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Volumn 35, Issue 5, 2013, Pages 402-409

OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL

Author keywords

chaperonin; Cpn60; plastid; rice; Rubisco

Indexed keywords

CHAPERONIN; CHAPERONIN 60 ALPHA; CHLOROPHYLL A BINDING PROTEIN 1; CHLOROPHYLL B BINDING PROTEIN 1; CHLOROPHYLL BINDING PROTEIN; HEAT SHOCK PROTEIN 70; HYBRID PROTEIN; OSCPN60 ALPHA 1; PEPTIDES AND PROTEINS; RIBULOSEBISPHOSPHATE CARBOXYLASE; UNCLASSIFIED DRUG; CHAPERONIN 60; CHLOROPHYLL; CHLOROPHYLL A; GREEN FLUORESCENT PROTEIN; RBCL PROTEIN, PLASTID;

EID: 84879089641     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.1007/s10059-013-2337-2     Document Type: Article
Times cited : (35)

References (58)
  • 1
    • 9144236348 scopus 로고    scopus 로고
    • Generation and analysis of end sequence database for T-DNA tagging lines in rice
    • 14630961 10.1104/pp.103.030478 1:CAS:528:DC%2BD2cXhvFOg
    • An, S., Park, S., Jeong, D.H., Lee, D.Y., Kang, H.G., Yu, J.H., Hur, J., Kim, S.R., Kim, Y.H., Lee, M., et al. (2003). Generation and analysis of end sequence database for T-DNA tagging lines in rice. Plant Physiol. 133, 2040-2047.
    • (2003) Plant Physiol. , vol.133 , pp. 2040-2047
    • An, S.1    Park, S.2    Jeong, D.H.3    Lee, D.Y.4    Kang, H.G.5    Yu, J.H.6    Hur, J.7    Kim, S.R.8    Kim, Y.H.9    Lee, M.10
  • 2
    • 0034979913 scopus 로고    scopus 로고
    • The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60 gene
    • 10.1104/pp.126.2.717 1:CAS:528:DC%2BD3MXks1Gms78%3D
    • Apuya, N.R., Yadegari, R., Fischer, R.L., Harada, J.J., Zimmerman, J.L., and Goldberg, R.B. (2001). The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60 gene. α Plant Physiol. 126, 717-730.
    • (2001) α Plant Physiol. , vol.126 , pp. 717-730
    • Apuya, N.R.1    Yadegari, R.2    Fischer, R.L.3    Harada, J.J.4    Zimmerman, J.L.5    Goldberg, R.B.6
  • 3
    • 0033800261 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic chaperonins: Phylogenetic evidence for ancient duplications in CCT genes
    • 11018153 10.1093/oxfordjournals.molbev.a026246 1:CAS:528: DC%2BD3cXnt1Cnsb8%3D
    • Archibald, J.M., Logsdon, J.M., Jr., and Doolittle, W.F. (2000). Origin and evolution of eukaryotic chaperonins: phylogenetic evidence for ancient duplications in CCT genes. Mol. Biol. Evol. 17, 1456-1466.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1456-1466
    • Archibald, J.M.1    Logsdon, Jr.J.M.2    Doolittle, W.F.3
  • 4
    • 0029346958 scopus 로고
    • Identification of NADPH: Protochlorophyllide oxidoreductases A and B: A branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana
    • 7659751 10.1104/pp.108.4.1505 1:CAS:528:DyaK2MXnsVagsb8%3D
    • Armstrong, G.A., Runge, S., Frick, G., Sperling, U., and Apel, K. (1995). Identification of NADPH: protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol. 108, 1505-1517.
    • (1995) Plant Physiol. , vol.108 , pp. 1505-1517
    • Armstrong, G.A.1    Runge, S.2    Frick, G.3    Sperling, U.4    Apel, K.5
  • 5
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated pea chloroplasts
    • 7388030 10.1016/0005-2787(80)90129-X 1:CAS:528:DyaL3cXks1Kntb8%3D
    • Barraclough, R., and Ellis, R.J. (1980). Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated pea chloroplasts. Biochim. Biophys. Acta 608, 19-31.
