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Volumn 145, Issue 1, 2012, Pages 203-214

FtsH proteases located in the plant chloroplast

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CHLOROPLAST PROTEIN; FTSH1 PROTEIN, ARABIDOPSIS; MEMBRANE PROTEIN; METALLOPROTEINASE;

EID: 84859875507     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2011.01548.x     Document Type: Review
Times cited : (101)

References (78)
  • 1
    • 33646145726 scopus 로고    scopus 로고
    • Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts.
    • Adam Z, Rudella A, van Wijk KJ (2006) Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts. Curr Opin Plant Biol 9: 234-240
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 234-240
    • Adam, Z.1    Rudella, A.2    van Wijk, K.J.3
  • 2
    • 0028033333 scopus 로고
    • Involvement of FtsH in protein assembly into and through the membrane. 2. Dominant mutations affecting FtsH functions.
    • Akiyama Y, Shirai Y, Ito K (1994) Involvement of FtsH in protein assembly into and through the membrane. 2. Dominant mutations affecting FtsH functions. J Biol Chem 269: 5225-5229
    • (1994) J Biol Chem , vol.269 , pp. 5225-5229
    • Akiyama, Y.1    Shirai, Y.2    Ito, K.3
  • 3
    • 0030577385 scopus 로고    scopus 로고
    • Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.
    • Akiyama Y, Kihara A, Ito K (1996) Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli. FEBS Lett 399: 26-28
    • (1996) FEBS Lett , vol.399 , pp. 26-28
    • Akiyama, Y.1    Kihara, A.2    Ito, K.3
  • 4
    • 33644841072 scopus 로고    scopus 로고
    • Characterization of the snowy cotyledon 1 mutant of Arabidopsis thaliana: the impact of chloroplast elongation factor G on chloroplast development and plant vitality.
    • Albrecht V, Ingenfeld A, Apel K (2006) Characterization of the snowy cotyledon 1 mutant of Arabidopsis thaliana: the impact of chloroplast elongation factor G on chloroplast development and plant vitality. Plant Mol Biol 60: 507-518
    • (2006) Plant Mol Biol , vol.60 , pp. 507-518
    • Albrecht, V.1    Ingenfeld, A.2    Apel, K.3
  • 5
    • 0037127195 scopus 로고    scopus 로고
    • A critical role for the var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo.
    • Bailey S, Thompson E, Nixon PJ, Horton P, Mullineaux CW, Robinson C, Mann NH (2002) A critical role for the var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo. J Biol Chem 277: 2006-2011
    • (2002) J Biol Chem , vol.277 , pp. 2006-2011
    • Bailey, S.1    Thompson, E.2    Nixon, P.J.3    Horton, P.4    Mullineaux, C.W.5    Robinson, C.6    Mann, N.H.7
  • 7
    • 76049099304 scopus 로고    scopus 로고
    • The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.
    • Bieniossek C, Niederhauser B, Baumann UM (2009) The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation. Proc Natl Acad Sci USA 106: 21579-21584
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21579-21584
    • Bieniossek, C.1    Niederhauser, B.2    Baumann, U.M.3
  • 8
    • 39849088298 scopus 로고    scopus 로고
    • Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development.
    • Blomqvist LA, Ryberg M, Sundqvist C (2008) Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development. Photosyn Res 96: 37-50
    • (2008) Photosyn Res , vol.96 , pp. 37-50
    • Blomqvist, L.A.1    Ryberg, M.2    Sundqvist, C.3
  • 9
    • 0032902789 scopus 로고    scopus 로고
    • The yellow variegated mutant of Arabidopsis is plastid autonomous and delayed in chloroplast biogenesis.
    • Chen M, Jensen M, Rodermel S (1999) The yellow variegated mutant of Arabidopsis is plastid autonomous and delayed in chloroplast biogenesis. J Hered 90: 207-214
    • (1999) J Hered , vol.90 , pp. 207-214
    • Chen, M.1    Jensen, M.2    Rodermel, S.3
  • 10
    • 0034047936 scopus 로고    scopus 로고
    • Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease.
