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Volumn 50, Issue 2, 2007, Pages 265-277

The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas

Author keywords

Chloroplast chaperone function; GrpE; microtubule like structures; J domain protein; Protein complex assembly and disassembly; Thylakoid biogenesis

Indexed keywords

CHLOROPLAST CHAPERONE FUNCTION; GRPE MICROTUBULE-LIKE STRUCTURES; J-DOMAIN PROTEIN; PROTEIN COMPLEX ASSEMBLY AND DISASSEMBLY; THYLAKOID BIOGENESIS;

EID: 34247185926     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2007.03047.x     Document Type: Article
Times cited : (105)

References (49)
  • 1
    • 0024978377 scopus 로고
    • Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication
    • Alfano, C. and McMacken, R. (1989) Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication. J. Biol. Chem. 264, 10709-10718.
    • (1989) J. Biol. Chem , vol.264 , pp. 10709-10718
    • Alfano, C.1    McMacken, R.2
  • 3
    • 0014083717 scopus 로고
    • Particle arrangements in proplastids of Triticum vulgare L. seedlings
    • Bartels, P.G. and Weier, T.E. (1967) Particle arrangements in proplastids of Triticum vulgare L. seedlings. J. Cell Biol. 33, 243-253.
    • (1967) J. Cell Biol , vol.33 , pp. 243-253
    • Bartels, P.G.1    Weier, T.E.2
  • 4
    • 33646160201 scopus 로고    scopus 로고
    • Non-vesicular and vesicular trafficking involving plastids
    • Benning, C., Xu, C. and Awai, K. (2006) Non-vesicular and vesicular trafficking involving plastids. Curr. Opin. Plant Biol. 9, 241-247.
    • (2006) Curr. Opin. Plant Biol , vol.9 , pp. 241-247
    • Benning, C.1    Xu, C.2    Awai, K.3
  • 5
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
    • Buchberger, A., Schröder, H., Büttner, M., Valencia, A. and Bukau, B. (1994) A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat. Struct. Biol. 1, 95-101.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Büttner, M.3    Valencia, A.4    Bukau, B.5
  • 6
    • 0001414675 scopus 로고
    • Electron microscopic studies of envelope membranes from spinach plastids
    • Carde, J.-P., Joyard, J. and Douce, R. (1982) Electron microscopic studies of envelope membranes from spinach plastids. Biol. Cell, 44, 315-324.
    • (1982) Biol. Cell , vol.44 , pp. 315-324
    • Carde, J.-P.1    Joyard, J.2    Douce, R.3
  • 7
    • 0042337379 scopus 로고    scopus 로고
    • Chaperonemediated in vitro assembly of Polyomavirus capsids
    • Chromy, L.R., Pipas, J.M. and Garcea, R.L. (2003) Chaperonemediated in vitro assembly of Polyomavirus capsids. Proc. Natl Acad. Sci. USA, 100, 10477-10482.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10477-10482
    • Chromy, L.R.1    Pipas, J.M.2    Garcea, R.L.3
  • 8
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D.M., Langer, T. and Douglas, M.G. (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19, 176-181.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 9
    • 0030239139 scopus 로고    scopus 로고
    • Light inducible gene HSP70B encodes a chloroplast-localized heat shock protein in Chlamydomonas reinhardtii
    • Drzymalla, C., Schroda, M. and Beck, C.F. (1996) Light inducible gene HSP70B encodes a chloroplast-localized heat shock protein in Chlamydomonas reinhardtii. Plant Mol. Biol. 31, 1185-1194.
    • (1996) Plant Mol. Biol , vol.31 , pp. 1185-1194
    • Drzymalla, C.1    Schroda, M.2    Beck, C.F.3
  • 10
    • 33745438296 scopus 로고    scopus 로고
    • One of two Alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas
    • Gohre, V., Ossenbuhl, F., Crevecoeur, M., Eichacker, L.A. and Rochaix, J.D. (2006) One of two Alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas. Plant Cell, 18, 1454-1466.
    • (2006) Plant Cell , vol.18 , pp. 1454-1466
    • Gohre, V.1    Ossenbuhl, F.2    Crevecoeur, M.3    Eichacker, L.A.4    Rochaix, J.D.5
