메뉴 건너뛰기




Volumn 136, Issue 4, 2004, Pages 4114-4126

Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; DISEASES; GENES; GENETIC ENGINEERING;

EID: 16644386554     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.053835     Document Type: Article
Times cited : (123)

References (55)
  • 2
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of chloroplast proteolysis
    • Adam Z, Clarke AK (2002) Cutting edge of chloroplast proteolysis. Trends Plant Sci 7: 451-456
    • (2002) Trends Plant Sci , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 3
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • Akita M, Nielsen E, Keegstra K (1997) Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. J Cell Biol 136: 983-994
    • (1997) J Cell Biol , vol.136 , pp. 983-994
    • Akita, M.1    Nielsen, E.2    Keegstra, K.3
  • 5
    • 0000600042 scopus 로고
    • Protoplast transformation and methods to create specific mutants in Arabidopsis thaliana
    • C Koncz, N-H Chua, J Schell, eds. World Scientific, London
    • Altman T, Damm B, Halfter U, Willmitzer L, Morris P-C (1992) Protoplast transformation and methods to create specific mutants in Arabidopsis thaliana. In C Koncz, N-H Chua, J Schell, eds. Methods in Arabidopsis Research. World Scientific, London, pp 310-330
    • (1992) Methods in Arabidopsis Research , pp. 310-330
    • Altman, T.1    Damm, B.2    Halfter, U.3    Willmitzer, L.4    Morris, P.-C.5
  • 6
    • 0037048707 scopus 로고    scopus 로고
    • A simple method for isolating import-competent Arabidopsis chloroplasts
    • Aronsson H, Jarvis P (2002) A simple method for isolating import-competent Arabidopsis chloroplasts. FEBS Lett 529: 215-220
    • (2002) FEBS Lett , vol.529 , pp. 215-220
    • Aronsson, H.1    Jarvis, P.2
  • 7
    • 0029047317 scopus 로고
    • A chloroplast lipoxygenase is required for wound-induced jasmonic accumulation in Arabidopsis
    • Bell E, Creelman RA, Mullet JE (1995) A chloroplast lipoxygenase is required for wound-induced jasmonic accumulation in Arabidopsis. Proc Natl Acad Sci USA 92: 8675-8679
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8675-8679
    • Bell, E.1    Creelman, R.A.2    Mullet, J.E.3
  • 8
    • 0030198323 scopus 로고    scopus 로고
    • The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants
    • Clarke AK, Eriksson M-J (1996) The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants. Plant Mol Biol 31: 721-730
    • (1996) Plant Mol Biol , vol.31 , pp. 721-730
    • Clarke, A.K.1    Eriksson, M.-J.2
  • 9
    • 0343907311 scopus 로고    scopus 로고
    • Immunochemical studies on the Clp-protease in chloroplasts: Evidence for the formation of a ClpC/P complex
    • Desimone M, Weiss-Wichert C, Wagner E, Altenfeld U, Johanningmeier U (1997) Immunochemical studies on the Clp-protease in chloroplasts: evidence for the formation of a ClpC/P complex. Bot Acta 110: 234-239
    • (1997) Bot Acta , vol.110 , pp. 234-239
    • Desimone, M.1    Weiss-Wichert, C.2    Wagner, E.3    Altenfeld, U.4    Johanningmeier, U.5
  • 10
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B (2002) AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett 529: 6-10
    • (2002) FEBS Lett , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 11
    • 0000656387 scopus 로고    scopus 로고
    • Developmental constraint on photosynthesis: Effects of light and nutrition
    • NR Baker, ed, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Evans JR (1996) Developmental constraint on photosynthesis: effects of light and nutrition. In NR Baker, ed, Photosynthesis and the Environment. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 281-304
    • (1996) Photosynthesis and the Environment , pp. 281-304
    • Evans, J.R.1
  • 12
    • 0032536779 scopus 로고    scopus 로고
    • A novel multi-functional chloroplast protein: Identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen
    • Fulgosi H, Vener AV, Altschmied L, Herrmann RG, Andersson B (1998) A novel multi-functional chloroplast protein: identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen. EMBO J 17: 1577-1587
    • (1998) EMBO J , vol.17 , pp. 1577-1587
