메뉴 건너뛰기




Volumn 218, Issue 3, 2004, Pages 396-405

A single recessive mutation in the proteolytic machinery of Arabidopsis chloroplasts impairs photoprotection and photosynthesis upon cold stress

Author keywords

Arabidopsis; Chloroplast; Photoprotection; Photosynthesis; Proteolysis

Indexed keywords

ADENOSINETRIPHOSPHATE; CHLOROPHYLL; GENES; MUTAGENESIS; PHOTOSYNTHESIS; PHYSIOLOGY; PROTEINS; SEED;

EID: 0742302388     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-003-1120-6     Document Type: Article
Times cited : (2)

References (45)
  • 1
    • 0030471302 scopus 로고    scopus 로고
    • Protein stability and degradation in chloroplasts
    • Adam Z (1996) Protein stability and degradation in chloroplasts. Plant Mol Biol 32:773-783
    • (1996) Plant Mol Biol , vol.32 , pp. 773-783
    • Adam, Z.1
  • 2
    • 0033865239 scopus 로고    scopus 로고
    • Chloroplast proteases: Possible regulators of gene expression?
    • Adam Z (2000) Chloroplast proteases: possible regulators of gene expression? Biochimie 82:647-654
    • (2000) Biochimie , vol.82 , pp. 647-654
    • Adam, Z.1
  • 3
    • 0003955248 scopus 로고    scopus 로고
    • Chloroplast proteases and their role in photosynthesis regulation
    • Aro E-M, Andersson B (eds). Kluwer, Dordrecht
    • Adam Z (2001) Chloroplast proteases and their role in photosynthesis regulation. In: Aro E-M, Andersson B (eds) Regulation of photosynthesis. Kluwer, Dordrecht, pp 265-276
    • (2001) Regulation of Photosynthesis , pp. 265-276
    • Adam, Z.1
  • 4
    • 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
  • 5
    • 0008398851 scopus 로고    scopus 로고
    • The proteolytic machinery of chloroplasts: Homologues of bacterial proteases
    • Garab G (ed). Kluwer, Dordrecht
    • Adam Z, Halperin T, Itzhaki H, Lindahl M, Ostersetzer O (1998). The proteolytic machinery of chloroplasts: homologues of bacterial proteases. In: Garab G (ed) Photosynthesis: mechanisms and effects, vol 3. Kluwer, Dordrecht, pp 1871-1876
    • (1998) Photosynthesis: Mechanisms and Effects , vol.3 , pp. 1871-1876
    • Adam, Z.1    Halperin, T.2    Itzhaki, H.3    Lindahl, M.4    Ostersetzer, O.5
  • 7
    • 0030767058 scopus 로고    scopus 로고
    • Proteolytic activities and proteases of plant chloroplasts
    • Andersson B, Aro E-M (1997) Proteolytic activities and proteases of plant chloroplasts. Physiol Plant 100:780-793
    • (1997) Physiol Plant , vol.100 , pp. 780-793
    • Andersson, B.1    Aro, E.-M.2
  • 8
    • 0027388885 scopus 로고
    • Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent protein degradation
    • Bachmair A, Becker F, Schell J (1993) Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent protein degradation. Proc Natl Acad Sci USA 90:418-421
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 418-421
    • Bachmair, A.1    Becker, F.2    Schell, J.3
  • 9
    • 0027435506 scopus 로고
    • In planta Agrobacterium mediated gene transfer by infiltration of adult Arabidopsis thaliana plants
    • Bechtold N, Ellis J, Pelletier G (1993) In planta Agrobacterium mediated gene transfer by infiltration of adult Arabidopsis thaliana plants. C R Acad Sci Paris Life Sci 316:1194-1199
    • (1993) C R Acad Sci Paris Life Sci , vol.316 , pp. 1194-1199
    • Bechtold, N.1    Ellis, J.2    Pelletier, G.3
  • 10
    • 0025098346 scopus 로고
    • Binary vectors which allow the exchange of plant selectable markers and reporter genes
    • Becker D (1990) Binary vectors which allow the exchange of plant selectable markers and reporter genes. Nucleic Acids Res 18:203
    • (1990) Nucleic Acids Res , vol.18 , pp. 203
    • Becker, D.1
  • 12
    • 0036800801 scopus 로고    scopus 로고
    • Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis thaliana
    • Chassin Y, Kapri-Pardes E, Sinvany G, Arad T, Adam Z (2002) Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis thaliana. Plant Physiol 130:857-864
    • (2002) Plant Physiol , vol.130 , pp. 857-864
    • Chassin, Y.1    Kapri-Pardes, E.2    Sinvany, G.3    Arad, T.4    Adam, Z.5
  • 13
    • 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
  • 14
    • 0033045606 scopus 로고    scopus 로고
    • ATP-dependent Clp proteases in photosynthetic organisms - A cut above the rest!
    • Clarke AK (1999) ATP-dependent Clp proteases in photosynthetic organisms - a cut above the rest! Ann Bot 83:593-599
    • (1999) Ann Bot , vol.83 , pp. 593-599
    • Clarke, A.K.1
  • 15
    • 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
  • 16
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S, Wickner S, Maurizi MR (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11:815-823
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 17
    • 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
  • 18
    • 0034850973 scopus 로고    scopus 로고
    • ATP-dependent association between subunits of Clp protease in pea chloroplasts
    • Halperin T, Ostersetzer O, Adam Z (2001) 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
  • 19
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II
    • Haussuhl K, Andersson B, Adamska I (2001) A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J 20:713-722
    • (2001) EMBO J , vol.20 , pp. 713-722
    • Haussuhl, K.1    Andersson, B.2    Adamska, I.3
  • 21
    • 0032549650 scopus 로고    scopus 로고
    • Identification and characterization of DegP, a serine protease associated with the luminal side of the thylakoid membrane
    • Itzhaki H, Naveh L, Lindahl M, Cook M, Adam Z (1998) Identification and characterization of DegP, a serine protease associated with the luminal side of the thylakoid membrane. J Biol Chem 273:7094-7098
    • (1998) J Biol Chem , vol.273 , pp. 7094-7098
    • Itzhaki, H.1    Naveh, L.2    Lindahl, M.3    Cook, M.4    Adam, Z.5
  • 24
    • 0029821246 scopus 로고    scopus 로고
    • Identification of transferred DNA insertions within Arabidopsis genes involved in signal transduction and ion transport
    • Krysan PJ, Young JC, Tax F, Sussman MR (1996) Identification of transferred DNA insertions within Arabidopsis genes involved in signal transduction and ion transport. Proc Natl Acad Sci USA 93:8145-50
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8145-8150
    • Krysan, P.J.1    Young, J.C.2    Tax, F.3    Sussman, M.R.4
  • 25
    • 0034194179 scopus 로고    scopus 로고
    • AAA proteases: Cellular machines for degrading membrane proteins
    • Langer T (2000) AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem Sci 25:247-251
    • (2000) Trends Biochem Sci , vol.25 , pp. 247-251
    • Langer, T.1
  • 26
    • 0030475162 scopus 로고    scopus 로고
    • Regulated protein degradation in mitochondria
    • Langer T, Neupert W (1996) Regulated protein degradation in mitochondria. Experientia 52:1069-1076
    • (1996) Experientia , vol.52 , pp. 1069-1076
    • Langer, T.1    Neupert, W.2
  • 27
    • 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
  • 28
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl, 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
    • Lindahl1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 31
    • 0032948239 scopus 로고    scopus 로고
    • Photosystem-II damage and repair cycle in chloroplasts: What modulates the rate of photodamage?
    • Melis A (1999) Photosystem-II damage and repair cycle in chloroplasts: what modulates the rate of photodamage? Trends Plant Sci 4:130-135
