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Volumn 123, Issue 4, 2005, Pages 413-420

The family of Deg proteases in cyanobacteria and chloroplasts of higher plants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYSIS; GENES; PHOTOSYNTHESIS; PLANTS (BOTANY);

EID: 17444411552     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2005.00458.x     Document Type: Review
Times cited : (62)

References (45)
  • 2
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of chloroplast proteolysis
    • Adam Z, Clarke AK (2002) Cutting edge of chloroplast proteolysis. Trends Plant Sci 7: 451-456
    • (2002) Trends Plant Sci , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 3
    • 17444405305 scopus 로고    scopus 로고
    • FtsH proteases in chloroplasts and cyanobacteria
    • DOI: 10.1111/j.1399-3054.2004.00436.x
    • Adam Z, Zaltsman A, Sinvany-Villalobo G, Sakamoto W (2004) FtsH proteases in chloroplasts and cyanobacteria. Physiol Plant DOI: 10.1111/j.1399-3054.2004. 00436.x
    • (2004) Physiol Plant
    • Adam, Z.1    Zaltsman, A.2    Sinvany-Villalobo, G.3    Sakamoto, W.4
  • 4
    • 0000040282 scopus 로고    scopus 로고
    • Photodamage and D1 protein turnover in photosystem II
    • Aro EM, Andersson B (eds) Kluwer Academic Publishers, Dordrecht, Boston, London
    • Andersson B, Aro EM (2001) Photodamage and D1 protein turnover in photosystem II. In: Aro EM, Andersson B (eds) Advances in Photosynthesis and Respiration - Regulation of Photosynthesis, Vol. 11. Kluwer Academic Publishers, Dordrecht, Boston, London, pp 377-393
    • (2001) Advances in Photosynthesis and Respiration - Regulation of Photosynthesis , vol.11 , pp. 377-393
    • Andersson, B.1    Aro, E.M.2
  • 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
  • 6
    • 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 (2002) Expression and characterization of the thylakoid lumen protease DegP1 from Arabidopsis. 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
  • 7
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • Clausen T, Southan C, 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
  • 9
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G (2000) Predicting subcellular localization of proteins on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 10
    • 0035047106 scopus 로고    scopus 로고
    • Proteases and cellular regulation in plants
    • Estelle M (2001) Proteases and cellular regulation in plants. Curr Opin Plant Biol 3: 254-260
    • (2001) Curr Opin Plant Biol , vol.3 , pp. 254-260
    • Estelle, M.1
  • 11
    • 0033797930 scopus 로고    scopus 로고
    • Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations
    • Fulda S, Huang F, Nilsson F, Hagemann M, Norling B (2000) Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations. Eur J Biochem 267: 5900-5907
    • (2000) Eur J Biochem , vol.267 , pp. 5900-5907
    • Fulda, S.1    Huang, F.2    Nilsson, F.3    Hagemann, M.4    Norling, B.5
  • 12
    • 0011203683 scopus 로고    scopus 로고
    • Family of Deg/Htr proteases in the cyanobacterium Synechocystis sp. PCC6803: Investigations toward their expression and function
    • Larkum T, Critchley C (eds) CSIRO, Canberra
    • Funk C, Haussuhl K, Adamska I (2001) Family of Deg/Htr proteases in the cyanobacterium Synechocystis sp. PCC6803: investigations toward their expression and function. In: Larkum T, Critchley C (eds) PS2001 Proceedings of the 12th International Congress on Photosynthesis. CSIRO, Canberra, pp S8-042
    • (2001) PS2001 Proceedings of the 12th International Congress on Photosynthesis
    • Funk, C.1    Haussuhl, K.2    Adamska, I.3
  • 13
    • 0035783236 scopus 로고    scopus 로고
    • Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy
    • Hankamer B, Morris E, Nield J, Gerle C, Barber J (2001) Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy. J Struct Biol 135: 262-269
    • (2001) J Struct Biol , vol.135 , pp. 262-269
    • Hankamer, B.1    Morris, E.2    Nield, J.3    Gerle, C.4    Barber, J.5
  • 14
    • 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
  • 16
    • 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
  • 17
    • 0345059200 scopus 로고    scopus 로고
    • Dissecting a cyanobacterial proteolytic system: Efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants
    • Kanervo E, Spetea C, Nishiyama Y, Murata N, Andersson B, Aro EM (2003) Dissecting a cyanobacterial proteolytic system: efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants. Biochim Biophys Acta 1607: 131-140
    • (2003) Biochim Biophys Acta , vol.1607 , pp. 131-140
    • Kanervo, E.1    Spetea, C.2    Nishiyama, Y.3    Murata, N.4    Andersson, B.5    Aro, E.M.6
  • 18
    • 0242277339 scopus 로고    scopus 로고
    • The family of Deg/HtrA proteases: From Escherichia coli to Arabidopsis
    • Kieselbach T, Funk C (2003) The family of Deg/HtrA proteases: from Escherichia coli to Arabidopsis. Physiol Plant 119: 337-346
    • (2003) Physiol Plant , vol.119 , pp. 337-346
    • Kieselbach, T.1    Funk, C.2
  • 19
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416: 455-459
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 20