    • Fulgosi, H.1    Vener, A.V.2    Altschmied, L.3    Herrmann, R.G.4    Andersson, B.5
  • 13
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM (1989) Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res 17: 4713-4730
    • (1989) Nucleic Acids Res , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 14
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S (1996) Proteases and their targets in Escherichia coli. Annu Rev Genet 30: 465-506
    • (1996) Annu Rev Genet , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 15
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman S, Maurizi MR, Wickner S (1997) Regulatory subunits of energy-dependent proteases. Cell 91: 435-438
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 17
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud R, Kessel M, Beuron F, Stevens AC (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J Biol Chem 273: 12476-12481
    • (1998) J Biol Chem , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Stevens, A.C.4
  • 18
    • 0030098733 scopus 로고    scopus 로고
    • Degradation of mistargeted OEE33 in the chloroplast stroma
    • Halperin T, Adam Z (1996) Degradation of mistargeted OEE33 in the chloroplast stroma. Plant Mol Biol 30: 925-933
    • (1996) Plant Mol Biol , vol.30 , pp. 925-933
    • Halperin, T.1    Adam, Z.2
  • 19
    • 0034850973 scopus 로고    scopus 로고
    • ATP-dependent association between subunits of Clp protease in pea chloroplasts
    • Halperin T, Ostersetzer O, Adam Z (2001b) ATP-dependent association between subunits of Clp protease in pea chloroplasts. Planta 213: 614-619
    • (2001) Planta , vol.213 , pp. 614-619
    • Halperin, T.1    Ostersetzer, O.2    Adam, Z.3
  • 20
    • 0035039711 scopus 로고    scopus 로고
    • Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease
    • Halperin T, Zheng B, Itzhaki H, Clarke AK, Adam Z (2001a) Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease. Plant Mol Biol 45: 461-468
    • (2001) Plant Mol Biol , vol.45 , pp. 461-468
    • Halperin, T.1    Zheng, B.2    Itzhaki, H.3    Clarke, A.K.4    Adam, Z.5
  • 21
    • 0036006185 scopus 로고    scopus 로고
    • Double mutation cpSRP43-/cpSRP54- is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins
    • Hutin C, Havaux M, Carde J, Kloppstech K, Meiherhoff K, Hoffman N, Nussaume L (2002) Double mutation cpSRP43-/cpSRP54- is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins. Plant J 29: 531-543
    • (2002) Plant J , vol.29 , pp. 531-543
    • Hutin, C.1    Havaux, M.2    Carde, J.3    Kloppstech, K.4    Meiherhoff, K.5    Hoffman, N.6    Nussaume, L.7
  • 22
    • 0141866809 scopus 로고    scopus 로고
    • Tic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts
    • Inaba T, Li M, Alvarez-Huerta M, Kessler F, Schnell DJ (2004) atTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts. J Biol Chem 278: 38617-38627
    • (2004) J Biol Chem , vol.278 , pp. 38617-38627
    • Inaba, T.1    Li, M.2    Alvarez-Huerta, M.3    Kessler, F.4    Schnell, D.J.5
  • 24
    • 0035852296 scopus 로고    scopus 로고
    • Molecular chaperones involved in chloroplast protein import
    • Jackson-Constan D, Akita M, Keegstra K (2001) Molecular chaperones involved in chloroplast protein import. Biochim Biophys Acta 1541: 102-113
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 102-113
    • Jackson-Constan, D.1    Akita, M.2    Keegstra, K.3
  • 27
    • 0032539010 scopus 로고    scopus 로고
    • Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane
    • Kouranov A, Chen X, Fuks B, Schnell DJ (1998) Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane. J Cell Biol 143: 991-1002
    • (1998) J Cell Biol , vol.143 , pp. 991-1002
    • Kouranov, A.1    Chen, X.2    Fuks, B.3    Schnell, D.J.4
  • 28
    • 0042823973 scopus 로고    scopus 로고
    • The plastid clpP1 protease gene is essential for plant development
    • Kuroda H, Maliga P (2003) The plastid clpP1 protease gene is essential for plant development. Nature 425: 86-89
    • (2003) Nature , vol.425 , pp. 86-89
    • Kuroda, H.1    Maliga, P.2
  • 29