    • (1999) Trends Plant Sci , vol.4 , pp. 130-135
    • Melis, A.1
  • 32
    • 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
  • 33
    • 0035844248 scopus 로고    scopus 로고
    • Identification of a 350 kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana
    • Peltier J-B, Ytterberg J, Liberles DA, Roepstorff P, van Wijk KJ (2001) Identification of a 350 kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana. J Biol Chem 276:16318-16327
    • (2001) J Biol Chem , vol.276 , pp. 16318-16327
    • Peltier, J.-B.1    Ytterberg, J.2    Liberles, D.A.3    Roepstorff, P.4    Van Wijk, K.J.5
  • 35
    • 0000226607 scopus 로고
    • Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes
    • Barber J (ed). Elsevier, Amsterdam
    • Prasil O, Adir N, Ohad I (1992) Dynamics of photosystem II: mechanism of photoinhibition and recovery processes. In: Barber J (ed) Topics in photosynthesis. Elsevier, Amsterdam, pp 295-348
    • (1992) Topics in Photosynthesis , pp. 295-348
    • Prasil, O.1    Adir, N.2    Ohad, I.3
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0000968916 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I: Its physiological significance in the chilling sensitivity of plants
    • Sonoike K (1996a) Photoinhibition of photosystem I: its physiological significance in the chilling sensitivity of plants. Plant Cell Physiol 37:239-247
    • (1996) Plant Cell Physiol , vol.37 , pp. 239-247
    • Sonoike, K.1
  • 39
    • 0000628304 scopus 로고    scopus 로고
    • Degradation of PsaB gene product, the reaction center subunit of photosystem I, is caused during photoinhibition of photosystem I: Possible involvement of active oxygen species
    • Sonoike K (1996b) Degradation of PsaB gene product, the reaction center subunit of photosystem I, is caused during photoinhibition of photosystem I: possible involvement of active oxygen species. Plant Sci 115:157-164
    • (1996) Plant Sci , vol.115 , pp. 157-164
    • Sonoike, K.1
  • 40
    • 0021796824 scopus 로고
    • The aminoglycoside resistance operon of the plasmid pSa: Nucleotide sequence of the streptomycin-spectinomycin resistance gene
    • Tait RC, Rempel H, Rodriguez RL, Kadu CI (1985) The aminoglycoside resistance operon of the plasmid pSa: nucleotide sequence of the streptomycin-spectinomycin resistance gene. Gene 36:97-104
    • (1985) Gene , vol.36 , pp. 97-104
    • Tait, R.C.1    Rempel, H.2    Rodriguez, R.L.3    Kadu, C.I.4
  • 41
    • 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    Sodmergen2    Murata, M.3    Motoyoshi, F.4    Sakamoto, W.5
  • 42
    • 0028025799 scopus 로고
    • The site of photoinhibition in leaves of Cucumis sativa L. at low temperatures is photosystem I, not photosystem II
    • Terashima I, Funayama S, Sonoike K (1994) The site of photoinhibition in leaves of Cucumis sativa L. at low temperatures is photosystem I, not photosystem II. Planta 193:300-306
    • (1994) Planta , vol.193 , pp. 300-306
    • Terashima, I.1    Funayama, S.2    Sonoike, K.3
  • 43
    • 0032876021 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I damages both reaction center proteins PSI-A and PSI-B and acceptor-side located small photosystem I polypeptides
    • Tjus SE, Moller BL, Scheller HV (1999) Photoinhibition of photosystem I damages both reaction center proteins PSI-A and PSI-B and acceptor-side located small photosystem I polypeptides. Photosynth Res 60:75-86
    • (1999) Photosynth Res , vol.60 , pp. 75-86
    • Tjus, S.E.1    Moller, B.L.2    Scheller, H.V.3
  • 45
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286:1888-1893
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.