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Volumn 1607, Issue 2-3, 2003, Pages 131-140

Dissecting a cyanobacterial proteolytic system: Efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants

Author keywords

Cyanobacterium; D1 protein; DegP; FtsH; Photosystem II; Synechocystis 6803

Indexed keywords

ANTIBODY; CARBON; FATTY ACID; PROTEIN; PROTEIN D1; PROTEINASE; UNCLASSIFIED DRUG;

EID: 0345059200     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.09.007     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0033045606 scopus 로고    scopus 로고
    • ATP-dependent Clp-proteases in photosynthetic organisms: A cut above the rest!
    • Clarke A.K. ATP-dependent Clp-proteases in photosynthetic organisms: a cut above the rest! Ann. Bot. 83:1999;593-599.
    • (1999) Ann. Bot. , vol.83 , pp. 593-599
    • Clarke, A.K.1
  • 2
    • 0003955248 scopus 로고    scopus 로고
    • Chloroplast proteases and their role in photosynthesis regulation
    • E.-M. Aro, & B. Andersson. Netherlands: Kluwer Academic Publishers
    • Adam Z. Chloroplast proteases and their role in photosynthesis regulation. Aro E.-M., Andersson B. Regulation of Photosynthesis. 2001;265-276 Kluwer Academic Publishers, Netherlands.
    • (2001) Regulation of Photosynthesis , pp. 265-276
    • Adam, Z.1
  • 3
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of chloroplast proteolysis
    • Adam Z., Clarke A.K. Cutting edge of chloroplast proteolysis. Trends Plant Sci. 7:2002;451-456.
    • (2002) Trends Plant Sci. , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 4
    • 0000040282 scopus 로고    scopus 로고
    • Photodamage and D1 protein turnover in Photosystem II
    • E.-M. Aro, & B. Andersson. Netherlands: Kluwer Academic Publishers
    • Andersson B., Aro E.-M. Photodamage and D1 protein turnover in Photosystem II. Aro E.-M., Andersson B. Regulation of Photosynthesis. 2001;377-393 Kluwer Academic Publishers, Netherlands.
    • (2001) Regulation of Photosynthesis , pp. 377-393
    • Andersson, B.1    Aro, E.-M.2
  • 5
    • 0030767058 scopus 로고    scopus 로고
    • Proteolytic activities and proteases of plant chloroplasts
    • Andersson B., Aro E.-M. Proteolytic activities and proteases of plant chloroplasts. Physiol. Plant. 100:1997;780-793.
    • (1997) Physiol. Plant. , vol.100 , pp. 780-793
    • Andersson, B.1    Aro, E.-M.2
  • 6
    • 0001449340 scopus 로고
    • Membrane protein damage and repair; Selective loss of a quinone protein function in chloroplast membranes
    • Kyle D.J., Ohad I., Arntzen C.J. Membrane protein damage and repair; selective loss of a quinone protein function in chloroplast membranes. Proc. Natl. Acad. Sci. U. S. A. 81:1984;4070-4074.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 7
    • 0001294420 scopus 로고
    • Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes
    • Mattoo A.K., Hoffman-Falk H., Marder J.B., Edelman M. Regulation of protein metabolism: coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes. Proc. Natl. Acad. Sci. U. S. A. 81:1984;1380-1384.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffman-Falk, H.2    Marder, J.B.3    Edelman, M.4
  • 8
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II inactivation, protein damage and turnover
    • Aro E.-M., Virgin I., Andersson B. Photoinhibition of photosystem II inactivation, protein damage and turnover. Biochim. Biophys. Acta. 1143:1993;113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 9
    • 0023429786 scopus 로고
    • Identification of a primary in vivo degradation product of the rapidly turning-over 32 kDa protein of photosystem II
    • Greenberg B.M., Gaba V., Mattoo A.K., Edelman M. Identification of a primary in vivo degradation product of the rapidly turning-over 32 kDa protein of photosystem II. EMBO J. 6:1987;2865-2869.
    • (1987) EMBO J. , vol.6 , pp. 2865-2869
    • Greenberg, B.M.1    Gaba, V.2    Mattoo, A.K.3    Edelman, M.4
  • 10
    • 0027325215 scopus 로고
    • Detection of a 10 kDa break-down product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism