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • 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
  • 30
    • 0034969531 scopus 로고    scopus 로고
    • The light sensitivity of ATP synthase mutants of Chlamydomonas reinhardtii
    • Majeran W, Olive J, Drapier D, Vallon O, Wollman F-A (2001) The light sensitivity of ATP synthase mutants of Chlamydomonas reinhardtii. Plant Physiol 126: 421-433
    • (2001) Plant Physiol , vol.126 , pp. 421-433
    • Majeran, W.1    Olive, J.2    Drapier, D.3    Vallon, O.4    Wollman, F.-A.5
  • 31
    • 0033961130 scopus 로고    scopus 로고
    • Evidence for a role of ClpP in the degradation of the chloroplast cytochrome b(6)f complex
    • Majeran W, Wollman FA, Vallon O (2000) Evidence for a role of ClpP in the degradation of the chloroplast cytochrome b(6)f complex. Plant Cell 12: 137-149
    • (2000) Plant Cell , vol.12 , pp. 137-149
    • Majeran, W.1    Wollman, F.A.2    Vallon, O.3
  • 32
    • 0027550578 scopus 로고
    • Characterization of a cDNA clone encoding a chloroplast-targeted Clp homologue
    • Moore T, Keegstra K (1993) Characterization of a cDNA clone encoding a chloroplast-targeted Clp homologue. Plant Mol Biol 21: 525-537
    • (1993) Plant Mol Biol , vol.21 , pp. 525-537
    • Moore, T.1    Keegstra, K.2
  • 33
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and ΔpH-dependent pathway
    • Mori H, Cline K (2001) Post-translational protein translocation into thylakoids by the Sec and ΔpH-dependent pathway. Biochim Biophys Acta 1541: 80-90
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 35
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • Nielsen E, Akita M, Davila-Aponte J, Keegstra K (1997) Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J 16: 935-946
    • (1997) EMBO J , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Davila-Aponte, J.3    Keegstra, K.4
  • 36
    • 0029240302 scopus 로고
    • Three types of nuclear genes encoding chloroplast RNA-binding proteins (cp29, cp31 and cp33) are present in Arabidopsis thaliana: Presence of cp31 in chloroplasts and its homologue in nuclei/cytoplasms
    • Ohta M, Sugita M, Sugiura M (1995) Three types of nuclear genes encoding chloroplast RNA-binding proteins (cp29, cp31 and cp33) are present in Arabidopsis thaliana: presence of cp31 in chloroplasts and its homologue in nuclei/cytoplasms. Plant Mol Biol 27: 529-539
    • (1995) Plant Mol Biol , vol.27 , pp. 529-539
    • Ohta, M.1    Sugita, M.2    Sugiura, M.3
  • 37
    • 4344577287 scopus 로고    scopus 로고
    • Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis
    • Park S, Rodermel SR (2004) Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis. Proc Natl Acad Sci USA 101: 12765-12770
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12765-12770
    • Park, S.1    Rodermel, S.R.2
  • 39
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27: 437-496
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 40
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier J, Ripoll DR, Friso G, Rudella A, Cai Y, Ytterberg J, Giacomelli L, Pillardy P, van Wijk KJ (2004) Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J Biol Chem 279: 4768-4781
    • (2004) J Biol Chem , vol.279 , pp. 4768-4781
    • Peltier, J.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, P.8    Van Wijk, K.J.9
  • 41
    • 0035844248 scopus 로고    scopus 로고
    • Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplast of Arabidopsis thaliana
    • Peltier J, Ytterberg J, Liberles DA, Roepstorff P, van Wijk KJ (2001) Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplast of Arabidopsis thaliana. J Biol Chem 276: 16318-16327
    • (2001) J Biol Chem , vol.276 , pp. 16318-16327
    • Peltier, J.1    Ytterberg, J.2    Liberles, D.A.3    Roepstorff, P.4    Van Wijk, K.J.5
  • 42
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra RJ, Thompson WA, Kriedemann PE (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim Biophys Acta 975: 384-394
    • (1989) Biochim Biophys Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 43
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: The driving forces behind RNA metabolism