    • (1980) Biochim. Biophys. Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 6
    • 0030194514 scopus 로고    scopus 로고
    • Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus
    • 8754688 10.1104/pp.111.3.931 1:CAS:528:DyaK28XktlKksbw%3D
    • Bonk, M., Tadros, M., Vandekerckhove, J., Al-Babili, S., and Beyer, P. (1996). Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus. Plant Physiol. 111, 931-939.
    • (1996) Plant Physiol. , vol.111 , pp. 931-939
    • Bonk, M.1    Tadros, M.2    Vandekerckhove, J.3    Al-Babili, S.4    Beyer, P.5
  • 7
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin GroEL at 2.8 Á
    • 7935790 10.1038/371578a0 1:CAS:528:DyaK2cXmslCrsbk%3D
    • Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D.C., Joachimiak, A., Horwich, A.L., and Sigler, P.B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Á. Nature 371, 578-586.
    • (1994) Nature , vol.371 , pp. 578-586
    • Braig, K.1    Otwinowski, Z.2    Hegde, R.3    Boisvert, D.C.4    Joachimiak, A.5    Horwich, A.L.6    Sigler, P.B.7
  • 8
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • 9476895 10.1016/S0092-8674(00)80928-9 1:CAS:528:DyaK1cXhtFGisLk%3D
    • Bukau, B., and Horwich, A.L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 9
    • 0022796983 scopus 로고
    • Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein
    • 3771637 10.1083/jcb.103.4.1327 1:CAS:528:DyaL2sXhslWqtr8%3D
    • Cannon, S., Wang, P., and Roy, H. (1986). Inhibition of ribulose bisphosphate carboxylase assembly by antibody to a binding protein. J. Cell Biol. 103, 1327-1335.
    • (1986) J. Cell Biol. , vol.103 , pp. 1327-1335
    • Cannon, S.1    Wang, P.2    Roy, H.3
  • 10
    • 0028431010 scopus 로고
    • Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides
    • 7913238 10.1104/pp.105.1.233 1:CAS:528:DyaK2cXktlWisb4%3D
    • Cloney, L.P., Bekkaoui, D.R., Feist, G.L., Lane, W.S., and Hemmingsen, S.M. (1994). Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides. Plant Physiol. 105, 233-241.
    • (1994) Plant Physiol. , vol.105 , pp. 233-241
    • Cloney, L.P.1    Bekkaoui, D.R.2    Feist, G.L.3    Lane, W.S.4    Hemmingsen, S.M.5
  • 11
    • 0034697297 scopus 로고    scopus 로고
    • Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding
    • 10766808 10.1074/jbc.275.16.11829 1:CAS:528:DC%2BD3cXisl2jsLw%3D
    • Dickson, R., Weiss, C., Howard, R.J., Alldrick, S.P., Ellis, R.J., Lorimer, G., Azem, A., and Viitanen, P.V. (2000). Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding. J. Biol. Chem. 275, 11829-11835.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11829-11835
    • Dickson, R.1    Weiss, C.2    Howard, R.J.3    Alldrick, S.P.4    Ellis, R.J.5    Lorimer, G.6    Azem, A.7    Viitanen, P.V.8
  • 12
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • 9546398 10.1016/S0092-8674(00)81152-6 1:CAS:528:DyaK1cXisFGitL4%3D
    • Ditzel, L., Löwe, J., Stock, D., Stetter, K.O., Huber, H., Huber, R., and Steinbacher, S. (1998). Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 13
    • 0024314918 scopus 로고
    • Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
    • 2572080 10.1016/0968-0004(89)90168-0 1:CAS:528:DyaL1MXlvV2ltrk%3D