    • Canovas P.M., Barber J. Detection of a 10 kDa break-down product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism. FEBS Lett. 324:1993;341-344.
    • (1993) FEBS Lett. , vol.324 , pp. 341-344
    • Canovas, P.M.1    Barber, J.2
  • 11
    • 0031712075 scopus 로고    scopus 로고
    • Massive breakdown of the Photosystem II polypeptides in a mutant of the cyanobacterium Synechocystis sp. PCC 6803
    • Kanervo E., Murata N., Aro E.-M. Massive breakdown of the Photosystem II polypeptides in a mutant of the cyanobacterium Synechocystis sp. PCC 6803. Photosynth. Res. 57:1998;81-91.
    • (1998) Photosynth. Res. , vol.57 , pp. 81-91
    • Kanervo, E.1    Murata, N.2    Aro, E.-M.3
  • 12
    • 0034786494 scopus 로고    scopus 로고
    • Engineering of the protein environment around the redox-active TyrZ in photosystem II
    • Wiklund R., Salih G., Mäenpää P., Jansson C. Engineering of the protein environment around the redox-active TyrZ in photosystem II. Eur. J. Biochem. 268:2001;5356-5364.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5356-5364
    • Wiklund, R.1    Salih, G.2    Mäenpää, P.3    Jansson, C.4
  • 13
    • 0025719094 scopus 로고
    • Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: Identification and localization of the C-terminal degradation products
    • Barbato R., Friso G., Giardi M.T., Rigoni F., Giacometti G.M. Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products. Biochemistry. 30:1991;10220-10226.
    • (1991) Biochemistry , vol.30 , pp. 10220-10226
    • Barbato, R.1    Friso, G.2    Giardi, M.T.3    Rigoni, F.4    Giacometti, G.M.5
  • 14
    • 0026597716 scopus 로고
    • Two sites of primary degradation of the D1 protein induced by acceptor or donor side photoinhibition in photosystem II core complexes
    • De Las Rivas J., Andersson B., Barber J. Two sites of primary degradation of the D1 protein induced by acceptor or donor side photoinhibition in photosystem II core complexes. FEBS Lett. 301:1992;246-252.
    • (1992) FEBS Lett. , vol.301 , pp. 246-252
    • De Las Rivas, J.1    Andersson, B.2    Barber, J.3
  • 15
    • 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., Andersson B. GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein. Proc. Natl. Acad. Sci. U. S. A. 96:1999;6547-6552.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6547-6552
    • Spetea, C.1    Hundal, T.2    Lohmann, F.3    Andersson, B.4
  • 16
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photo-damaged D1 protein in plant photosystem II
    • Haussuhl K., Andersson B., Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photo-damaged D1 protein in plant photosystem II. EMBO J. 20:2001;713-722.
    • (2001) EMBO J. , vol.20 , pp. 713-722
    • Haussuhl, K.1    Andersson, B.2    Adamska, I.3
  • 17
    • 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 A.B., Adam Z., Andersson B. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell. 12:2000;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
  • 19
    • 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., Mann N.H. A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the Photosystem II repair cycle in vivo. J. Biol. Chem. 277:2002;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
  • 20
    • 0037015689 scopus 로고    scopus 로고
    • Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer
    • Georgakopoulos J.H., Sokolenko A., Arkas M., Sofou G., Herrmann R.G., Argyroudi-Akoyunoglou J.H. Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer. Biochim. Biophys. Acta. 1556:2002;53-64.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 53-64
    • Georgakopoulos, J.H.1    Sokolenko, A.2    Arkas, M.3    Sofou, G.4    Herrmann, R.G.5    Argyroudi-Akoyunoglou, J.H.6
  • 21
    • 0000288410 scopus 로고
    • Synechocystis PCC 6803 mutants defective in desaturation of fatty acids
    • Wada H., Murata N. Synechocystis PCC 6803 mutants defective in desaturation of fatty acids. Plant Cell Physiol. 30:1989;971-978.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 971-978