  • 11
    • 0037928428 scopus 로고    scopus 로고
    • Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system
    • Han, W. and Christen, P. (2003) Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system. J. Biol. Chem. 278, 19038-19043.
    • (2003) J. Biol. Chem , vol.278 , pp. 19038-19043
    • Han, W.1    Christen, P.2
  • 14
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F.-U. and Kuriyan, J. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science, 276, 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.-U.4    Kuriyan, J.5
  • 15
    • 0039572781 scopus 로고
    • The composition and ultrastructure of the nucellus in cotton
    • Jensen, W.A. (1965) The composition and ultrastructure of the nucellus in cotton. J. Ultrastruct. Res. 13, 112-128.
    • (1965) J. Ultrastruct. Res , vol.13 , pp. 112-128
    • Jensen, W.A.1
  • 17
    • 0028356858 scopus 로고
    • A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya, S., Gambill, B.D. and Craig, E.A. (1994) A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation. Proc. Natl Acad. Sci. USA, 91, 6481-6485.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 19
    • 0002865022 scopus 로고
    • Observations of microtubule-like structures within spinach plastids
    • Lawrence, M.E. and Possingham, J.V. (1984) Observations of microtubule-like structures within spinach plastids. Biol. Cell, 52, 77-82.
    • (1984) Biol. Cell , vol.52 , pp. 77-82
    • Lawrence, M.E.1    Possingham, J.V.2
  • 20
    • 0028467779 scopus 로고
    • Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes
    • Li, H.M., Kaneko, Y. and Keegstra, K. (1994) Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol. Biol. 25, 619-632.
    • (1994) Plant Mol. Biol , vol.25 , pp. 619-632
    • Li, H.M.1    Kaneko, Y.2    Keegstra, K.3
  • 21
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. and Zylicz, M. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci. USA, 88, 2874-2878.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 22
    • 14844293494 scopus 로고    scopus 로고
    • J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle inducing protein in plastids 1 (VIPP1)
    • Liu, C., Willmund, F., Whitelegge, J.P., Hawat, S., Knapp, B., Lodha, M. and Schroda, M. (2005) J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle inducing protein in plastids 1 (VIPP1). Mol. Biol. Cell, 16, 1165-1177.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1165-1177
    • Liu, C.1    Willmund, F.2    Whitelegge, J.P.3    Hawat, S.4    Knapp, B.5    Lodha, M.6    Schroda, M.7
  • 23
    • 0016468831 scopus 로고
    • Unusual structures associated with peripheral reticulum in chloroplasts of Myriophyllum spicatum L
    • Lunney, C.A., Davis, G.J. and Jones, M.N. (1975) Unusual structures associated with peripheral reticulum in chloroplasts of Myriophyllum spicatum L. J. Ultrastruct. Res. 50, 293-296.
    • (1975) J. Ultrastruct. Res , vol.50 , pp. 293-296
    • Lunney, C.A.1    Davis, G.J.2    Jones, M.N.3
  • 24
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M.P. and Bukau, B. (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 25
    • 0014078612 scopus 로고
    • Fine structure of protein-storing plastids in bean root tips
    • Newcomb, E.H. (1967) Fine structure of protein-storing plastids in bean root tips. J. Cell Biol. 33, 143-163.
    • (1967) J. Cell Biol , vol.33 , pp. 143-163
    • Newcomb, E.H.1
  • 26
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros, D.R., Welch, W.J. and Fink, A.L. (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl Acad. Sci. USA, 88, 5719-5723.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 27
    • 0007015590 scopus 로고
    • Microtubule-like structures in the growing plastids of two algae
    • Pickett-Heaps, J.D. (1968) Microtubule-like structures in the growing plastids of two algae. Planta, 81, 193-200.