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M (2001) MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17: 1244-1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 22
    • 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
  • 23
    • 0036260673 scopus 로고    scopus 로고
    • Love it or leave it: Tough choices in protein quality control
    • Maurizi MR (2002) Love it or leave it: Tough choices in protein quality control. Nat Struct Biol 9: 410-412
    • (2002) Nat Struct Biol , vol.9 , pp. 410-412
    • Maurizi, M.R.1
  • 24
    • 0042473085 scopus 로고    scopus 로고
    • Degradation of the D1 protein of photosystem II under illumination in vivo: Two different pathways involving cleavage or intermolecular cross-linking
    • Mizusawa N, Tomo T, Satoh K, Miyao M (2003) Degradation of the D1 protein of photosystem II under illumination in vivo: two different pathways involving cleavage or intermolecular cross-linking. Biochemistry 42: 10 034-10 044
    • (2003) Biochemistry , vol.42 , pp. 10034-10044
    • Mizusawa, N.1    Tomo, T.2    Satoh, K.3    Miyao, M.4
  • 25
    • 0037394645 scopus 로고    scopus 로고
    • Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2
    • Nie GY, Hampton A, Li Y, Findlay JK, Salamonsen LA (2003) Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2. Biochem J 371: 39-48
    • (2003) Biochem J , vol.371 , pp. 39-48
    • Nie, G.Y.1    Hampton, A.2    Li, Y.3    Findlay, J.K.4    Salamonsen, L.A.5
  • 26
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic peptides and prediction of their cleavage sites. Prot Eng 10: 1-6
    • (1997) Prot Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 27
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 28
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen MJ, Wren BW (1997) The HtrA family of serine proteases. Mol Microbiol 26: 209-221
    • (1997) Mol Microbiol , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 30
    • 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
  • 32
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C (2001) PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24: 1-29
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 33
    • 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 YJ, Hassan HA, Nixon PJ (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 London B: Biol Sci 357: 1461-1487
    • (2002) Philos Trans R Soc London B: Biol Sci , vol.357 , pp. 1461-1487
    • Silva, P.1    Choi, Y.J.2    Hassan, H.A.3    Nixon, P.J.4
  • 35
    • 3543046184 scopus 로고    scopus 로고
    • Expression in multi-gene families: Analysis of chloroplast and mitochondrial proteases
    • Sinvany-Villalobo G, Davydov GBA, Ben-Ari G, Zaltsman A, Raskind A, Adam. Z (2004) Expression in multi-gene families: analysis of chloroplast and mitochondrial proteases. Plant Physiol 135: 1336-1345
    • (2004) Plant Physiol , vol.135 , pp. 1336-1345
    • Sinvany-Villalobo, G.1    Gba, D.2    Ben-Ari, G.3    Zaltsman, A.4    Raskind, A.5    Adam, Z.6
  • 36
    • 0026642331 scopus 로고
    • Occurrence of a photosystem II polypeptide in non-photosynthetic membranes of cyanobacteria
    • Smith D, Bendall DS, Howe CJ (1992) Occurrence of a photosystem II polypeptide in non-photosynthetic membranes of cyanobacteria. Mol Microbiol 6: 1821-1827
    • (1992) Mol Microbiol , vol.6 , pp. 1821-1827
    • Smith, D.1    Bendall, D.S.2    Howe, C.J.3
  • 37
    • 0036935397 scopus 로고    scopus 로고
    • The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC6803 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. PCC6803 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
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C, Beil A, Ehrmann M (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97: 339-347
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 39
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT (2003) OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113: 61-71
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 40
    • 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
  • 41
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T (2004) Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease. Cell 117: 483-494
    • (2004) Cell , vol.117 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 42
    • 0035083795 scopus 로고    scopus 로고
    • Quality control of photosystem II
    • Yamamoto Y (2001) Quality control of photosystem II. Plant Cell Physiol 42: 121-128
    • (2001) Plant Cell Physiol , vol.42 , pp. 121-128
    • Yamamoto, Y.1
  • 43
  • 44
    • 3042644567 scopus 로고    scopus 로고
    • Structural analysis of DegS, a stress sensor of the bacterial periplasm
    • Zeth K (2004) Structural analysis of DegS, a stress sensor of the bacterial periplasm. FEBS Lett 569: 351-358
    • (2004) FEBS Lett , vol.569 , pp. 351-358
    • Zeth, K.1
  • 45
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A, Witt HT, Kern J, Fromme P, Krauss N, Saenger W, Orth P (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409: 739-743
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7


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