    • Wada, H.1    Murata, N.2
  • 22
    • 0000165790 scopus 로고
    • Genetic manipulation of the extent of desaturation of fatty acids in membrane lipids in the cyanobacterium Synechocystis PCC 6803
    • Wada H., Gombos Z., Sakamoto T., Murata N. Genetic manipulation of the extent of desaturation of fatty acids in membrane lipids in the cyanobacterium Synechocystis PCC 6803. Plant Cell Physiol. 33:1992;535-540.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 535-540
    • Wada, H.1    Gombos, Z.2    Sakamoto, T.3    Murata, N.4
  • 23
    • 0028933939 scopus 로고
    • Low unsaturation level of thylakoid membrane lipids limits turnover of the D1 protein of photosystem II at high irradiance
    • Kanervo E., Aro E.-M., Murata N. Low unsaturation level of thylakoid membrane lipids limits turnover of the D1 protein of photosystem II at high irradiance. FEBS Lett. 364:1995;239-242.
    • (1995) FEBS Lett. , vol.364 , pp. 239-242
    • Kanervo, E.1    Aro, E.-M.2    Murata, N.3
  • 24
    • 0026687943 scopus 로고
    • Unsaturation of fatty acids in membrane lipids enhances tolerance of the cyanobacterium Synechocystis PCC 6803 to low-temperature photoinhibition
    • Gombos Z., Wada H., Murata N. Unsaturation of fatty acids in membrane lipids enhances tolerance of the cyanobacterium Synechocystis PCC 6803 to low-temperature photoinhibition. Proc. Natl. Acad. Sci. U. S. A. 89:1992;9959-9963.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9959-9963
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 25
    • 0002872106 scopus 로고
    • Oxygen evolving membranes and particles from the transformable cyanobacterium Synechocystis PCC 6803
    • Burnap R., Koike H., Sotiropoulou G., Sherman L.A., Inoue Y. Oxygen evolving membranes and particles from the transformable cyanobacterium Synechocystis PCC 6803. Photosynth. Res. 22:1989;123-130.
    • (1989) Photosynth. Res. , vol.22 , pp. 123-130
    • Burnap, R.1    Koike, H.2    Sotiropoulou, G.3    Sherman, L.A.4    Inoue, Y.5
  • 26
    • 0033034478 scopus 로고    scopus 로고
    • Isolation of a highly active PSII-LHCII supercomplex from thylakoid membranes by a direct method
    • Eshaghi S., Andersson B., Barber J. Isolation of a highly active PSII-LHCII supercomplex from thylakoid membranes by a direct method. FEBS Lett. 446:1999;23-26.
    • (1999) FEBS Lett. , vol.446 , pp. 23-26
    • Eshaghi, S.1    Andersson, B.2    Barber, J.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1979;680-685.
    • (1979) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 29
    • 0025298292 scopus 로고
    • Structure of donor side components of Photosystem II predicted by computer modelling
    • Svensson B., Vass I., Cedergren E., Styring S. Structure of donor side components of Photosystem II predicted by computer modelling. EMBO J. 9:1990;2051-2059.
    • (1990) EMBO J. , vol.9 , pp. 2051-2059
    • Svensson, B.1    Vass, I.2    Cedergren, E.3    Styring, S.4
  • 30
    • 0025899668 scopus 로고
    • New evidence suggests that the initial photoinduced cleavage of the D1 protein may not occur near the PEST sequence
    • Barbato R., Shipton C.A., Giacometti G.M., Barber J. New evidence suggests that the initial photoinduced cleavage of the D1 protein may not occur near the PEST sequence. FEBS Lett. 290:1991;162-166.
    • (1991) FEBS Lett. , vol.290 , pp. 162-166
    • Barbato, R.1    Shipton, C.A.2    Giacometti, G.M.3    Barber, J.4
  • 31
    • 0026043886 scopus 로고
    • Photoinduced degradation of the D1 polypeptide in isolated reaction centers of Photosystem II: Evidence for an autoproteolytic process triggered by the oxidising side
    • Shipton C.A., Barber J. Photoinduced degradation of the D1 polypeptide in isolated reaction centers of Photosystem II: evidence for an autoproteolytic process triggered by the oxidising side. Proc. Natl. Acad. Sci. U. S. A. 88:1991;6691-6695.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 6691-6695
    • Shipton, C.A.1    Barber, J.2