    • Ellis, R.J., and Hemmingsen, S.M. (1989) Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14, 339-342.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 14
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • 2563997 1:CAS:528:DyaL1MXhs1OjtL8%3D
    • Fayet, O., Ziegelhoffer, T., and Georgopoulos, C. (1989). The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 15
    • 0025251691 scopus 로고
    • Chaperone function: The assembly of ribulose bisphosphate carboxylase-oxygenase
    • 1980417 10.1146/annurev.cb.06.110190.001013 1:CAS:528:DyaK3MXit1emur4%3D
    • Gatenby, A.A., and Ellis, R.J. (1990). Chaperone function: the assembly of ribulose bisphosphate carboxylase-oxygenase. Annu. Rev. Cell Biol. 6, 125-149.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 125-149
    • Gatenby, A.A.1    Ellis, R.J.2
  • 16
    • 0031561403 scopus 로고    scopus 로고
    • Chaperonin genes of the Synechocystis PCC 6803 are differentially regulated under light-dark transition during heat stress
    • 9345313 10.1006/bbrc.1997.7463 1:CAS:528:DyaK2sXmvVKmt7g%3D
    • Glatz, A., Horváth, I., Varvasovszki, V., Kovács, E., Török, Z., and Vigh, L. (1997). Chaperonin genes of the Synechocystis PCC 6803 are differentially regulated under light-dark transition during heat stress. Biochem. Biophys. Res. Commun. 239, 291-297.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 291-297
    • Glatz, A.1    Horváth, I.2    Varvasovszki, V.3    Kovács, E.4    Török, Z.5    Vigh, L.6
  • 17
    • 34548043303 scopus 로고    scopus 로고
    • Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent
    • 10.1379/CSC-227R.1 1:CAS:528:DC%2BD2sXoslGntb0%3D
    • Gould, P.S., Burgar, H.R., and Lund, P.A. (2007). Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent. Cell Stress Chaper 12, 123-131.
    • (2007) Cell Stress Chaper , vol.12 , pp. 123-131
    • Gould, P.S.1    Burgar, H.R.2    Lund, P.A.3
  • 18
    • 0028843014 scopus 로고
    • Rubisco synthesis, assembly, mechanism and regulation
    • 12242387 1:CAS:528:DyaK2MXnt1Sgsbg%3D
    • Gutteridge, S., and Gatenby, A.A. (1995). Rubisco synthesis, assembly, mechanism and regulation. Plant Cell 7, 809-819.
    • (1995) Plant Cell , vol.7 , pp. 809-819
    • Gutteridge, S.1    Gatenby, A.A.2
  • 19
    • 33845247111 scopus 로고    scopus 로고
    • Rice Immature Pollen 1 (RIP1) is a regulator of late pollen development
    • 16990291 10.1093/pcp/pcl013 1:CAS:528:DC%2BD28XhtlWqsr%2FO
    • Han, M.J., Jung, K.H., Yi, G., Lee, D.Y., and An, G. (2006). Rice Immature Pollen 1 (RIP1) is a regulator of late pollen development. Plant Cell Physiol. 47, 1457-1472.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1457-1472
    • Han, M.J.1    Jung, K.H.2    Yi, G.3    Lee, D.Y.4    An, G.5
  • 20
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 8637592 10.1038/381571a0 1:CAS:528:DyaK28XjsFyltb8%3D
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 21
    • 0001643571 scopus 로고
    • Purification and properties of ribulose bisphosphate carboxylase large subunit binding protein
    • 16664596 10.1104/pp.80.1.269 1:CAS:528:DyaL28XhtVGjsbs%3D
    • Hemmingsen, S.M., and Ellis, R.J. (1986). Purification and properties of ribulose bisphosphate carboxylase large subunit binding protein. Plant Physiol. 80, 269-276.
