메뉴 건너뛰기




Volumn 15, Issue 9, 2003, Pages 2152-2164

FtsH is involved in the early stages of repair of photosystem II in Synechocystis sp PCC 6803

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; BIOSYNTHESIS; MUTAGENESIS; PHOTOCHEMICAL REACTIONS; PLANTS (BOTANY);

EID: 0141787934     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.012609     Document Type: Article
Times cited : (201)

References (68)
  • 2
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of proteolysis
    • Adam, Z., and Clarke, A.K. (2002). Cutting edge of proteolysis. Trends Plant Sci. 7, 451-456.
    • (2002) Trends Plant Sci. , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 3
    • 0037062428 scopus 로고    scopus 로고
    • Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli
    • Akiyama, Y. (2002). Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli. Proc. Natl. Acad. Sci. USA 99, 8066-8071.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8066-8071
    • Akiyama, Y.1
  • 4
    • 0038043180 scopus 로고    scopus 로고
    • Reconstitution of membrane proteolysis by FtsH
    • Akiyama, Y., and Ito, K. (2003). Reconstitution of membrane proteolysis by FtsH. J. Biol. Chem. 278, 18146-18153.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18146-18153
    • Akiyama, Y.1    Ito, K.2
  • 5
    • 0000040282 scopus 로고    scopus 로고
    • Photodamage and D1 protein turnover in photosystem II
    • E.-M. Aro and B. Andersson, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Andersson, B., and Aro, E.-M. (2001). Photodamage and D1 protein turnover in photosystem II. In Regulation of Photosynthesis, E.-M. Aro and B. Andersson, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 377-393.
    • (2001) Regulation of Photosynthesis , pp. 377-393
    • Andersson, B.1    Aro, E.-M.2
  • 6
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II: Inactivation, protein damage and turnover
    • Aro, E.M., Virgin, I., and Andersson, B. (1993). Photoinhibition of photosystem II: Inactivation, protein damage and turnover. Biochim. Biophys. Acta 1143, 113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 7
    • 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, P.J., Horton, P., Mullineaux, C.W., Robinson, C., and Mann, N.H. (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
  • 8
    • 0026547142 scopus 로고
    • Too much of a good thing: Light can be bad for photosynthesis
    • Barber, J., and Andersson, B. (1992). Too much of a good thing: Light can be bad for photosynthesis. Trends Biochem. Sci. 17, 61-66.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 61-66
    • Barber, J.1    Andersson, B.2
  • 9
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H.J. (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 10
    • 0032476625 scopus 로고    scopus 로고
    • Isolation of a highly active photosystem II preparation from Synechocystis 6803 using a histidine-tagged mutant of CP 47
    • Bricker, T.M., Morvant, J., Masri, N., Sutton, H.M., and Frankel, L.K. (1998). Isolation of a highly active photosystem II preparation from Synechocystis 6803 using a histidine-tagged mutant of CP 47. Biochim. Biophys. Acta 1409, 50-57.
    • (1998) Biochim. Biophys. Acta , vol.1409 , pp. 50-57
    • Bricker, T.M.1    Morvant, J.2    Masri, N.3    Sutton, H.M.4    Frankel, L.K.5
  • 11
    • 0027325215 scopus 로고
    • Detection of a 10 kDa breakdown product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism
    • Canovas, P.M., and Barber, J. (1993). Detection of a 10 kDa breakdown product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism. FEBS Lett. 324, 341-344.
    • (1993) FEBS Lett. , vol.324 , pp. 341-344
    • Canovas, P.M.1    Barber, J.2
  • 12
    • 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, D.F., and 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
  • 13
    • 0036720126 scopus 로고    scopus 로고
    • Membrane protein degradation by FtsH can be initiated from either end
    • Chiba, S., Akiyama, Y., and Ito, K. (2002). Membrane protein degradation by FtsH can be initiated from either end. J. Bacteriol. 184, 4775-4782.