    • Chen M, Choi Y, Voytas DF, Rodermel S (2000) Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease. Plant J 22: 303-313
    • (2000) Plant J , vol.22 , pp. 303-313
    • Chen, M.1    Choi, Y.2    Voytas, D.F.3    Rodermel, S.4
  • 11
    • 33748632913 scopus 로고    scopus 로고
    • FtsH11 protease plays a critical role in Arabidopsis thermotolerance.
    • Chen J, Burke JJ, Velten J, Xin Z (2006) FtsH11 protease plays a critical role in Arabidopsis thermotolerance. Plant J 48: 73-84
    • (2006) Plant J , vol.48 , pp. 73-84
    • Chen, J.1    Burke, J.J.2    Velten, J.3    Xin, Z.4
  • 12
    • 79955632311 scopus 로고    scopus 로고
    • Proteomic identification of differentially expressed proteins in Arabidopsis in response to methyl jasmonate.
    • Chen Y, Pang Q, Dai S, Wang Y, Chen S, Yan X (2011) Proteomic identification of differentially expressed proteins in Arabidopsis in response to methyl jasmonate. J Plant Physiol 168: 995-1008
    • (2011) J Plant Physiol , vol.168 , pp. 995-1008
    • Chen, Y.1    Pang, Q.2    Dai, S.3    Wang, Y.4    Chen, S.5    Yan, X.6
  • 17
    • 79959847676 scopus 로고    scopus 로고
    • ATP-dependent proteases in the plant chloroplast.
    • In: Kutejová E (ed) Research Signpost, Kerala, India
    • Garcia-Lorenzo M, Pruzinska A, Funk C (2008) ATP-dependent proteases in the plant chloroplast. In: Kutejová E (ed) ATP-Dependent Proteases. Research Signpost, Kerala, India, pp 145-177
    • (2008) ATP-Dependent Proteases. , pp. 145-177
    • Garcia-Lorenzo, M.1    Pruzinska, A.2    Funk, C.3
  • 18
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.
    • Hinnerwisch J, Fenton WA, Furtak KJ, Farr GW, Horwich AL (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121: 1029-1041
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 19
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases.
    • Hooper NM (1994) Families of zinc metalloproteases. FEBS Lett 354: 1-6
    • (1994) FEBS Lett , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 20
    • 0029019481 scopus 로고
    • Identification of a plastid protein involved in vesicle fusion and/or membrane-protein translocation.
    • Hugueney P, Bouvier F, Badillo A, Dharlingue A, Kuntz M, Camara B (1995) Identification of a plastid protein involved in vesicle fusion and/or membrane-protein translocation. Proc Natl Acad Sci USA 92: 5630-5634
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5630-5634
    • Hugueney, P.1    Bouvier, F.2    Badillo, A.3    Dharlingue, A.4    Kuntz, M.5    Camara, B.6
  • 21
    • 17444420141 scopus 로고    scopus 로고
    • ATP-dependent proteases in plant mitochondria: what do we know about them today?
    • Janska H (2005) ATP-dependent proteases in plant mitochondria: what do we know about them today? Physiol Plant 123: 399-405
    • (2005) Physiol Plant , vol.123 , pp. 399-405
    • Janska, H.1
  • 22
    • 77957966789 scopus 로고    scopus 로고
    • New insights into the types and function of proteases in plastids.
    • Kato Y, Sakamoto W (2010) New insights into the types and function of proteases in plastids. Int Rev Cell Mol Biol 280: 185-218
    • (2010) Int Rev Cell Mol Biol , vol.280 , pp. 185-218
    • Kato, Y.1    Sakamoto, W.2
  • 23
    • 34250666671 scopus 로고    scopus 로고
    • White leaf sectors in yellow variegated2 are formed by viable cells with undifferentiated plastids.
    • Kato Y, Miura E, Matsushima R, Sakamoto W (2007) White leaf sectors in yellow variegated2 are formed by viable cells with undifferentiated plastids. Plant Physiol 144: 952-960
    • (2007) Plant Physiol , vol.144 , pp. 952-960
    • Kato, Y.1    Miura, E.2    Matsushima, R.3    Sakamoto, W.4
  • 24
    • 71049174469 scopus 로고    scopus 로고
    • The variegated mutants lacking chloroplastic FtsHs are defective in D1 degradation and accumulate reactive oxygen species.
