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Volumn 1797, Issue 8, 2010, Pages 1546-1554

Psb30 contributes to structurally stabilise the Photosystem II complex in the thermophilic cyanobacterium Thermosynechococcus elongatus

Author keywords

Cytochrome b559; Photosystem II; Psb30; Side path electron transfer; Small subunit; Thermosynechococcus elongatus; Trans membrane protein

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME B559; D1 PROTEIN; MUTANT PROTEIN; PROTEIN PSB30; UNCLASSIFIED DRUG;

EID: 77953812232     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.03.020     Document Type: Article
Times cited : (12)

References (52)
  • 2
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of Photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., Biesiadka J. Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of Photosystem II. Nature 2005, 438:1040-1044.
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 3
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial Photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride
    • Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W. Cyanobacterial Photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 2009, 16:334-342.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5    Saenger, W.6
  • 5
    • 66649106614 scopus 로고    scopus 로고
    • Location of chloride and its possible functions in oxygen evolving Photosystem II revealed by X-ray crystallography
    • Kawakami K., Umena Y., Kamiya N., Shen J.-R. Location of chloride and its possible functions in oxygen evolving Photosystem II revealed by X-ray crystallography. Proc. Natl Acad. Sci. USA 2009, 106:8567-8572.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8567-8572
    • Kawakami, K.1    Umena, Y.2    Kamiya, N.3    Shen, J.-R.4
  • 6
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of Photosystem II of oxygenic photosynthesis
    • Diner B.A., Rappaport F. Structure, dynamics, and energetics of the primary photochemistry of Photosystem II of oxygenic photosynthesis. Annu. Rev. Plant. Biol. 2002, 53:551-580.
    • (2002) Annu. Rev. Plant. Biol. , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 7
  • 8
    • 33144472069 scopus 로고    scopus 로고
    • Kinetics and mechanism of electron transfer in intact Photosystem II and in the isolated reaction center: pheophytin is the primary electron acceptor
    • Holzwarth A.R., Muller M.G., Reus M., Nowaczyk M., Sander J., Rogner M. Kinetics and mechanism of electron transfer in intact Photosystem II and in the isolated reaction center: pheophytin is the primary electron acceptor. Proc. Natl Acad. Sci. USA 2006, 103:6895-6900.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6895-6900
    • Holzwarth, A.R.1    Muller, M.G.2    Reus, M.3    Nowaczyk, M.4    Sander, J.5    Rogner, M.6
  • 12
    • 12444311793 scopus 로고    scopus 로고
    • PSII-Tc protein plays an important role in dimerization of Photosystem II
    • Iwai M., Katoh H., Katayama M., Ikeuchi M. PSII-Tc protein plays an important role in dimerization of Photosystem II. Plant Cell Physiol. 2004, 45:1809-1816.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1809-1816
    • Iwai, M.1    Katoh, H.2    Katayama, M.3    Ikeuchi, M.4
  • 13
    • 42449084991 scopus 로고    scopus 로고
    • X-ray crystallographic and biochemical characterizations of a mutant Photosystem II complex from Thermosynechococcus vulcanus with the psbTc gene inactivated by an insertion mutation
    • Henmi T., Iwai M., Ikeuchi M., Kawakami K., Shen J.-R., Kamiya N. X-ray crystallographic and biochemical characterizations of a mutant Photosystem II complex from Thermosynechococcus vulcanus with the psbTc gene inactivated by an insertion mutation. J. Synchrotron Radiat. 2008, 15:304-307.
    • (2008) J. Synchrotron Radiat. , vol.15 , pp. 304-307
    • Henmi, T.1    Iwai, M.2    Ikeuchi, M.3    Kawakami, K.4    Shen, J.-R.5    Kamiya, N.6
  • 14
    • 57849105843 scopus 로고    scopus 로고
    • Directed mutagenesis of the transmembrane domain of the PsbL subunit of Photosystem II in Synechocystis sp. PCC 6803
    • Luo H., Eaton-Rye J.J. Directed mutagenesis of the transmembrane domain of the PsbL subunit of Photosystem II in Synechocystis sp. PCC 6803. Photosynth. Res. 2008, 98:337-347.
    • (2008) Photosynth. Res. , vol.98 , pp. 337-347
    • Luo, H.1    Eaton-Rye, J.J.2