    • (2002) J. Bacteriol. , vol.184 , pp. 4775-4782
    • Chiba, S.1    Akiyama, Y.2    Ito, K.3
  • 14
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • Clausen, T., Southan, C., and Ehrmann, M. (2002). The HtrA family of proteases: Implications for protein composition and cell fate. Mol. Cell 10, 443-455.
    • (2002) Mol. Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 15
    • 0034728355 scopus 로고    scopus 로고
    • Recovery of photosystem II activity in photoinhibited Synechocystis cells: Light-dependent translation activity is required besides light-independent synthesis of the D1 protein
    • Constant, S., Eisenberg-Domovitch, Y., Ohad, I., and Kirilovsky, D. (2000). Recovery of photosystem II activity in photoinhibited Synechocystis cells: Light-dependent translation activity is required besides light-independent synthesis of the D1 protein. Biochemistry 39, 2032-2041.
    • (2000) Biochemistry , vol.39 , pp. 2032-2041
    • Constant, S.1    Eisenberg-Domovitch, Y.2    Ohad, I.3    Kirilovsky, D.4
  • 16
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis
    • Diner, B.A., and Rappaport, F. (2002). Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis. Annu. Rev. Plant Biol. 53, 551-580.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 17
    • 0000829783 scopus 로고
    • Characterization of the photosystem II 32kDa protein in Synechococcus PCC 7942
    • Goloubinoff, P., Brusslan, J., Golden, S., Haselkorn, R., and Edelman, M. (1988). Characterization of the photosystem II 32kDa protein in Synechococcus PCC 7942. Plant Mol. Biol. 11, 441-447.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 441-447
    • Goloubinoff, P.1    Brusslan, J.2    Golden, S.3    Haselkorn, R.4    Edelman, M.5
  • 18
    • 0023429786 scopus 로고
    • Identification of a primary in vivo degradation product of the rapidly-turning-over 32 kD protein of photosystem II
    • Greenberg, B.M., Gaba, V., Mattoo, A.K., and Edelman, M. (1987). Identification of a primary in vivo degradation product of the rapidly-turning-over 32 kD protein of photosystem II. EMBO J. 6, 2865-2869.
    • (1987) EMBO J. , vol.6 , pp. 2865-2869
    • Greenberg, B.M.1    Gaba, V.2    Mattoo, A.K.3    Edelman, M.4
  • 19
    • 0031028204 scopus 로고    scopus 로고
    • Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo
    • Hankamer, B., Nield, J., Zheleva, D., Boekema, E., Jansson, S., and Barber, J. (1997). Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo. Eur. J. Biochem. 243, 422-429.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 422-429
    • Hankamer, B.1    Nield, J.2    Zheleva, D.3    Boekema, E.4    Jansson, S.5    Barber, J.6
  • 20
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II
    • Haußühl, K., Andersson, B., and 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
    • Haußühl, K.1    Andersson, B.2    Adamska, I.3
  • 21
    • 0035037364 scopus 로고    scopus 로고
    • DNA microarray analysis of cyanobacterial gene expression during acclimation to high light
    • Hihara, Y., Kamei, A., Kanehisa, M., Kaplan, A., and Ikeuchi, M. (2001). DNA microarray analysis of cyanobacterial gene expression during acclimation to high light. Plant Cell 13, 793-806.
    • (2001) Plant Cell , vol.13 , pp. 793-806
    • Hihara, Y.1    Kamei, A.2    Kanehisa, M.3    Kaplan, A.4    Ikeuchi, M.5
  • 22
    • 0035824790 scopus 로고    scopus 로고
    • A sequential two-step proteolytic process in the carboxyl-terminal truncation or precursor D1 protein in Synechocystis sp. PCC6803
    • Inagaki, N., Yamamoto, Y., and Satoh, K. (2001). A sequential two-step proteolytic process in the carboxyl-terminal truncation or precursor D1 protein in Synechocystis sp. PCC6803. FEBS Lett. 509, 197-201.