    • Kato Y, Miura E, Ido K, Ifuku K, Sakamoto W (2009) The variegated mutants lacking chloroplastic FtsHs are defective in D1 degradation and accumulate reactive oxygen species. Plant Physiol 151: 790-1801
    • (2009) Plant Physiol , vol.151 , pp. 790-1801
    • Kato, Y.1    Miura, E.2    Ido, K.3    Ifuku, K.4    Sakamoto, W.5
  • 25
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.
    • Kihara A, Akiyama Y, Ito K (1995) FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci USA 92: 4532-4536
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 27
    • 33845642214 scopus 로고    scopus 로고
    • Significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes.
    • Kolodziejczak M, Gibala M, Urantowka A, Hanna J (2007) Significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes. Physiol Plant 129: 135-142
    • (2007) Physiol Plant , vol.129 , pp. 135-142
    • Kolodziejczak, M.1    Gibala, M.2    Urantowka, A.3    Hanna, J.4
  • 28
    • 77950370531 scopus 로고    scopus 로고
    • Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster.
    • Komenda J, Knoppova J, Krynicka V, Nixon PJ, Tichy M (2010) Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster. Biochim Biophys Acta 1797: 566-575
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 566-575
    • Komenda, J.1    Knoppova, J.2    Krynicka, V.3    Nixon, P.J.4    Tichy, M.5
  • 30
    • 0029799889 scopus 로고    scopus 로고
    • Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants.
    • Lindahl M, Tabak S, Cseke L, Pichersky E, Andersson B, Adam Z (1996) Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants. J Biol Chem 271: 29329-29334
    • (1996) J Biol Chem , vol.271 , pp. 29329-29334
    • Lindahl, M.1    Tabak, S.2    Cseke, L.3    Pichersky, E.4    Andersson, B.5    Adam, Z.6
  • 31
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein.
    • Lindahl M, Spetea C, Hundal T, Oppenheim AB, Adam Z, Andersson B (2000) The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell 12: 419-431
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 32
    • 78649761939 scopus 로고    scopus 로고
    • An Arabidopsis pentatricopeptide repeat protein, SUPPRESSOR OF VARIEGATION7, is required for FtsH-mediated chloroplast biogenesis.
    • Liu X, Yu F, Rodermel S (2010a) An Arabidopsis pentatricopeptide repeat protein, SUPPRESSOR OF VARIEGATION7, is required for FtsH-mediated chloroplast biogenesis. Plant Physiol 154: 1588-1601
    • (2010) Plant Physiol , vol.154 , pp. 1588-1601
    • Liu, X.1    Yu, F.2    Rodermel, S.3
  • 33
    • 77955124084 scopus 로고    scopus 로고
    • Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review.
    • Liu XY, Yu F, Rodermel S (2010b) Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review. J Integr Plant Biol 52: 750-761
    • (2010) J Integr Plant Biol , vol.52 , pp. 750-761
    • Liu, X.Y.1    Yu, F.2    Rodermel, S.3
  • 35
    • 34250659199 scopus 로고    scopus 로고
    • The balance between protein synthesis and degradation in chloroplasts determines leaf variegation in Arabidopsis yellow variegated mutants.
    • Miura E, Kato Y, Matsushima R, Albrecht V, Laalami S, Sakamoto W (2007) The balance between protein synthesis and degradation in chloroplasts determines leaf variegation in Arabidopsis yellow variegated mutants. Plant Cell 19: 1313-1328
    • (2007) Plant Cell , vol.19 , pp. 1313-1328
    • Miura, E.1    Kato, Y.2    Matsushima, R.3    Albrecht, V.4    Laalami, S.5    Sakamoto, W.6
  • 37
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II.
    • Nixon PJ, Michoux F, Yu JF, Boehm M, Komenda J (2010) Recent advances in understanding the assembly and repair of photosystem II. Ann Bot 106: 1-16
    • (2010) Ann Bot , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.F.3    Boehm, M.4    Komenda, J.5
  • 38
    • 0034885052 scopus 로고    scopus 로고
    • AAA(+) superfamily ATPases: common structure-diverse function.
    • Ogura T, Wilkinson AJ (2001) AAA(+) superfamily ATPases: common structure-diverse function. Genes Cells 6: 575-597
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 39
    • 0031153994 scopus 로고    scopus 로고
    • Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease.