  • 15
    • 55249115772 scopus 로고    scopus 로고
    • Effects of inactivating psbM and psbT on photodamage and assembly of Photosystem II in Synechocystis sp. PCC 6803
    • Bentley F.K., Luo H., Dilbeck P., Burnap R.L., Eaton-Rye J.J. Effects of inactivating psbM and psbT on photodamage and assembly of Photosystem II in Synechocystis sp. PCC 6803. Biochemistry 2008, 47:11637-11646.
    • (2008) Biochemistry , vol.47 , pp. 11637-11646
    • Bentley, F.K.1    Luo, H.2    Dilbeck, P.3    Burnap, R.L.4    Eaton-Rye, J.J.5
  • 16
    • 0035081590 scopus 로고    scopus 로고
    • Targeted disruption of psbX and biochemical characterization of photosysytem II complex in the thermophilic cyanobacterium Synechococcus elongatus
    • Katoh H., Ikeuchi M. Targeted disruption of psbX and biochemical characterization of photosysytem II complex in the thermophilic cyanobacterium Synechococcus elongatus. Plant Cell Physiol. 2001, 42:179-188.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 179-188
    • Katoh, H.1    Ikeuchi, M.2
  • 17
    • 0033401728 scopus 로고    scopus 로고
    • Highly purified thermo-stable oxygen-evolving Photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43
    • Sugiura M., Inoue Y. Highly purified thermo-stable oxygen-evolving Photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43. Plant Cell Physiol. 1999, 40:1219-1231.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2
  • 20
    • 0242581701 scopus 로고    scopus 로고
    • Evidence that the PsbK polypeptide is associated with the Photosystem II core antenna complex CP43
    • Sugimoto I., Takahashi Y. Evidence that the PsbK polypeptide is associated with the Photosystem II core antenna complex CP43. J. Biol. Chem. 2003, 278:45004-45010.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45004-45010
    • Sugimoto, I.1    Takahashi, Y.2
  • 21
    • 0027396153 scopus 로고
    • Genetic and immunological analyses of the cyanobacterium Synechocystis sp. PCC 6803 show that the protein encoded by the psbJ gene regulates the number of Photosystem II centers in thylakoid membranes
    • Lind L.K., Shukla V.K., Nyhus K.J., Pakrasi H.B. Genetic and immunological analyses of the cyanobacterium Synechocystis sp. PCC 6803 show that the protein encoded by the psbJ gene regulates the number of Photosystem II centers in thylakoid membranes. J. Biol. Chem. 1993, 268:1575-1579.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1575-1579
    • Lind, L.K.1    Shukla, V.K.2    Nyhus, K.J.3    Pakrasi, H.B.4
  • 22
    • 37149048393 scopus 로고    scopus 로고
    • Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with the PSII complex in the thermophilic cyanobacterium Thermosynechococcus elongatus
    • Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M. Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with the PSII complex in the thermophilic cyanobacterium Thermosynechococcus elongatus. Plant Cell Physiol. 2007, 48:1758-1763.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 1758-1763
    • Iwai, M.1    Suzuki, T.2    Dohmae, N.3    Inoue, Y.4    Ikeuchi, M.5
  • 24
    • 1642580518 scopus 로고    scopus 로고
    • Protein assembly of Photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ
    • Suora M., Regel R.E., Paakkarinen V., Battchikova N., Herrmann R.G., Aro E.-M. Protein assembly of Photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ. Eur. J. Biochem. 2004, 271:96-107.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 96-107
    • Suora, M.1    Regel, R.E.2    Paakkarinen, V.3    Battchikova, N.4    Herrmann, R.G.5    Aro, E.-M.6
  • 25
    • 57849098696 scopus 로고    scopus 로고
    • Y, Kashino, Evidence for a stable association of Psb30 (Ycf12) with Photosystem II core complex in the cyanobacterium Synechocystis sp. PCC 6803
    • Inoue-Kashino N., Takahashi T., Ban A., Sugiura M., Takahashi Y., Satoh K. Y, Kashino, Evidence for a stable association of Psb30 (Ycf12) with Photosystem II core complex in the cyanobacterium Synechocystis sp. PCC 6803. Photosynth. Res. 2008, 98:323-335.
    • (2008) Photosynth. Res. , vol.98 , pp. 323-335
    • Inoue-Kashino, N.1    Takahashi, T.2    Ban, A.3    Sugiura, M.4    Takahashi, Y.5    Satoh, K.6
  • 26
    • 41249098659 scopus 로고    scopus 로고
    • Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P-680, of Photosystem II in Thermosynechococcus elongatus