    • Rocak S, Linder L (2004) DEAD-box proteins: the driving forces behind RNA metabolism. Nat Rev Mol Cell Biol 5: 232-241
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, L.2
  • 44
    • 0037302244 scopus 로고    scopus 로고
    • Leaf-variegated mutations and their responsible genes in Arabidopsis thaliana
    • Sakamoto W (2003) Leaf-variegated mutations and their responsible genes in Arabidopsis thaliana. Genes Genet Syst 78: 1-9
    • (2003) Genes Genet Syst , vol.78 , pp. 1-9
    • Sakamoto, W.1
  • 46
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin J, Dewitt ND, Flanagan JM (1995) The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant Cell 7: 1713-1722
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    Dewitt, N.D.2    Flanagan, J.M.3
  • 47
    • 0035043874 scopus 로고    scopus 로고
    • The chloroplast clpP gene encoding a proteolytic subunit of ATP-dependent protease and is indispensable for chloroplast development in tobacco
    • Shikanai T, Shimizu K, Ueda K, Nishimura Y, Kuroiwa T, Hashimoto T (2001) The chloroplast clpP gene encoding a proteolytic subunit of ATP-dependent protease and is indispensable for chloroplast development in tobacco. Plant Cell Physiol 42: 264-273
    • (2001) Plant Cell Physiol , vol.42 , pp. 264-273
    • Shikanai, T.1    Shimizu, K.2    Ueda, K.3    Nishimura, Y.4    Kuroiwa, T.5    Hashimoto, T.6
  • 48
    • 0001142686 scopus 로고
    • Ultrastructure of the mesophyll in Scots pine and Norway spruce: Seasonal variation and molarity of fixative buffer
    • Soikkeli S (1980) Ultrastructure of the mesophyll in Scots pine and Norway spruce: seasonal variation and molarity of fixative buffer. Protoplasma 103: 241-252
    • (1980) Protoplasma , vol.103 , pp. 241-252
    • Soikkeli, S.1
  • 50
    • 0002314808 scopus 로고    scopus 로고
    • Protein synthesis, assembly, and degradation
    • B Buchanan, W Gruissem, R Jones, eds, American Society of Plant Physiologists, Rockville, MD
    • Spremulli L (2000) Protein synthesis, assembly, and degradation. In B Buchanan, W Gruissem, R Jones, eds, Biochemistry & Biology of Plants. American Society of Plant Physiologists, Rockville, MD, pp 412-456
    • (2000) Biochemistry & Biology of Plants , pp. 412-456
    • Spremulli, L.1
  • 51
    • 85005307126 scopus 로고
    • Cytology of Norway spruce needles: Changes during ageing
    • Sutinen S (1987) Cytology of Norway spruce needles: changes during ageing. Eur J For Pathol 17: 65-73
    • (1987) Eur J For Pathol , vol.17 , pp. 65-73
    • Sutinen, S.1
  • 52
    • 0033117630 scopus 로고    scopus 로고
    • Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis
    • Weaver LM, Froehlich JE, Amasino RM (1999) Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis. Plant Physiol 119: 1209-1216
    • (1999) Plant Physiol , vol.119 , pp. 1209-1216
    • Weaver, L.M.1    Froehlich, J.E.2    Amasino, R.M.3
  • 53
    • 2942596463 scopus 로고    scopus 로고
    • Unscrambling an egg: Protein disaggregation by AAA+ proteins
    • Weibezahn J, Bukau B, Mogk A (2004) Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb Cell Fact 3: 1-12
    • (2004) Microb Cell Fact , vol.3 , pp. 1-12
    • Weibezahn, J.1    Bukau, B.2    Mogk, A.3
  • 54
    • 0026930457 scopus 로고
    • Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants
    • Wong EY, Hironaka CM, Fischhoff DA (1992) Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants. Plant Mol Biol 20: 81-93
    • (1992) Plant Mol Biol , vol.20 , pp. 81-93
    • Wong, E.Y.1    Hironaka, C.M.2    Fischhoff, D.A.3
  • 55
    • 0036095346 scopus 로고    scopus 로고
    • Characterization of chloroplast Clp proteins in Arabidopsis: Localization, tissue specificity and stress responses
    • Zheng B, Halperin T, Hruskova-Heidingsfeldova O, Adam Z, Clarke AK (2002) Characterization of chloroplast Clp proteins in Arabidopsis: localization, tissue specificity and stress responses. Physiol Plant 114: 92-101
    • (2002) Physiol Plant , vol.114 , pp. 92-101
    • Zheng, B.1    Halperin, T.2    Hruskova-Heidingsfeldova, O.3    Adam, Z.4    Clarke, A.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.