    • (1986) Plant Physiol. , vol.80 , pp. 269-276
    • Hemmingsen, S.M.1    Ellis, R.J.2
  • 23
    • 0034809742 scopus 로고    scopus 로고
    • Arabidopsis thaliana type i and II chaperonins
    • 10.1379/1466-1268(2001)006<0190:ATTIAI>2.0.CO;2 1:CAS:528:DC%2BD3MXnslKhtLk%3D
    • Hill, J.E., and Hemmingsen, S.M. (2001). Arabidopsis thaliana type I and II chaperonins. Cell Stress Chaper. 6, 190-200.
    • (2001) Cell Stress Chaper. , vol.6 , pp. 190-200
    • Hill, J.E.1    Hemmingsen, S.M.2
  • 24
    • 36949033246 scopus 로고    scopus 로고
    • Two families of chaperonin: Physiology and mechanism
    • 17489689 10.1146/annurev.cellbio.23.090506.123555 1:CAS:528: DC%2BD2sXhtlartrzE
    • Horwich, A.L., Fenton, W.A., Chapman, E., and Farr, G.W. (2007). Two families of chaperonin: physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23, 115-145.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 115-145
    • Horwich, A.L.1    Fenton, W.A.2    Chapman, E.3    Farr, G.W.4
  • 25
    • 0037364978 scopus 로고    scopus 로고
    • Deletion of a chaperonin 60β gene leads to cell death in the Arabidopsis lesion initiation 1 mutant
    • 12668771 10.1093/pcp/pcg031 1:CAS:528:DC%2BD3sXivVWitrg%3D
    • Ishikawa, A., Tanaka, H., Nakai, M., and Asahi, T. (2003). Deletion of a chaperonin 60β gene leads to cell death in the Arabidopsis lesion initiation 1 mutant. Plant Cell Physiol. 44, 255-261.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 255-261
    • Ishikawa, A.1    Tanaka, H.2    Nakai, M.3    Asahi, T.4
  • 26
    • 33646854724 scopus 로고    scopus 로고
    • Validation of housekeeping genes as internal control for studying gene expression in rice by quantitative real-time PCR
    • 10.1016/j.bbrc.2006.04.140
    • Jain, M., Nijhawan, A., Tyagi, A.K., and Khurana, J.P. (2006). Validation of housekeeping genes as internal control for studying gene expression in rice by quantitative real-time PCR. Biochem. Biophys. Res. Commun. 45, 646-651.
    • (2006) Biochem. Biophys. Res. Commun. , vol.45 , pp. 646-651
    • Jain, M.1    Nijhawan, A.2    Tyagi, A.K.3    Khurana, J.P.4
  • 27
    • 0033918191 scopus 로고    scopus 로고
    • T-DNA insertional mutagenesis for functional genomics in rice
    • 10886776 10.1046/j.1365-313x.2000.00767.x 1:CAS:528:DC%2BD3cXltFKksbo%3D
    • Jeon, J.S., Lee, S., Jung, K.H., Jun, S.H., Jeong, D.H., Lee, J., Kim, C., Jang, S., Yang, K., Nam, J., et al. (2000). T-DNA insertional mutagenesis for functional genomics in rice. Plant J. 22, 561-570.
    • (2000) Plant J. , vol.22 , pp. 561-570
    • Jeon, J.S.1    Lee, S.2    Jung, K.H.3    Jun, S.H.4    Jeong, D.H.5    Lee, J.6    Kim, C.7    Jang, S.8    Yang, K.9    Nam, J.10
  • 28
    • 33644868552 scopus 로고    scopus 로고
    • Generation of a flanking sequence-tag database for activation-tagging lines in japonica rice
    • 16367959 10.1111/j.1365-313X.2005.02610.x 1:CAS:528: DC%2BD28XjvFOntA%3D%3D
    • Jeong, D.H., An, S., Park, S., Kang, H.G., Park, G.G., Kim, S.R., Sim, J., Kim, Y.O., Kim, M.K., Kim, S.R., et al. (2006). Generation of a flanking sequence-tag database for activation-tagging lines in japonica rice. Plant J. 45, 123-132.