    • Ostersetzer O, Adam Z (1997) Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease. Plant Cell 9: 957-965
    • (1997) Plant Cell , vol.9 , pp. 957-965
    • Ostersetzer, O.1    Adam, Z.2
  • 40
    • 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
  • 42
    • 77951246247 scopus 로고    scopus 로고
    • Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana.
    • Piechota J, Kolodziejczak M, Juszczak I, Sakamoto W, Janska H (2010) Identification and characterization of high molecular weight complexes formed by matrix AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana. J Biol Chem 285: 12512-12521
    • (2010) J Biol Chem , vol.285 , pp. 12512-12521
    • Piechota, J.1    Kolodziejczak, M.2    Juszczak, I.3    Sakamoto, W.4    Janska, H.5
  • 43
    • 79551639846 scopus 로고    scopus 로고
    • FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex.
    • Rodrigues RAO, Silva MC, Cline K (2011) FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex. Plant J 65: 600-609
    • (2011) Plant J , vol.65 , pp. 600-609
    • Rodrigues, R.A.O.1    Silva, M.C.2    Cline, K.3
  • 45
    • 1642356725 scopus 로고    scopus 로고
    • FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli.
    • Saikawa N, Akiyama Y, Ito KJ (2004) FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli. Struct Biol 146: 123-129
    • (2004) Struct Biol , vol.146 , pp. 123-129
    • Saikawa, N.1    Akiyama, Y.2    Ito, K.J.3
  • 46
    • 0036668462 scopus 로고    scopus 로고
    • The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles.
    • Sakamoto W, Tamura T, Hanba-Tomita Y, Murata M (2002) The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles. Genes Cells 7: 769-780
    • (2002) Genes Cells , vol.7 , pp. 769-780
    • Sakamoto, W.1    Tamura, T.2    Hanba-Tomita, Y.3    Murata, M.4
  • 47
    • 0347380954 scopus 로고    scopus 로고
    • Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes.
    • Sakamoto W, Zaltsman A, Adam Z, Takahashi Y (2003) Coordinated regulation and complex formation of yellow variegated1 and yellow variegated2, chloroplastic FtsH metalloproteases involved in the repair cycle of photosystem II in Arabidopsis thylakoid membranes. Plant Cell 15: 2843-2855
    • (2003) Plant Cell , vol.15 , pp. 2843-2855
    • Sakamoto, W.1    Zaltsman, A.2    Adam, Z.3    Takahashi, Y.4
  • 48
    • 72649100053 scopus 로고    scopus 로고
    • Arrested differentiation of proplastids into chloroplasts in variegated leaves characterized by plastid ultrastructure and nucleoid morphology.
    • Sakamoto W, Uno Y, Zhang Q, Miura E, Kato Y, Sodmergen (2009) Arrested differentiation of proplastids into chloroplasts in variegated leaves characterized by plastid ultrastructure and nucleoid morphology. Plant Cell Physiol 50: 2069-2083
    • (2009) Plant Cell Physiol , vol.50 , pp. 2069-2083
    • Sakamoto, W.1    Uno, Y.2    Zhang, Q.3    Miura, E.4    Kato, Y.5    Sodmergen6
  • 49
    • 0016627718 scopus 로고
    • Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12.
    • Santos D, De Almeida DF (1975) Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12. J Bacteriol 124: 1502-1507
    • (1975) J Bacteriol , vol.124 , pp. 1502-1507
    • Santos, D.1    De Almeida, D.F.2
  • 50
    • 0032965905 scopus 로고    scopus 로고
    • FtsH - a single-chain charonin?
    • Schumann W (1999) FtsH - a single-chain charonin? Fems Microbiol Rev 23: 1-11
    • (1999) Fems Microbiol Rev , vol.23 , pp. 1-11
    • Schumann, W.1
  • 51
    • 0033923140 scopus 로고    scopus 로고
    • Reduced levels of chloroplast FtsH protein in tobacco mosaic virus-infected tobacco leaves accelerate the hypersensitive reaction.