    • Sugiura M., Boussac A., Noguchi T., Rappaport F. Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P-680, of Photosystem II in Thermosynechococcus elongatus. Biochim. Biophys. Acta 2008, 1777:341-342.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 341-342
    • Sugiura, M.1    Boussac, A.2    Noguchi, T.3    Rappaport, F.4
  • 28
    • 33947396788 scopus 로고    scopus 로고
    • Z* state of Photosystem II from Thermosynechococcus elongatus
    • Z* state of Photosystem II from Thermosynechococcus elongatus. Biochemistry 2007, 46:3138-3150.
    • (2007) Biochemistry , vol.46 , pp. 3138-3150
    • Un, S.1    Boussac, A.2    Sugiura, M.3
  • 30
    • 23144463393 scopus 로고    scopus 로고
    • Direct targeting of human plasma for matrix-assisted laser desorption/ionization and analysis of plasma proteins by time of flight-mass spectrometry
    • Jin Y., Manabe T. Direct targeting of human plasma for matrix-assisted laser desorption/ionization and analysis of plasma proteins by time of flight-mass spectrometry. Electrophoresis 2005, 26:2823-2834.
    • (2005) Electrophoresis , vol.26 , pp. 2823-2834
    • Jin, Y.1    Manabe, T.2
  • 31
    • 0026454816 scopus 로고
    • Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in Photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds
    • Berthomieu C., Boussac A., Mäntele W., Breton J., Nabedryk E. Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in Photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds. Biochemistry. 1992, 31:11460-11471.
    • (1992) Biochemistry. , vol.31 , pp. 11460-11471
    • Berthomieu, C.1    Boussac, A.2    Mäntele, W.3    Breton, J.4    Nabedryk, E.5
  • 32
    • 0037259956 scopus 로고    scopus 로고
    • Redox properties of the Photosystem II cytochrome b559 and c550 in the cyanobacterium Thermosynechococcus elongatus
    • Roncel M., Boussac A., Zurita J.L., Bottin H., Sugiura M., Kirilovsky D., Ortega J.M. Redox properties of the Photosystem II cytochrome b559 and c550 in the cyanobacterium Thermosynechococcus elongatus. J. Biol. Inorg. Chem. 2003, 8:206-216.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 206-216
    • Roncel, M.1    Boussac, A.2    Zurita, J.L.3    Bottin, H.4    Sugiura, M.5    Kirilovsky, D.6    Ortega, J.M.7
  • 33
    • 45149089916 scopus 로고    scopus 로고
    • Biosynthetic exchange of bromide for chloride and strontium for calcium in the Photosystem II oxygen-evolving enzyme of Thermosynechococcus elongatus
    • Ishida N., Sugiura M., Rappaport F., Lai T.-L., Rutherford A.W., Boussac A. Biosynthetic exchange of bromide for chloride and strontium for calcium in the Photosystem II oxygen-evolving enzyme of Thermosynechococcus elongatus. J. Biol. Chem. 2008, 283:1330-13340.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1330-13340
    • Ishida, N.1    Sugiura, M.2    Rappaport, F.3    Lai, T.-L.4    Rutherford, A.W.5    Boussac, A.6
  • 34
    • 34250332693 scopus 로고    scopus 로고
    • Influence of the redox potential of the primary quinone electron acceptor on photoinhibition in Photosystem II
    • Fufezan C., Gross C.M., Sjödin M., Rutherford A.W., Krieger-Liszkay A., Kirilovsky D. Influence of the redox potential of the primary quinone electron acceptor on photoinhibition in Photosystem II. J. Biol. Chem. 2007, 282:12492-12502.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12492-12502
    • Fufezan, C.1    Gross, C.M.2    Sjödin, M.3    Rutherford, A.W.4    Krieger-Liszkay, A.5    Kirilovsky, D.6
  • 35
    • 25444441462 scopus 로고    scopus 로고
    • Secondary quinone in Photosystem II of Thermosynechococcus elongatus: semiquinone-iron EPR signals and temperature dependence of electron transfer
    • Fufezan C., Zhang C., Krieger-Liszkay A., Rutherford A.W. Secondary quinone in Photosystem II of Thermosynechococcus elongatus: semiquinone-iron EPR signals and temperature dependence of electron transfer. Biochemistry 2005, 44:12780-12789.
    • (2005) Biochemistry , vol.44 , pp. 12780-12789
    • Fufezan, C.1    Zhang, C.2    Krieger-Liszkay, A.3    Rutherford, A.W.4
  • 40
    • 0000883295 scopus 로고    scopus 로고
    • Low-temperature optical and resonance Raman spectra of a carotenoid cation radical in Photosystem II
    • Vrettos J.S., Stewart D.H., de Paula J.C., Brudvig G.W. Low-temperature optical and resonance Raman spectra of a carotenoid cation radical in Photosystem II. J. Phys. Chem. 1999, 103:6403-6406.