    • (2006) Plant J. , vol.45 , pp. 123-132
    • Jeong, D.H.1    An, S.2    Park, S.3    Kang, H.G.4    Park, G.G.5    Kim, S.R.6    Sim, J.7    Kim, Y.O.8    Kim, M.K.9    Kim, S.R.10
  • 29
    • 84872334825 scopus 로고    scopus 로고
    • Application of MapMan and RiceNet drives systematic analyses of the early heat stress transcriptome in rice seedlings
    • 10.1007/s12374-012-0270-0 1:CAS:528:DC%2BC3sXnt1Khuw%3D%3D
    • Jung, K.H., and An, G. (2012). Application of MapMan and RiceNet drives systematic analyses of the early heat stress transcriptome in rice seedlings. J. Plant Biol. 55, 436-449.
    • (2012) J. Plant Biol. , vol.55 , pp. 436-449
    • Jung, K.H.1    An, G.2
  • 30
    • 84872273003 scopus 로고    scopus 로고
    • Genome-wide identification and analysis of early heat stress responsive genes in rice
    • 10.1007/s12374-012-0271-z 1:CAS:528:DC%2BC3sXnt1Khsw%3D%3D
    • Jung, K.H., Gho, H.J., Kim, S.R., Ronald, P.C., and An, G. (2012). Genome-wide identification and analysis of early heat stress responsive genes in rice. J. Plant Biol. 55, 458-468.
    • (2012) J. Plant Biol. , vol.55 , pp. 458-468
    • Jung, K.H.1    Gho, H.J.2    Kim, S.R.3    Ronald, P.C.4    An, G.5
  • 33
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries in the chloroplast
    • 8755536 10.1073/pnas.93.15.7684 1:CAS:528:DyaK28XksFSrsb8%3D
    • Kessler, F., and Blobel, G. (1996). Interaction of the protein import and folding machineries in the chloroplast. Proc. Natl. Acad. Sci. USA 93, 7684-7689.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 34
    • 69249104408 scopus 로고    scopus 로고
    • Cloning vectors for rice
    • 10.1007/s12374-008-9008-4 1:CAS:528:DC%2BD1MXovFSgsrg%3D
    • Kim, S.R., Lee, D.Y., Yang, J.I., Moon, S., and An, G. (2009). Cloning vectors for rice. J. Plant Biol. 52, 73-78.
    • (2009) J. Plant Biol. , vol.52 , pp. 73-78
    • Kim, S.R.1    Lee, D.Y.2    Yang, J.I.3    Moon, S.4    An, G.5
  • 35
    • 79952200398 scopus 로고    scopus 로고
    • Development of an efficient inverse PCR method for isolating gene tags from T-DNA insertional mutants in rice
    • 20931378 10.1007/978-1-60761-682-5-11 1:CAS:528:DC%2BC3cXhsFKnsr7N
    • Kim, S.R., Jeon, J.S., and An, G. (2011). Development of an efficient inverse PCR method for isolating gene tags from T-DNA insertional mutants in rice. Methods Mol. Biol. 678, 139-146.
    • (2011) Methods Mol. Biol. , vol.678 , pp. 139-146
    • Kim, S.R.1    Jeon, J.S.2    An, G.3
  • 36
    • 0000767802 scopus 로고    scopus 로고
    • Binary vectors for efficient transformation of rice
    • 10.1007/BF03030346 1:CAS:528:DC%2BD3cXhtFShtb0%3D
    • Lee, S., Jeon, J.S., Jung, K.H., and An, G. (1999). Binary vectors for efficient transformation of rice. J. Plant Biol. 42, 310-316.
    • (1999) J. Plant Biol. , vol.42 , pp. 310-316
    • Lee, S.1    Jeon, J.S.2    Jung, K.H.3    An, G.4
  • 37
    • 84863470985 scopus 로고    scopus 로고
    • Activation of rice nicotianamine synthase 2 (OsNAS2) enhances iron availability for biofortification
    • 22228185 10.1007/s10059-012-2231-3 1:CAS:528:DC%2BC38Xkt1ert7s%3D
    • Lee, S., Kim, Y.S., Jeon, U.S., Kim, Y.K., Schjoerring, J.K., and An, G. (2012). Activation of rice nicotianamine synthase 2 (OsNAS2) enhances iron availability for biofortification. Mol. Cells 33, 269-275.