  • 32
    • 0001535840 scopus 로고    scopus 로고
    • Mechanisms of photodamage and protein degradation during photoinhibition of Photosystem II
    • N.R. Baker. Dordrecht: Kluwer Academic Publishers
    • Andersson B., Barber J. Mechanisms of photodamage and protein degradation during photoinhibition of Photosystem II. Baker N.R. Photosynthesis and the Environment. 1996;101-121 Kluwer Academic Publishers, Dordrecht.
    • (1996) Photosynthesis and the Environment , pp. 101-121
    • Andersson, B.1    Barber, J.2
  • 33
    • 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., Shestakov S.V. The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts. Curr. Genet. 41:2002;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
  • 34
    • 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. Identification and characterization of DegP, a serine protease associated with the luminal side of the thylakoid membrane. J. Biol. Chem. 273:1998;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
  • 35
    • 0036800801 scopus 로고    scopus 로고
    • Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis
    • Chassin Y., Kapri-Pardes E., Sinvany G., Arad T., Adam Z. Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis. Plant Physiol. 130:2002;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
  • 36
    • 0035985049 scopus 로고    scopus 로고
    • The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site
    • Shimohata N., Chiba S., Saikawa N., Ito K., Akiyama Y. The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site. Genes Cells. 7:2002;653-662.
    • (2002) Genes Cells , vol.7 , pp. 653-662
    • Shimohata, N.1    Chiba, S.2    Saikawa, N.3    Ito, K.4    Akiyama, Y.5
  • 37
    • 0035823557 scopus 로고    scopus 로고
    • Identification and characterization of SppA, a novel light-inducible chloroplast protease complex associated with thylakoid membranes
    • Lensch M., Herrmann R.G., Sokolenko A. Identification and characterization of SppA, a novel light-inducible chloroplast protease complex associated with thylakoid membranes. J. Biol. Chem. 276:2001;33645-33651.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33645-33651
    • Lensch, M.1    Herrmann, R.G.2    Sokolenko, A.3
  • 38
    • 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., Pakrasi H.B. Proteomic analysis of a highly active Photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry. 41:2002;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
  • 39
    • 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., Ito K. 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. 15:1996;6122-6131.
    • (1996) EMBO J. , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 40
    • 0028928968 scopus 로고
    • Prohibitin, an antiproliferative protein, is localized to mitochondria
    • Ikonen E., Fiedler K., Parton R., Simmons K. Prohibitin, an antiproliferative protein, is localized to mitochondria. FEBS Lett. 358:1995;273-277.
    • (1995) FEBS Lett. , vol.358 , pp. 273-277
    • Ikonen, E.1    Fiedler, K.2    Parton, R.3    Simmons, K.4
  • 41
    • 0032577263 scopus 로고    scopus 로고
    • Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: An implication from the interference by a mutant form of a new substrate protein, YccA
    • Kihara A., Akiyama Y., Ito K. Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA. J. Mol. Biol. 279:1998;175-188.
    • (1998) J. Mol. Biol. , vol.279 , pp. 175-188
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 42
    • 0035715212 scopus 로고    scopus 로고
    • Escherichia coli FtsH (HflB) degrades a membrane-associated TolAI-II-β-lactamase fusion protein under highly denaturing conditions
    • Cooper K.W., Baneyx F. Escherichia coli FtsH (HflB) degrades a membrane-associated TolAI-II-β-lactamase fusion protein under highly denaturing conditions. Protein Expr. Purif. 21:2001;323-332.
    • (2001) Protein Expr. Purif. , vol.21 , pp. 323-332
    • Cooper, K.W.1    Baneyx, F.2


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