    • (1968) Planta , vol.81 , pp. 193-200
    • Pickett-Heaps, J.D.1
  • 28
    • 0016616415 scopus 로고
    • Eine störungsfreie Mikromethode zur Bestimmung des Proteingehalts in Gewebshomogenaten
    • Popov, N., Schmitt, S. and Matthies, H. (1975) Eine störungsfreie Mikromethode zur Bestimmung des Proteingehalts in Gewebshomogenaten. Acta Biol. Germ. 34, 1441-1446.
    • (1975) Acta Biol. Germ , vol.34 , pp. 1441-1446
    • Popov, N.1    Schmitt, S.2    Matthies, H.3
  • 29
    • 84982534281 scopus 로고
    • Tubular structures in the plastids of Echinomastus intertextus Brit & Rose (Cactaceae)
    • Rivera, E.R. and Arnott, H.J. (1982) Tubular structures in the plastids of Echinomastus intertextus Brit & Rose (Cactaceae). New Phytol. 90, 551-561.
    • (1982) New Phytol , vol.90 , pp. 551-561
    • Rivera, E.R.1    Arnott, H.J.2
  • 30
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening of cellulose-bound peptide libraries
    • Rüdiger, S., Germeroth, L., Schneider-Mergener, J. and Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening of cellulose-bound peptide libraries. EMBO J. 16, 1501-1507.
    • (1997) EMBO J , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 31
    • 0036263966 scopus 로고    scopus 로고
    • The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
    • Schiene-Fischer, C., Habazettl, J., Schmid, F.X. and Fischer, G. (2002) The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nat. Struct. Biol. 9, 419-424.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 419-424
    • Schiene-Fischer, C.1    Habazettl, J.2    Schmid, F.X.3    Fischer, G.4
  • 32
    • 34247274957 scopus 로고
    • Plastidenstrukturen bei Passiflora
    • Schnepf, E. (1961) Plastidenstrukturen bei Passiflora. Protoplasma, 54, 310-313.
    • (1961) Protoplasma , vol.54 , pp. 310-313
    • Schnepf, E.1
  • 33
    • 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. (2004) The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast. Photosynth. Res. 82, 221-240.
    • (2004) Photosynth. Res , vol.82 , pp. 221-240
    • Schroda, M.1
  • 34
    • 0033149821 scopus 로고    scopus 로고
    • A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition
    • Schroda, M., Vallon, O., Wollman, F.-A. and Beck, C.F. (1999) A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition. Plant Cell, 11, 1165-1178.
    • (1999) Plant Cell , vol.11 , pp. 1165-1178
    • Schroda, M.1    Vallon, O.2    Wollman, F.-A.3    Beck, C.F.4
  • 35
    • 0035542788 scopus 로고    scopus 로고
    • The chloroplastic GrpE homolog of Chlamydomonas: Two isoforms generated by differential splicing
    • Schroda, M., Vallon, O., Whitelegge, J.P., Beck, C.F. and Wollman, F.-A. (2001) The chloroplastic GrpE homolog of Chlamydomonas: two isoforms generated by differential splicing. Plant Cell, 13, 2823-2839.
    • (2001) Plant Cell , vol.13 , pp. 2823-2839
    • Schroda, M.1    Vallon, O.2    Whitelegge, J.P.3    Beck, C.F.4    Wollman, F.-A.5
  • 36
    • 0008796812 scopus 로고
    • Fine structure changes during function of the digestive gland of Venus's-flytrap
    • Schwab, D.W., Simmons, E. and Scala, J. (1969) Fine structure changes during function of the digestive gland of Venus's-flytrap. Am. J. Bot. 56, 88-100.
    • (1969) Am. J. Bot , vol.56 , pp. 88-100
    • Schwab, D.W.1    Simmons, E.2    Scala, J.3
  • 37
    • 0000571028 scopus 로고
    • Zur Feinstruktur des Plastidenstromas von Hordeum vulgare L
    • Sprey, B. (1968) Zur Feinstruktur des Plastidenstromas von Hordeum vulgare L. Protoplasma, 66, 469-479.
    • (1968) Protoplasma , vol.66 , pp. 469-479
    • Sprey, B.1
  • 39
    • 23644458111 scopus 로고    scopus 로고
    • Chloroplast membrane transport: Interplay of prokaryotic and eukaryotic traits