    • (2012) Mol. Cells , vol.33 , pp. 269-275
    • Lee, S.1    Kim, Y.S.2    Jeon, U.S.3    Kim, Y.K.4    Schjoerring, J.K.5    An, G.6
  • 38
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • 12493248 10.1016/S0168-9525(02)00003-3 1:CAS:528:DC%2BD38XpsFaqtLk%3D
    • Leister, D. (2003). Chloroplast research in the genomic age. Trends Genet. 19, 47-56.
    • (2003) Trends Genet. , vol.19 , pp. 47-56
    • Leister, D.1
  • 39
    • 77952506871 scopus 로고    scopus 로고
    • Protein transport into chloroplasts
    • 20192748 10.1146/annurev-arplant-042809-112222 1:CAS:528: DC%2BC3cXnslSjs7Y%3D
    • Li, H.M., and Chiu, C.C. (2010). Protein transport into chloroplasts. Annu. Rev. Plant Biol. 61, 157-180.
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 157-180
    • Li, H.M.1    Chiu, C.C.2
  • 40
    • 4544322591 scopus 로고    scopus 로고
    • Chlorophylls and carotenoids: Measurement and characterization by UV-VIS spectroscopy
    • R. Wrolstad (eds)
    • Lichtenthaler, H., and Buschmann, C. (2001). Chlorophylls and carotenoids: measurement and characterization by UV-VIS spectroscopy. In Current Protocols in Food Analytical Chemistry, R. Wrolstad, ed. (John Wiley & Sons, Inc.), F4.3.1-F4.3.8.
    • (2001) Current Protocols in Food Analytical Chemistry
    • Lichtenthaler, H.1    Buschmann, C.2
  • 42
    • 0025200907 scopus 로고
    • Unique composition of plastid chaperonin-60: Alpha and beta polypeptide-encoding genes are highly divergent
    • 1979547 10.1016/0378-1119(90)90385-5 1:CAS:528:DyaK3MXls1Kltg%3D%3D
    • Martel, R., Cloney, L.P., Pelcher, L.E., and Hemmingsen, S.M. (1990). Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent. Gene 94, 181-187.
    • (1990) Gene , vol.94 , pp. 181-187
    • Martel, R.1    Cloney, L.P.2    Pelcher, L.E.3    Hemmingsen, S.M.4
  • 43
    • 0021305210 scopus 로고
    • ATP-released large subunits participate in the assembly of RuBP carboxylase
    • 6725425 10.1002/jcb.240240206 1:CAS:528:DyaL2cXktlGiurw%3D
    • Milos, P., and Roy, H. (1984). ATP-released large subunits participate in the assembly of RuBP carboxylase. J. Cell Biochem. 24, 153-162.
    • (1984) J. Cell Biochem. , vol.24 , pp. 153-162
    • Milos, P.1    Roy, H.2
  • 44
    • 0023657522 scopus 로고
    • Dissociation of the ribulose bisphosphate-carboxylase large-subunit binding protein into dissimilar subunits
    • 10.1111/j.1432-1033.1987.tb10900.x 1:CAS:528:DyaL2sXitV2ks78%3D
    • Musgrove, J.E., Johnson, R.A., and Ellis, R.J. (1987). Dissociation of the ribulose bisphosphate-carboxylase large-subunit binding protein into dissimilar subunits. Euro. J. Biochem. 163, 529-534.