    • (1999) J. Phys. Chem. , vol.103 , pp. 6403-6406
    • Vrettos, J.S.1    Stewart, D.H.2    de Paula, J.C.3    Brudvig, G.W.4
  • 41
    • 0035830370 scopus 로고    scopus 로고
    • Characterization of carotenoid and chlorophyll photooxidation in Photosystem II
    • Tracewell C.A., Cua A., Stewart D.H., Bocian D.F., Brudvig G.W. Characterization of carotenoid and chlorophyll photooxidation in Photosystem II. Biochemistry 2001, 40:193-203.
    • (2001) Biochemistry , vol.40 , pp. 193-203
    • Tracewell, C.A.1    Cua, A.2    Stewart, D.H.3    Bocian, D.F.4    Brudvig, G.W.5
  • 42
    • 55249086054 scopus 로고    scopus 로고
    • Multiple redox-active chlorophylls in thesecondary electron-tranfer pathways of oxygen-evolving Photosystem II
    • Tracewell C.A., Brudvig G.W. Multiple redox-active chlorophylls in thesecondary electron-tranfer pathways of oxygen-evolving Photosystem II. Biochemistry 2008, 47:11559-11572.
    • (2008) Biochemistry , vol.47 , pp. 11559-11572
    • Tracewell, C.A.1    Brudvig, G.W.2
  • 43
    • 0024280216 scopus 로고
    • Cytochrome b-559 may function to protect Photosystem II from photoinhibition
    • Thompson L.K., Brudvig G.W. Cytochrome b-559 may function to protect Photosystem II from photoinhibition. Biochemistry 1988, 27:6653-6658.
    • (1988) Biochemistry , vol.27 , pp. 6653-6658
    • Thompson, L.K.1    Brudvig, G.W.2
  • 44
    • 0035967507 scopus 로고    scopus 로고
    • SS-Carotene redox reactions in Photosystem II: electron transfer pathway
    • Faller P., Pascal A., Rutherford A.W. ß-Carotene redox reactions in Photosystem II: electron transfer pathway. Biochemistry 2001, 40:6431-6440.
    • (2001) Biochemistry , vol.40 , pp. 6431-6440
    • Faller, P.1    Pascal, A.2    Rutherford, A.W.3
  • 45
    • 0000263207 scopus 로고    scopus 로고
    • A new model of cytochrome b559 function based on the observation of a reversible redox-linked interconversion between two redox forms of chytochrome b559, in G. Garab (ed) Photosynthesis Mechanism and Effects. Kluwer Academic Publisheres, Dordrecht, The Netherlands
    • D.H. Stewart, G.W. Brudvig, A new model of cytochrome b559 function based on the observation of a reversible redox-linked interconversion between two redox forms of chytochrome b559, in G. Garab (ed) Photosynthesis Mechanism and Effects, vol 2. Kluwer Academic Publisheres, Dordrecht, The Netherlands, pp 1113-1116.
    • Stewart, D.H.1    Brudvig, G.W.2
  • 49
    • 57849100600 scopus 로고    scopus 로고
    • Characterization of the secondary electron-transfer pathway intermediates of Photosystem II containing low-potential cytochrome b559
    • Tracewell C.A., Brudvig G.W. Characterization of the secondary electron-transfer pathway intermediates of Photosystem II containing low-potential cytochrome b559. Photosynth. Res. 2008, 98:189-197.
    • (2008) Photosynth. Res. , vol.98 , pp. 189-197
    • Tracewell, C.A.1    Brudvig, G.W.2
  • 50
    • 37549052159 scopus 로고    scopus 로고
    • Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1
    • Kós P.B., Deák Z., Cheregi O., Vass I. Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1. Biochim. Biophys. Acta 2008, 1777:74-83.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 74-83
    • Kós, P.B.1    Deák, Z.2    Cheregi, O.3    Vass, I.4
  • 51
    • 45749102065 scopus 로고    scopus 로고
    • Modeling of variant copies of subunit D1 in the structure of Photosystem II from Thermosynechococcus elongatus
    • Loll B., Broser M., Kós P.B., Kern J., Biesiadka J., Vass I., Saenger W., Zouni A. Modeling of variant copies of subunit D1 in the structure of Photosystem II from Thermosynechococcus elongatus. Biol. Chem. 2008, 389:609-617.
    • (2008) Biol. Chem. , vol.389 , pp. 609-617
    • Loll, B.1    Broser, M.2    Kós, P.B.3    Kern, J.4    Biesiadka, J.5    Vass, I.6    Saenger, W.7    Zouni, A.8
  • 52
    • 0024282920 scopus 로고
    • Genome rearrangement and nitrogen fixation in Anabaena blocked by inactivation of xisA gene
    • Golden J.W., Wiest D.R. Genome rearrangement and nitrogen fixation in Anabaena blocked by inactivation of xisA gene. Science 1988, 242:1421-1423.
    • (1988) Science , vol.242 , pp. 1421-1423
    • Golden, J.W.1    Wiest, D.R.2


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