    • Seo S, Okamoto M, Iwai T, Iwano M, Fukui K, Isogai A, Nakajima N, Ohashi Y (2000) Reduced levels of chloroplast FtsH protein in tobacco mosaic virus-infected tobacco leaves accelerate the hypersensitive reaction. Plant Cell 12: 917-932
    • (2000) Plant Cell , vol.12 , pp. 917-932
    • Seo, S.1    Okamoto, M.2    Iwai, T.3    Iwano, M.4    Fukui, K.5    Isogai, A.6    Nakajima, N.7    Ohashi, Y.8
  • 53
    • 35148872652 scopus 로고    scopus 로고
    • The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts.
    • Shen G, Adam Z, Zhang H (2007) The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts. Plant J 52: 309-321
    • (2007) Plant J , vol.52 , pp. 309-321
    • Shen, G.1    Adam, Z.2    Zhang, H.3
  • 55
    • 0036935397 scopus 로고    scopus 로고
    • The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts.
    • Sokolenko A, Pojidaeva E, Zinchenko V, Panichkin V, Glaser VM, Herrmann RG, Shestakov SV (2002) The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts. Curr Genet 41: 291-310
    • (2002) Curr Genet , vol.41 , pp. 291-310
    • Sokolenko, A.1    Pojidaeva, E.2    Zinchenko, V.3    Panichkin, V.4    Glaser, V.M.5    Herrmann, R.G.6    Shestakov, S.V.7
  • 56
    • 0034604535 scopus 로고    scopus 로고
    • The thylakoid delta pH-dependent pathway machinery facilitates RR-independent N-tail protein integration.
    • Summer EJ, Mori H, Settles AM, Cline K (2000) The thylakoid delta pH-dependent pathway machinery facilitates RR-independent N-tail protein integration. J Biol Chem 275: 23483-23490
    • (2000) J Biol Chem , vol.275 , pp. 23483-23490
    • Summer, E.J.1    Mori, H.2    Settles, A.M.3    Cline, K.4
  • 57
    • 30944434604 scopus 로고    scopus 로고
    • Identification and characterization of a heat-inducible FtsH gene from tomato (Lycopersicon esculentum Mill.).
    • Sun A, Yi S, Yang J, Zhao C, Liu J (2006) Identification and characterization of a heat-inducible FtsH gene from tomato (Lycopersicon esculentum Mill.). Plant Sci 170: 551-562
    • (2006) Plant Sci , vol.170 , pp. 551-562
    • Sun, A.1    Yi, S.2    Yang, J.3    Zhao, C.4    Liu, J.5
  • 58
    • 33744552902 scopus 로고    scopus 로고
    • Structure of the whole cytosolic region of ATP-dependent protease FtsH.
    • Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K (2006) Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol Cell 22: 575-585
    • (2006) Mol Cell , vol.22 , pp. 575-585
    • Suno, R.1    Niwa, H.2    Tsuchiya, D.3    Zhang, X.4    Yoshida, M.5    Morikawa, K.6
  • 59
    • 0034485494 scopus 로고    scopus 로고
    • The YELLOW VARIEGATED (VAR2) locus encodes a homologue of FtsH, an ATP-dependent protease in Arabidopsis.
    • Takechi K, Sodmergen Murata M, Motoyoshi F, Sakamoto W (2000) The YELLOW VARIEGATED (VAR2) locus encodes a homologue of FtsH, an ATP-dependent protease in Arabidopsis. Plant Cell Physiol 41: 1334-1346
    • (2000) Plant Cell Physiol , vol.41 , pp. 1334-1346
    • Takechi, K.1    Sodmergen Murata, M.2    Motoyoshi, F.3    Sakamoto, W.4
  • 60
    • 0035979317 scopus 로고    scopus 로고
    • Multiple transcription-factor genes are early targets of phytochrome A signaling.
    • Tepperman JM, Zhu T, Chang HS, Wang X, Quail PH (2001) Multiple transcription-factor genes are early targets of phytochrome A signaling. Proc Natl Acad Sci USA 98: 9437-9442
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9437-9442
    • Tepperman, J.M.1    Zhu, T.2    Chang, H.S.3    Wang, X.4    Quail, P.H.5
  • 61
    • 0027535381 scopus 로고
    • The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell-cycle control, and gene-expression.