    • (1987) Euro. J. Biochem. , vol.163 , pp. 529-534
    • Musgrove, J.E.1    Johnson, R.A.2    Ellis, R.J.3
  • 45
    • 0033590077 scopus 로고    scopus 로고
    • Chloroplast chaperonins: Evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer
    • 10600546 10.1006/bbrc.1999.1868 1:CAS:528:DyaK1MXnvFertrY%3D
    • Nishio, K., Hirohashi, T., and Nakai, M. (1999). Chloroplast chaperonins: evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer. Biochem. Biophys. Res. Commun. 266, 584-587.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 584-587
    • Nishio, K.1    Hirohashi, T.2    Nakai, M.3
  • 46
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential for folding of a specific substrate
    • 21483722 10.1371/journal.pbio.1001040 1:CAS:528:DC%2BC3MXkvV2gtb4%3D
    • Peng, L., Fukao, Y., Myouga, F., Motohashi, R., Shinozaki, K., and Shikanai, T. (2011). A chaperonin subunit with unique structures is essential for folding of a specific substrate. PLoS Biol. 9, e1001040. doi:10.1371/journal.pbio.1001040.
    • (2011) PLoS Biol. , vol.9 , pp. 1001040
    • Peng, L.1    Fukao, Y.2    Myouga, F.3    Motohashi, R.4    Shinozaki, K.5    Shikanai, T.6
  • 48
    • 0024755607 scopus 로고
    • Rubisco assembly: A model system for studying the mechanism of chaperonin action
    • 2577726 1:CAS:528:DyaK3cXltVKmsQ%3D%3D
    • Roy, H. (1989). Rubisco assembly: a model system for studying the mechanism of chaperonin action. Plant Cell 1, 1035-1042.
    • (1989) Plant Cell , vol.1 , pp. 1035-1042
    • Roy, H.1
  • 49
    • 0023893987 scopus 로고
    • Ribulose bisphosphate carboxylase assembly: What is the role of the large subunit binding protein?
    • 3255196 10.1016/0968-0004(88)90139-9 1:CAS:528:DyaL1cXks12iur8%3D
    • Roy, H., and Cannon, S. (1988). Ribulose bisphosphate carboxylase assembly: what is the role of the large subunit binding protein? Trends Biochem. Sci. 13, 163-165.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 163-165
    • Roy, H.1    Cannon, S.2
  • 50
    • 0034081637 scopus 로고    scopus 로고
    • Molecular chaperones: Containers and surfaces for folding, stabilising or unfolding proteins
    • 10753820 10.1016/S0959-440X(00)00074-9 1:CAS:528:DC%2BD3cXivFWgtbc%3D
    • Saibil, H. (2000). Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins. Curr. Opin. Struct. Biol. 10, 251-258.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 251-258
    • Saibil, H.1
  • 51
    • 0031684079 scopus 로고    scopus 로고
    • Structure and function in GroEL-mediated protein folding
    • 9759498 10.1146/annurev.biochem.67.1.581 1:CAS:528:DyaK1cXlsFOmsb0%3D
    • Sigler, P.B., Xu, Z., Rye, H.S., Burston, S.G., Fenton, W.A., and Horwich, A.L. (1998). Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581-608.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 581-608
    • Sigler, P.B.1    Xu, Z.2    Rye, H.S.3    Burston, S.G.4    Fenton, W.A.5    Horwich, A.L.6
  • 52
    • 65249090789 scopus 로고    scopus 로고
    • Plastid chaperonin proteins Cpn60α and Cpn60β are required for plastid division in Arabidopsis thaliana
    • 19344532 10.1186/1471-2229-9-38
    • Suzuki, K., Nakanishi, H., Bower, J., Yoder, D.W., Osteryoung, K.W., and Miyagishima, S.Y. (2009). Plastid chaperonin proteins Cpn60α and Cpn60β are required for plastid division in Arabidopsis thaliana. BMC Plant Biol. 9, 38. doi: 10.1186/1471-2229-9-38.