    • (2001) FEBS Lett. , vol.509 , pp. 197-201
    • Inagaki, N.1    Yamamoto, Y.2    Satoh, K.3
  • 23
    • 0031266743 scopus 로고    scopus 로고
    • Complete genome structure of the unicellular cyanobacterium Synechocystis sp. PCC6803
    • Kaneko, T., and Tabata, S. (1997). Complete genome structure of the unicellular cyanobacterium Synechocystis sp. PCC6803. Plant Cell Physiol. 38, 1171-1176.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1171-1176
    • Kaneko, T.1    Tabata, S.2
  • 24
    • 0031177711 scopus 로고    scopus 로고
    • Membrane lipid unsaturation modulates processing of the photosystem II reaction-center protein DS1 at low temperatures
    • Kanervo, E., Tasaka, Y., Murata, N., and Aro, E.-M. (1997). Membrane lipid unsaturation modulates processing of the photosystem II reaction-center protein DS1 at low temperatures. Plant Physiol. 114, 841-849.
    • (1997) Plant Physiol. , vol.114 , pp. 841-849
    • Kanervo, E.1    Tasaka, Y.2    Murata, N.3    Aro, E.-M.4
  • 25
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases: Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., Inagawa, T., Wilkinson, A.J., Tatsuta, T., and Ogura, T. (1999). Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases: Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274, 26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 26
    • 0141510346 scopus 로고    scopus 로고
    • Characterization of purified Histagged CP47-containing photosystem II complexes from a cyanobacterium, Synechocystis sp. PCC 6803
    • Melbourne, Australia: CSIRO Publishing
    • Kashino, Y., Lauber, W.M., Carroll, J.A., Wang, Q., Whitmarsh, J., Satoh, K., and Pakrasi, H.B. (2001). Characterization of purified Histagged CP47-containing photosystem II complexes from a cyanobacterium, Synechocystis sp. PCC 6803. In 12th International Congress of Photosynthesis. (Melbourne, Australia: CSIRO Publishing).
    • (2001) 12th International Congress of Photosynthesis
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 27
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • Kashino, Y., Lauber, W.M., Carroll, J.A., Wang, Q., Whitmarsh, J., Satoh, K., and Pakrasi, H.B. (2002). Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry 41, 8004-8012.
    • (2002) Biochemistry , vol.41 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 28
    • 0003018424 scopus 로고    scopus 로고
    • State transition and photoinhibition
    • J.-D. Rochaix, M.G. Clermont, and S. Merchant, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Keren, N., and Ohad, I. (1998). State transition and photoinhibition. In The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas, J.-D. Rochaix, M.G. Clermont, and S. Merchant, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 569-596.
    • (1998) The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas , pp. 569-596
    • Keren, N.1    Ohad, I.2
  • 29
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
    • Kihara, A., Akiyama, Y., and Ito, K. (1996). A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY. EMBO J. 15, 6122-6131.
    • (1996) EMBO J. , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 30
    • 0029088399 scopus 로고
    • B site and dependent on protein synthesis
    • B site and dependent on protein synthesis. Biochemistry 34, 9625-9631.
    • (1995) Biochemistry , vol.34 , pp. 9625-9631
    • Komenda, J.1    Barber, J.2
  • 31
    • 0034058872 scopus 로고    scopus 로고
    • Degradation of the photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript
    • Komenda, J., Hassan, H.A., Diner, B.A., Debus, R.J., Barber, J., and Nixon, P.J. (2000). Degradation of the photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript. Plant Mol. Biol. 42, 635-645.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 635-645
    • Komenda, J.1    Hassan, H.A.2    Diner, B.A.3    Debus, R.J.4    Barber, J.5    Nixon, P.J.6
  • 33
    • 0001449340 scopus 로고
    • Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes
    • Kyle, D.J., Ohad, I., and Arntzen, C.J. (1984). Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes. Proc. Natl. Acad. Sci. USA 81, 4070-4074.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 34
    • 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
  • 35
    • 0034031132 scopus 로고    scopus 로고
    • The thylakold FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl, M., Spetea, C., Hundal, T., Oppenheim, A.B., Adam, Z., and Andersson, B. (2000). The thylakold 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
  • 36
    • 0029799889 scopus 로고    scopus 로고
    • Identification, characterisation 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., and Adam, Z. (1996). Identification, characterisation 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
  • 38
    • 0034637466 scopus 로고    scopus 로고
    • Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium Synechocystis sp. PCC 6803
    • Mann, N., Novac, N., Mullineaux, C., Newman, J., Bailey S., and Robinson, C. (2000). Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 479, 72-77.
