메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

The Cpn10(1) co-chaperonin of a. thaliana functions only as a hetero-oligomer with Cpn20

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CHAPERONIN; CHAPERONIN 20; EARLY PREGNANCY FACTOR; UNCLASSIFIED DRUG; CPN10(1) PROTEIN, ARABIDOPSIS; CPN20 PROTEIN, ARABIDOPSIS; PROTEIN SUBUNIT;

EID: 84912571357     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113835     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature. 1996;381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 2
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z, Horwich AL, Sigler PB. 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    Horwich, A.L.2    Sigler, P.B.3
  • 4
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin GroEL at 2.8 A
    • Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, et al. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature. 1994;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
  • 6
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
    • Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB. The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat Struct Biol. 1996;3:170-177.
    • (1996) Nat Struct Biol , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 7
    • 0037418665 scopus 로고    scopus 로고
    • Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution
    • Wang J, Boisvert DC. Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution. J Mol Biol. 2003;327:843-855.
    • (2003) J Mol Biol , vol.327 , pp. 843-855
    • Wang, J.1    Boisvert, D.C.2
  • 11
    • 80051900180 scopus 로고    scopus 로고
    • Chloroplast beta chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro
    • Vitlin A, Weiss C, Demishtein-Zohary K, Rasouly A, Levin D, 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    Weiss, C.2    Demishtein-Zohary, K.3    Rasouly, A.4    Levin, D.5
  • 13
    • 0033103962 scopus 로고    scopus 로고
    • Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana
    • Koumoto Y, Shimada T, Kondo M, Takao T, Shimonishi 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    Shimada, T.2    Kondo, M.3    Takao, T.4    Shimonishi, Y.5
  • 14
    • 0032898910 scopus 로고    scopus 로고
    • cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana
    • Hirohashi T, Nishio K, Nakai M. cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana. Biochim Biophys Acta. 1999;1429:512-515.
    • (1999) Biochim Biophys Acta , vol.1429 , pp. 512-515
    • Hirohashi, T.1    Nishio, K.2    Nakai, M.3
  • 15
    • 0029066222 scopus 로고
    • Functional characterization of the higher plant chloroplast chaperonins
    • Viitanen PV, Schmidt M, Buchner J, Suzuki T, Vierling E, 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    Schmidt, M.2    Buchner, J.3    Suzuki, T.4    Vierling, E.5
  • 16
    • 84862025119 scopus 로고    scopus 로고
    • Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes
    • Tsai YC, Mueller-Cajar O, Saschenbrecker S, Hartl FU, Hayer-Hartl M. 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    Mueller-Cajar, O.2    Saschenbrecker, S.3    Hartl, F.U.4    Hayer-Hartl, M.5
  • 18
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals, N-terminal modifications and abundance of the chloroplast proteome
    • Zybailov B, Rutschow H, Friso G, Rudella A, Emanuelsson O, et al. Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS One. 2008;3:e1994.
    • (2008) PLoS One , vol.3 , pp. e1994
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3    Rudella, A.4    Emanuelsson, O.5
  • 19
    • 0035839528 scopus 로고    scopus 로고
    • Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana
    • Koumoto Y, Shimada T, Kondo M, Hara-Nishimura I, Nishimura M. 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    Shimada, T.2    Kondo, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 20
    • 33947516022 scopus 로고    scopus 로고
    • Significance of the N-terminal domain for the function of chloroplast cpn20 chaperonin
    • Bonshtien AL, Weiss C, Vitlin A, Niv A, Lorimer GH, 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    Weiss, C.2    Vitlin, A.3    Niv, A.4    Lorimer, G.H.5
  • 21
    • 0031939210 scopus 로고    scopus 로고
    • Purification of recombinant plant and animal GroES homologs: Chloroplast and mitochondrial chaperonin 10
    • Viitanen PV, Bacot K, Dickson R, Webb T. Purification of recombinant plant and animal GroES homologs: chloroplast and mitochondrial chaperonin 10. Methods Enzymol. 1998;290:218-230.
    • (1998) Methods Enzymol , vol.290 , pp. 218-230
    • Viitanen, P.V.1    Bacot, K.2    Dickson, R.3    Webb, T.4
  • 22
    • 0346101774 scopus 로고    scopus 로고
    • The voltage-dependent calcium channel beta subunit contains two stable interacting domains
    • Opatowsky Y, Chomsky-Hecht O, Kang MG, Campbell KP, Hirsch JA. The voltage-dependent calcium channel beta subunit contains two stable interacting domains. J Biol Chem. 2003;278:52323-52332.
    • (2003) J Biol Chem , vol.278 , pp. 52323-52332
    • Opatowsky, Y.1    Chomsky-Hecht, O.2    Kang, M.G.3    Campbell, K.P.4    Hirsch, J.A.5
  • 23
    • 0034697297 scopus 로고    scopus 로고
    • Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding
    • Dickson R, Weiss C, Howard RJ, Alldrick SP, Ellis RJ, 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    Weiss, C.2    Howard, R.J.3    Alldrick, S.P.4    Ellis, R.J.5
  • 24
    • 84884502211 scopus 로고    scopus 로고
    • Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis
    • Zhang XF, Jiang T, Wu Z, Du SY, Yu YT, et al. Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis. Plant Mol Biol. 2013;83:205-218.
    • (2013) Plant Mol Biol , vol.83 , pp. 205-218
    • Zhang, X.F.1    Jiang, T.2    Wu, Z.3    Du, S.Y.4    Yu, Y.T.5
  • 25
    • 0031919657 scopus 로고    scopus 로고
    • Structural analysis of GroE chaperonin complexes using chemical cross-linking
    • Azem A, Weiss C, Goloubinoff P. Structural analysis of GroE chaperonin complexes using chemical cross-linking. Methods Enzymol. 1998;290:253-268.
    • (1998) Methods Enzymol , vol.290 , pp. 253-268
    • Azem, A.1    Weiss, C.2    Goloubinoff, P.3
  • 26
    • 11144314848 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals its secrets: Chaperone genes and the potential roles of their gene products in the chloroplast
    • Schroda M. The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast. Photosynth Res. 2004;82:221-240.
    • (2004) Photosynth Res , vol.82 , pp. 221-240
    • Schroda, M.1
  • 27
    • 0034809742 scopus 로고    scopus 로고
    • Arabidopsis thaliana type I and II chaperonins
    • Hill JE, Hemmingsen SM. 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
  • 28
    • 49649089314 scopus 로고    scopus 로고
    • Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL
    • Nojima T, Murayama S, Yoshida M, Motojima F. Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL. J Biol Chem. 2008;283:18385-18392.
    • (2008) J Biol Chem , vol.283 , pp. 18385-18392
    • Nojima, T.1    Murayama, S.2    Yoshida, M.3    Motojima, F.4
  • 30
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential for folding of a specific substrate
    • Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, 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 , pp. e1001040
    • Peng, L.1    Fukao, Y.2    Myouga, F.3    Motohashi, R.4    Shinozaki, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.