    • (2009) BMC Plant Biol. , vol.9 , pp. 38
    • Suzuki, K.1    Nakanishi, H.2    Bower, J.3    Yoder, D.W.4    Osteryoung, K.W.5    Miyagishima, S.Y.6
  • 53
    • 33749242963 scopus 로고    scopus 로고
    • Tic21 is an essential translocon component for protein translocation across the chloroplast inner envelope membrane
    • 16891400 10.1105/tpc.106.044305 1:CAS:528:DC%2BD28XhtVKgurnE
    • Teng, Y.S., Su, Y.S., Chen, L.J., Lee, Y.J., Hwang, I., and Li, H.M. (2006). Tic21 is an essential translocon component for protein translocation across the chloroplast inner envelope membrane. Plant Cell 18, 2247-2257.
    • (2006) Plant Cell , vol.18 , pp. 2247-2257
    • Teng, Y.S.1    Su, Y.S.2    Chen, L.J.3    Lee, Y.J.4    Hwang, I.5    Li, H.M.6
  • 55
    • 80051900180 scopus 로고    scopus 로고
    • Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro
    • 21633907 10.1007/s11103-011-9797-6 1:CAS:528:DC%2BC3MXhtVKjtrvL
    • Vitlin, A., Weiss, C., Demishtein-Zohary, K., Rasouly, A., Levin, D., Pisanty-Farchi, O., Breiman, A., and Azem, A. (2011). Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro. Plant Mol. Biol. 77, 105-115.
    • (2011) Plant Mol. Biol. , vol.77 , pp. 105-115
    • Vitlin, A.1    Weiss, C.2    Demishtein-Zohary, K.3    Rasouly, A.4    Levin, D.5    Pisanty-Farchi, O.6    Breiman, A.7    Azem, A.8
  • 56
    • 0032902669 scopus 로고    scopus 로고
    • Ancient gene duplication and differential gene flow in plastid lineages: The GroEL/Cpn60 example
    • 9873083 10.1007/PL00006438 1:CAS:528:DyaK1MXlvFyhtg%3D%3D
    • Wastl, J., Fraunholz, M., Zauner, S., Douglas, S., and Maier, U.G. (1999). Ancient gene duplication and differential gene flow in plastid lineages: the GroEL/Cpn60 example. J. Mol. Evol. 48, 112-117.
    • (1999) J. Mol. Evol. , vol.48 , pp. 112-117
    • Wastl, J.1    Fraunholz, M.2    Zauner, S.3    Douglas, S.4    Maier, U.G.5
  • 57
    • 58549113565 scopus 로고    scopus 로고
    • Cpn20: Siamese twins of the chaperonin world
    • 19031045 10.1007/s11103-008-9432-3 1:CAS:528:DC%2BD1MXotVyjtg%3D%3D
    • Weiss, C., Bonshtien, A., Farchi-Pisanty, O., Vitlin, A., and Azem, A. (2009). Cpn20: Siamese twins of the chaperonin world. Plant Mol. Biol. 69, 227-238.
    • (2009) Plant Mol. Biol. , vol.69 , pp. 227-238
    • Weiss, C.1    Bonshtien, A.2    Farchi-Pisanty, O.3    Vitlin, A.4    Azem, A.5
  • 58
    • 71249160931 scopus 로고    scopus 로고
    • Improvement of DNA/Metal particle adsorption in tungsten-based biolistic bombardment; Alkaline pH is necessary for DNA adsorption and suppression of DNA degradation
    • 10.1007/s12374-009-9068-0 1:CAS:528:DC%2BD1MXhsFSrur%2FE
    • Yoshimitsu, Y., Tanaka, K., Tagawa, T., Nakamura, Y., Matsuo, T., and Okamoto, S. (2009). Improvement of DNA/Metal particle adsorption in tungsten-based biolistic bombardment; Alkaline pH is necessary for DNA adsorption and suppression of DNA degradation. J. Plant Biol. 52, 524-532.
    • (2009) J. Plant Biol. , vol.52 , pp. 524-532
    • Yoshimitsu, Y.1    Tanaka, K.2    Tagawa, T.3    Nakamura, Y.4    Matsuo, T.5    Okamoto, S.6


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