    • (2000) FEBS Lett. , vol.479 , pp. 72-77
    • Mann, N.1    Novac, N.2    Mullineaux, C.3    Newman, J.4    Bailey, S.5    Robinson, C.6
  • 39
    • 0028232687 scopus 로고
    • Destructive role of singlet oxygen during aerobic illumination of the photosystem II core complex
    • Mishra, N.P., Francke, C., van Gorkom, H.J., and Ghanotakis, D.F. (1994). Destructive role of singlet oxygen during aerobic illumination of the photosystem II core complex. Biochim. Biophys. Acta 1186, 81-90.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 81-90
    • Mishra, N.P.1    Francke, C.2    Van Gorkom, H.J.3    Ghanotakis, D.F.4
  • 40
    • 0029127671 scopus 로고
    • Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: Implications for the mechanism of degradation of the D1 protein under illumination
    • Miyao, M., Ikeuchi, M., Yamamoto, N., and Ono, T. (1995). Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: Implications for the mechanism of degradation of the D1 protein under illumination. Biochemistry 34, 10019-10026.
    • (1995) Biochemistry , vol.34 , pp. 10019-10026
    • Miyao, M.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.4
  • 41
    • 0141621593 scopus 로고
    • A Synechocystis PCC 6803 psbA deletion mutant and its transformation with a psbA gene from a higher plant
    • M. Baltscheffsky, ed (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Nixon, P.J., Metz, J.G., Rögner, M., and Diner, B.A. (1990). A Synechocystis PCC 6803 psbA deletion mutant and its transformation with a psbA gene from a higher plant. In Current Research in Photosynthesis, Vol. 1, M. Baltscheffsky, ed (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 471-474.
    • (1990) Current Research in Photosynthesis , vol.1 , pp. 471-474
    • Nixon, P.J.1    Metz, J.G.2    Rögner, M.3    Diner, B.A.4
  • 42
    • 0345523771 scopus 로고    scopus 로고
    • Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    • Ogura, T., et al. (1999). Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol. Microbiol. 31, 833-844.
    • (1999) Mol. Microbiol. , vol.31 , pp. 833-844
    • Ogura, T.1
  • 44
    • 0003131973 scopus 로고
    • Light-induced degradation of the photosystem II reaction centre D1 protein in vivo: An integrative approach
    • N.R. Baker and J.R. Bowyer, eds (Oxford, UK: Bios Scientific Publishers)
    • Ohad, I., Keren, N., Zer, H., Gong, H., Mor, T.S., Gal, A., Tal, S., and Domovich, Y. (1994). Light-induced degradation of the photosystem II reaction centre D1 protein in vivo: An integrative approach. In Photoinhibition of Photosynthesis, N.R. Baker and J.R. Bowyer, eds (Oxford, UK: Bios Scientific Publishers), pp. 161-177.
    • (1994) Photoinhibition of Photosynthesis , pp. 161-177
    • Ohad, I.1    Keren, N.2    Zer, H.3    Gong, H.4    Mor, T.S.5    Gal, A.6    Tal, S.7    Domovich, Y.8
  • 45
    • 0141844925 scopus 로고
    • Membrane protein damage and repair: Removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes
    • Ohad, I., Kyle, D.J., and Arntzen, C.J. (1984). Membrane protein damage and repair: Removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes. J. Cell Biol. 270, 14919-14927.