    • Tomoyasu T, Yuki T, Morimura S, Mori H, Yamanaka K, Niki H, Hiraga S, Ogura T (1993) The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell-cycle control, and gene-expression. J Bacteriol 175: 1344-1351
    • (1993) J Bacteriol , vol.175 , pp. 1344-1351
    • Tomoyasu, T.1    Yuki, T.2    Morimura, S.3    Mori, H.4    Yamanaka, K.5    Niki, H.6    Hiraga, S.7    Ogura, T.8
  • 63
    • 22044437388 scopus 로고    scopus 로고
    • The botany array resource: e-Northerns, expression angling, and promoter analyses.
    • Toufighi K, Brady SM, Austin R, Ly E, Provart NJ (2005) The botany array resource: e-Northerns, expression angling, and promoter analyses. Plant J 43: 153-163
    • (2005) Plant J , vol.43 , pp. 153-163
    • Toufighi, K.1    Brady, S.M.2    Austin, R.3    Ly, E.4    Provart, N.J.5
  • 65
    • 42049104126 scopus 로고    scopus 로고
    • Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins.
    • van Bloois E, Dekker HL, Froderberg L, Houben EN, Urbanus ML, de Koster CG, de Gier JW, Luirink J (2008) Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins. FEBS Lett 582: 1419-1424
    • (2008) FEBS Lett , vol.582 , pp. 1419-1424
    • van Bloois, E.1    Dekker, H.L.2    Froderberg, L.3    Houben, E.N.4    Urbanus, M.L.5    de Koster, C.G.6    de Gier, J.W.7    Luirink, J.8
  • 66
    • 79959856338 scopus 로고    scopus 로고
    • Fitness analyses of Arabidopsis thaliana mutants depleted of FtsH metalloproteases and characterization of three ftsh6 deletion mutants exposed to high light stress, senescence and chilling.
    • Wagner R, Aigner H, Pruzinska A, Jänkänpää HJ, Jansson S, Funk C (2011) Fitness analyses of Arabidopsis thaliana mutants depleted of FtsH metalloproteases and characterization of three ftsh6 deletion mutants exposed to high light stress, senescence and chilling. New Phytol 191: 449-458
    • (2011) New Phytol , vol.191 , pp. 449-458
    • Wagner, R.1    Aigner, H.2    Pruzinska, A.3    Jänkänpää, H.J.4    Jansson, S.5    Funk, C.6
  • 67
    • 40349091686 scopus 로고    scopus 로고
    • An "electronic fluorescent pictograph" browser for exploring and analyzing large-scale biological data sets.
    • Winter D, Vinegar B, Nahal H, Ammar R, Wilson GV, Provart NJ (2007) An "electronic fluorescent pictograph" browser for exploring and analyzing large-scale biological data sets. PloS One 2: e718
    • (2007) PloS One , vol.2
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6
  • 68
    • 33746811366 scopus 로고    scopus 로고
    • Quality control of photosystem II - cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress.
    • Yoshioka M, Uchida S, Mori H, Komayama K, Ohira S, Morita N, Nakanishi T, Yamamoto Y (2006) Quality control of photosystem II - cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress. J Biol Chem 281: 21660-21669
    • (2006) J Biol Chem , vol.281 , pp. 21660-21669
    • Yoshioka, M.1    Uchida, S.2    Mori, H.3    Komayama, K.4    Ohira, S.5    Morita, N.6    Nakanishi, T.7    Yamamoto, Y.8
  • 69
    • 78650640619 scopus 로고    scopus 로고
    • Quality control of photosystem II: FtsH hexamers are localized near photosystem II at grana for the swift repair of damage.
    • Yoshioka M, Nakayama Y, Yoshida M, Ohashi K, Morita N, Kobayashi H, Yamamoto Y (2010) Quality control of photosystem II: FtsH hexamers are localized near photosystem II at grana for the swift repair of damage. J Biol Chem 285: 41972-41981
    • (2010) J Biol Chem , vol.285 , pp. 41972-41981
    • Yoshioka, M.1    Nakayama, Y.2    Yoshida, M.3    Ohashi, K.4    Morita, N.5    Kobayashi, H.6    Yamamoto, Y.7
  • 70
    • 1642278051 scopus 로고    scopus 로고
    • The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes.
