5 , pp. 389-402
    • Barkan, A.1
  • 74
    • 84879089641 scopus 로고    scopus 로고
    • OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL
    • Kim S.R., et al. OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL. Mol. Cells 2013, 35:402-409.
    • (2013) Mol. Cells , vol.35 , pp. 402-409
    • Kim, S.R.1
  • 75
    • 33947433661 scopus 로고    scopus 로고
    • Only one of five groEL genes is required for viability and successful symbiosis in Sinorhizobium meliloti
    • Bittner A.N., et al. Only one of five groEL genes is required for viability and successful symbiosis in Sinorhizobium meliloti. J. Bacteriol. 2007, 189:1884-1889.
    • (2007) J. Bacteriol. , vol.189 , pp. 1884-1889
    • Bittner, A.N.1
  • 76
    • 28344453690 scopus 로고    scopus 로고
    • GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria
    • Ojha A., et al. GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria. Cell 2005, 123:861-873.
    • (2005) Cell , vol.123 , pp. 861-873
    • Ojha, A.1
  • 77
    • 34548043303 scopus 로고    scopus 로고
    • Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent
    • Gould P.S., et al. Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent. Cell Stress Chaperones 2007, 12:123-131.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 123-131
    • Gould, P.S.1
  • 78
    • 1642431647 scopus 로고    scopus 로고
    • The use of DsRED in single- and dual-color fluorescence labeling of mitochondrial and plastid organelles in Plasmodium falciparum
    • Sato S., Wilson R.J. The use of DsRED in single- and dual-color fluorescence labeling of mitochondrial and plastid organelles in Plasmodium falciparum. Mol. Biochem. Parasitol. 2004, 134:175-179.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 175-179
    • Sato, S.1    Wilson, R.J.2
  • 79
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals N-terminal modifications and abundance of the chloroplast proteome
    • Zybailov B., et al. Sorting signals N-terminal modifications and abundance of the chloroplast proteome. PLoS One 2008, 3:e1994.
    • (2008) PLoS One , vol.3
    • Zybailov, B.1
  • 80
    • 28444461062 scopus 로고    scopus 로고
    • Crystal structure of wild-type chaperonin GroEL
    • Bartolucci C., et al. Crystal structure of wild-type chaperonin GroEL. J. Mol. Biol. 2005, 354:940-951.
    • (2005) J. Mol. Biol. , vol.354 , pp. 940-951
    • Bartolucci, C.1
  • 81
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., et al. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1


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