    • (1984) J. Cell Biol. , vol.270 , pp. 14919-14927
    • Ohad, I.1    Kyle, D.J.2    Arntzen, C.J.3
  • 46
    • 0000226607 scopus 로고
    • Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes
    • J. Barber, ed (Amsterdam: Elsevier Science Publishers)
    • Prasil, O., Adir, N., and Ohad, I. (1992). Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes. In The Photosystems: Structure, Function and Molecular Biology, J. Barber, ed (Amsterdam: Elsevier Science Publishers), pp. 295-348.
    • (1992) The Photosystems: Structure, Function and Molecular Biology , pp. 295-348
    • Prasil, O.1    Adir, N.2    Ohad, I.3
  • 47
    • 0141621594 scopus 로고    scopus 로고
    • Biochemical analysis of IMMUTANS, a potential plastoquinol oxidase of the thylakoid membrane
    • Melbourne, Australia: CSIRO Publishing
    • Prommeenate, P., Lennon, A.M., and Nixon, P.J. (2001). Biochemical analysis of IMMUTANS, a potential plastoquinol oxidase of the thylakoid membrane. In 12th International Congress of Photosynthesis. (Melbourne, Australia: CSIRO Publishing).
    • (2001) 12th International Congress of Photosynthesis
    • Prommeenate, P.1    Lennon, A.M.2    Nixon, P.J.3
  • 48
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction centre at 8Å resolution
    • Rhee, K.H., Morris, E.P., Barber, J., and Kühlbrandt, W. (1998). Three-dimensional structure of the plant photosystem II reaction centre at 8Å resolution. Nature 396, 283-286.
    • (1998) Nature , vol.396 , pp. 283-286
    • Rhee, K.H.1    Morris, E.P.2    Barber, J.3    Kühlbrandt, W.4
  • 49
    • 34250455512 scopus 로고
    • Photoheterotrophy and chemoheterotrophy among unicellular blue-green algae
    • Rippka, R. (1972). Photoheterotrophy and chemoheterotrophy among unicellular blue-green algae. Arch. Mikrobiol. 87, 93-98.
    • (1972) Arch. Mikrobiol. , vol.87 , pp. 93-98
    • Rippka, R.1
  • 50
    • 0025093577 scopus 로고
    • Mono-, di- and trimeric PSI reaction center complexes isolated from the thermophilic cyanobacterium Synechococcus sp.: Size, shape and activity
    • Rögner, M., Mühlenhoff, U., Boekema, E.J., and Witt, H.T. (1990). Mono-, di- and trimeric PSI reaction center complexes isolated from the thermophilic cyanobacterium Synechococcus sp.: Size, shape and activity. Biochim. Biophys. Acta 1015, 415-424.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 415-424
    • Rögner, M.1    Mühlenhoff, U.2    Boekema, E.J.3    Witt, H.T.4
  • 51
    • 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., and 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
  • 52
    • 0016627718 scopus 로고
    • Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12
    • Santos, D., and De Almeida, D.F. (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
  • 53
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W.A., and von Jagow, G. (1994). Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 54
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H., and von Jagow, G. (1991). Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 55
    • 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., and 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
  • 56
    • 0031468625 scopus 로고    scopus 로고
    • Primary structure characterization of the photosystem II D1 and D2 subunits
    • Sharma, J., Panico, M., Shipton, C.A., Nilsson, F., Morris, H.R., and Barber, J. (1997). Primary structure characterization of the photosystem II D1 and D2 subunits. J. Biol. Chem. 272, 33158-33166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33158-33166
    • Sharma, J.1    Panico, M.2    Shipton, C.A.3    Nilsson, F.4    Morris, H.R.5    Barber, J.6
  • 59
    • 0037195339 scopus 로고    scopus 로고
    • Involvement of the HtrA family of proteases in the protection of the cyanobacterium Synechocystis PCC 6803 from light stress and in the repair of photosystem II
    • Silva, P., Choi, Y.-J., Hassan, H.A.G., and Nixon, P.J. (2002). Involvement of the HtrA family of proteases in the protection of the cyanobacterium Synechocystis PCC 6803 from light stress and in the repair of photosystem II. Philos. Trans. R. Soc. Lond. B Biol. Sci. 357, 1461-1468.