    • Vothknecht, U.C. and Soll, J. (2005) Chloroplast membrane transport: interplay of prokaryotic and eukaryotic traits. Gene, 354, 99-109.
    • (2005) Gene , vol.354 , pp. 99-109
    • Vothknecht, U.C.1    Soll, J.2
  • 41
    • 0035957413 scopus 로고    scopus 로고
    • Vipp1 deletion mutant of Synechocystis: A connection between bacterial phage shock and thylakoid biogenesis?
    • Westphal, S., Heins, L., Soll, J. and Vothknecht, U.C. (2001) Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis? Proc. Natl Acad. Sci. USA, 98, 4243-4248.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4243-4248
    • Westphal, S.1    Heins, L.2    Soll, J.3    Vothknecht, U.C.4
  • 42
    • 0035957290 scopus 로고    scopus 로고
    • Discovery of a protein required for photosynthetic membrane assembly
    • von Wettstein, D. (2001) Discovery of a protein required for photosynthetic membrane assembly. Proc. Natl Acad. Sci. USA, 98, 3633-3635.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3633-3635
    • von Wettstein, D.1
  • 43
    • 84982073159 scopus 로고
    • The establishment of the plastid thylakoid system
    • Whatley, J.M., Hawes, C.R., Horne, J.C. and Kerr, J.D.A. (1982) The establishment of the plastid thylakoid system. New Phytol. 90, 619-629.
    • (1982) New Phytol , vol.90 , pp. 619-629
    • Whatley, J.M.1    Hawes, C.R.2    Horne, J.C.3    Kerr, J.D.A.4
  • 44
    • 0025788990 scopus 로고
    • Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin
    • Wickner, S., Hoskins, J. and McKenney, K. (1991) Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. Proc. Natl Acad. Sci. USA, 88, 7903-7907.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7903-7907
    • Wickner, S.1    Hoskins, J.2    McKenney, K.3
  • 45
    • 33644666048 scopus 로고    scopus 로고
    • HSP90C is a bona-fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii
    • Willmund, F. and Schroda, M. (2005) HSP90C is a bona-fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. Plant Physiol. 138, 2310-2322.
    • (2005) Plant Physiol , vol.138 , pp. 2310-2322
    • Willmund, F.1    Schroda, M.2
  • 46
    • 34249703965 scopus 로고    scopus 로고
    • 2-terminal domain of the chloroplast GrpE homolog CGE1 is required for dimerization and cochaperone function in vivo
    • in press
    • 2-terminal domain of the chloroplast GrpE homolog CGE1 is required for dimerization and cochaperone function in vivo. J. Biol. Chem., in press
    • (2007) J. Biol. Chem
    • Willmund, F.1    Mühlhaus, T.2    Wojciechowska, M.3    Schroda, M.4
  • 47
    • 1842583782 scopus 로고    scopus 로고
    • Zimmerman, S., Tran, P.T., Daga, R.R., Niwa, O. and Chang, F. (2004) Rsp1p, a J domain protein required for disassembly and assembly of microtubule organizing centers during the fission yeast cell cycle. Mol. Cell, 6, 497-509.
    • Zimmerman, S., Tran, P.T., Daga, R.R., Niwa, O. and Chang, F. (2004) Rsp1p, a J domain protein required for disassembly and assembly of microtubule organizing centers during the fission yeast cell cycle. Mol. Cell, 6, 497-509.
  • 48
    • 0023622594 scopus 로고
    • The grpE protein of Escherichia coli. Purification and properties
    • Zylicz, M., Ang, D. and Georgopoulos, C. (1987) The grpE protein of Escherichia coli. Purification and properties. J. Biol. Chem. 262, 17437-17442.
    • (1987) J. Biol. Chem , vol.262 , pp. 17437-17442
    • Zylicz, M.1    Ang, D.2    Georgopoulos, C.3
  • 49
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- and bacteriophageencoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M., Ang, D., Liberek, K. and Georgopoulos, C. (1989) Initiation of λ DNA replication with purified host- and bacteriophageencoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J. 8, 1601-1608.
    • (1989) EMBO J , vol.8 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4


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