    • Yu F, Park S, Rodermel SR (2004) The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes. Plant J 37: 864-876
    • (2004) Plant J , vol.37 , pp. 864-876
    • Yu, F.1    Park, S.2    Rodermel, S.R.3
  • 71
    • 33644684616 scopus 로고    scopus 로고
    • Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes.
    • Yu F, Park S, Rodermel SR (2005) Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes. Plant Physiol 138: 1957-1966
    • (2005) Plant Physiol , vol.138 , pp. 1957-1966
    • Yu, F.1    Park, S.2    Rodermel, S.R.3
  • 72
    • 57749111990 scopus 로고    scopus 로고
    • Mutations in suppressor of variegation1, a factor required for normal chloroplast translation, suppress var2-mediated leaf variegation in Arabidopsis.
    • Yu F, Liu XY, Alsheikh M, Park S, Rodermel S (2008) Mutations in suppressor of variegation1, a factor required for normal chloroplast translation, suppress var2-mediated leaf variegation in Arabidopsis. Plant Cell 20: 1786-1804
    • (2008) Plant Cell , vol.20 , pp. 1786-1804
    • Yu, F.1    Liu, X.Y.2    Alsheikh, M.3    Park, S.4    Rodermel, S.5
  • 74
    • 20444444744 scopus 로고    scopus 로고
    • Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts - implications for thylakoid formation and photosystem II maintenance.
    • Zaltsman A, Feder A, Adam Z (2005a) Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts - implications for thylakoid formation and photosystem II maintenance. Plant J 42: 609-617
    • (2005) Plant J , vol.42 , pp. 609-617
    • Zaltsman, A.1    Feder, A.2    Adam, Z.3
  • 75
    • 33644874521 scopus 로고    scopus 로고
    • Two types of FtsH protease subunits are required for chloroplast biogenesis and photosystem II repair in Arabidopsis.
    • Zaltsman A, Ori N, Adam Z (2005b) Two types of FtsH protease subunits are required for chloroplast biogenesis and photosystem II repair in Arabidopsis. Plant Cell 17: 2782-2790
    • (2005) Plant Cell , vol.17 , pp. 2782-2790
    • Zaltsman, A.1    Ori, N.2    Adam, Z.3
  • 76
    • 26444535294 scopus 로고    scopus 로고
    • AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence.
    • Zelisko A, Garcia-Lorenzo M, Jackowski G, Jansson S, Funk C (2005) AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence. Proc Natl Acad Sci USA 102: 13699-13704
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13699-13704
    • Zelisko, A.1    Garcia-Lorenzo, M.2    Jackowski, G.3    Jansson, S.4    Funk, C.5
  • 77
    • 66949133502 scopus 로고    scopus 로고
    • Activation of the heterotrimeric G protein alpha-subunit GPA1 suppresses the ftsh-mediated inhibition of chloroplast development in Arabidopsis.
    • Zhang LG, Wei Q, Wu WJ, Cheng YX, Hu GZ, Hu FH, Sun Y, Zhu Y, Sakamoto W, Huang J (2009) Activation of the heterotrimeric G protein alpha-subunit GPA1 suppresses the ftsh-mediated inhibition of chloroplast development in Arabidopsis. Plant J 58: 1041-1053
    • (2009) Plant J , vol.58 , pp. 1041-1053
    • Zhang, L.G.1    Wei, Q.2    Wu, W.J.3    Cheng, Y.X.4    Hu, G.Z.5    Hu, F.H.6    Sun, Y.7    Zhu, Y.8    Sakamoto, W.9    Huang, J.10
  • 78
    • 78650855762 scopus 로고    scopus 로고
    • The FtsH protease heterocomplex in Arabidopsis: dispensability of type-B protease activity for proper chloroplast development.
    • Zhang D, Kato Y, Zhang LG, Fujimoto M, Tsutsumi N, Sodmergen Sakamoto W (2010) The FtsH protease heterocomplex in Arabidopsis: dispensability of type-B protease activity for proper chloroplast development. Plant Cell 22: 3710-3725
    • (2010) Plant Cell , vol.22 , pp. 3710-3725
    • Zhang, D.1    Kato, Y.2    Zhang, L.G.3    Fujimoto, M.4    Tsutsumi, N.5    Sodmergen, S.W.6


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