    • (2002) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.357 , pp. 1461-1468
    • Silva, P.1    Choi, Y.-J.2    Hassan, H.A.G.3    Nixon, P.J.4
  • 60
    • 0141621595 scopus 로고    scopus 로고
    • Identification of possible assembly and repair factors in photosystem two preparations of Synechocystis sp. PCC 6803: A new model for D1 turnover
    • Melbourne, Australia: CSIRO Publishing
    • Silva, P., and Nixon, P.J. (2001). Identification of possible assembly and repair factors in photosystem two preparations of Synechocystis sp. PCC 6803: A new model for D1 turnover. In 12th International Congress of Photosynthesis. (Melbourne, Australia: CSIRO Publishing).
    • (2001) 12th International Congress of Photosynthesis
    • Silva, P.1    Nixon, P.J.2
  • 61
    • 0027219798 scopus 로고
    • The distribution of photosystem I and photosystem II polypeptides between the cytoplasmic and thylakoid membranes of cyanobacteria
    • Smith, D., and Howe, C.J. (1993). The distribution of photosystem I and photosystem II polypeptides between the cytoplasmic and thylakoid membranes of cyanobacteria. FEMS Microbiol. Lett. 110, 341-348.
    • (1993) FEMS Microbiol. Lett. , vol.110 , pp. 341-348
    • Smith, D.1    Howe, C.J.2
  • 62
    • 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, V.M., Herrmann, R.G., and Shestakov, S.V. (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
  • 63
    • 0032991536 scopus 로고    scopus 로고
    • GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein
    • Spetea, C., Hundal, T., Lohmann, F., and Andersson, B. (1999). GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein. Proc. Natl. Acad. Sci. USA 96, 6547-6552.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6547-6552
    • Spetea, C.1    Hundal, T.2    Lohmann, F.3    Andersson, B.4
  • 64
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich, G., Neupert, W., and Langer, T. (1999). Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol. Cell. Biol. 19, 3435-3442.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 65
    • 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., and 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
  • 66
    • 0029804115 scopus 로고    scopus 로고
    • Targeted mutagenesis of acyl-lipid desaturases in Synechocystis 6803: Evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis
    • Tasaka, Y., Gombos, Z., Nishiyama, Y., Mohanty, P., Ohba, T., Ohki, K., and Murata, N. (1996). Targeted mutagenesis of acyl-lipid desaturases in Synechocystis 6803: Evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis. EMBO J. 15, 6416-6425.
    • (1996) EMBO J. , vol.15 , pp. 6416-6425
    • Tasaka, Y.1    Gombos, Z.2    Nishiyama, Y.3    Mohanty, P.4    Ohba, T.5    Ohki, K.6    Murata, N.7
  • 67
    • 77957024978 scopus 로고
    • Construction of a specific mutation in photosystem II photosynthetic reaction center by genetic engineering methods in Synechocystis 6803
    • Williams, J.G.K. (1988). Construction of a specific mutation in photosystem II photosynthetic reaction center by genetic engineering methods in Synechocystis 6803. Methods Enzymol. 167, 766-778.
    • (1988) Methods Enzymol. , vol.167 , pp. 766-778
    • Williams, J.G.K.1
  • 68
    • 0035818524 scopus 로고    scopus 로고
    • The initial steps of biogenesis of cyanobacterial photosystems occur in plasma membranes
    • Zak, E., Norling, B., Maitra, R., Huang, F., Andersson, B., and Pakrasi, H.B. (2001). The initial steps of biogenesis of cyanobacterial photosystems occur in plasma membranes. Proc. Natl. Acad. Sci. USA 98, 13443-13448.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13443-13448
    • Zak, E.1    Norling, B.2    Maitra, R.3    Huang, F.4    Andersson, B.5    Pakrasi, H.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.