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Volumn 1767, Issue 6, 2007, Pages 677-685

Insights into the function of PsbR protein in Arabidopsis thaliana

Author keywords

Arabidopsis; Photosynthesis; Photosystem II; PsbR; Thylakoid membrane

Indexed keywords

ALGAL PROTEIN; DNA; PROTEIN PSBR; UNCLASSIFIED DRUG;

EID: 34249869311     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.01.011     Document Type: Article
Times cited : (47)

References (37)
  • 2
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • Debus R.J. The manganese and calcium ions of photosynthetic oxygen evolution. Biochim. Biophys. Acta 1102 (1992) 269-352
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 3
    • 33745585779 scopus 로고    scopus 로고
    • Refinement of the structural model for the Photosystem II supercomplex of higher plants
    • Nield J., and Barber J. Refinement of the structural model for the Photosystem II supercomplex of higher plants. Biochim. Biophys. Acta 1757 (2006) 353-361
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 353-361
    • Nield, J.1    Barber, J.2
  • 4
    • 4043080672 scopus 로고    scopus 로고
    • Analysis of the structure of the PsbO protein and its implications
    • De Las Rivas J., and Barber J. Analysis of the structure of the PsbO protein and its implications. Photosynth. Res. 81 (2004) 329-343
    • (2004) Photosynth. Res. , vol.81 , pp. 329-343
    • De Las Rivas, J.1    Barber, J.2
  • 5
    • 0001660407 scopus 로고
    • Identification of a new gene in the chloroplast genome encoding a low-molecular-mass polypeptide of photosystem II complexes
    • Murata N., Miyao M., Hayashida N., Hidaka T., and Sugiura M. Identification of a new gene in the chloroplast genome encoding a low-molecular-mass polypeptide of photosystem II complexes. FEBS Lett. 235 (1988) 283-288
    • (1988) FEBS Lett. , vol.235 , pp. 283-288
    • Murata, N.1    Miyao, M.2    Hayashida, N.3    Hidaka, T.4    Sugiura, M.5
  • 8
    • 0000981541 scopus 로고
    • Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted Photosystem II preparations
    • Ghanotakis D.F., Babcock G.T., and Yocum C.F. Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted Photosystem II preparations. FEBS Lett. 167 (1984) 127-130
    • (1984) FEBS Lett. , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 9
    • 0024398556 scopus 로고
    • The mode of binding of three extrinsic proteins of 33 kDa, 23 kDa and 18 kDa in the Photosystem II complex of spinach
    • Miyao M., and Murata N. The mode of binding of three extrinsic proteins of 33 kDa, 23 kDa and 18 kDa in the Photosystem II complex of spinach. Biochim. Biophys. Acta 977 (1989) 315-321
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 315-321
    • Miyao, M.1    Murata, N.2
  • 10
    • 0035808693 scopus 로고    scopus 로고
    • The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation
    • Ananyev G.M., Zaltsman L., Vasko C., and Dismukes G.C. The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation. Biochim. Biophys. Acta 1503 (2001) 52-68
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 52-68
    • Ananyev, G.M.1    Zaltsman, L.2    Vasko, C.3    Dismukes, G.C.4
  • 11
    • 0028980975 scopus 로고
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in Photosystem II from spinach
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in Photosystem II from spinach. Biochim. Biophys. Acta 1230 (1995) 155-164
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andŕeasson, L.-E.1    Vas, I.2    Styring, S.3
  • 12
    • 0032516020 scopus 로고    scopus 로고
    • Thermoluminescence measurements on chloride-depleted and calcium-depleted Photosystem II
    • Krieger A., Rutherford A.W., and Jegerschöld C. Thermoluminescence measurements on chloride-depleted and calcium-depleted Photosystem II. Biochim. Biophys. Acta 1364 (1998) 46-54
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 46-54
    • Krieger, A.1    Rutherford, A.W.2    Jegerschöld, C.3
  • 13
    • 0029124281 scopus 로고
    • Granal Photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium
    • McNamara V.P., and Gounaris K. Granal Photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium. Biochim. Biophys. Acta 1231 (1995) 289-296
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 289-296
    • McNamara, V.P.1    Gounaris, K.2
  • 14
    • 0342601459 scopus 로고    scopus 로고
    • Comparison of chloride-depleted and calcium depleted PSII: the midpoint potential of QA and susceptibility to photodamage
    • Krieger A., and Rutherford A.W. Comparison of chloride-depleted and calcium depleted PSII: the midpoint potential of QA and susceptibility to photodamage. Biochim. Biophys. Acta 1319 (1997) 91-98
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 91-98
    • Krieger, A.1    Rutherford, A.W.2
  • 15
    • 0029826533 scopus 로고    scopus 로고
    • Photoactivation and photoinhibition are competing in a mutant of Chlamydomonas reinhardtii lacking the 23-kDa extrinsic subunit of photosystem II
    • Rova E.M., Mc Ewen B., Fredriksson P.O., and Styring S. Photoactivation and photoinhibition are competing in a mutant of Chlamydomonas reinhardtii lacking the 23-kDa extrinsic subunit of photosystem II. J. Biol. Chem. 271 (1996) 28918-28924
    • (1996) J. Biol. Chem. , vol.271 , pp. 28918-28924
    • Rova, E.M.1    Mc Ewen, B.2    Fredriksson, P.O.3    Styring, S.4
  • 16
    • 20444394336 scopus 로고    scopus 로고
    • Function of the 23 kDa extrinsic protein of Photosystem II as a manganese binding protein and its role in photoactivation
    • Bondarava N., Beyer P., and Krieger-Liszkay A. Function of the 23 kDa extrinsic protein of Photosystem II as a manganese binding protein and its role in photoactivation. Biochim. Biophys. Acta 1708 (2005) 63-70
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 63-70
    • Bondarava, N.1    Beyer, P.2    Krieger-Liszkay, A.3
  • 17
    • 0025046737 scopus 로고
    • Anti-sense RNA efficiently inhibits formation of the 10 kd polypeptide of Photosystem II in transgenic potato plants: analysis of the role of the 10 kd protein
    • Stockhaus J., Hofer M., Renger G., Westhoff P., Wydrzynski T., and Willmitzer L. Anti-sense RNA efficiently inhibits formation of the 10 kd polypeptide of Photosystem II in transgenic potato plants: analysis of the role of the 10 kd protein. EMBO J. 9 (1990) 3013-3021
    • (1990) EMBO J. , vol.9 , pp. 3013-3021
    • Stockhaus, J.1    Hofer, M.2    Renger, G.3    Westhoff, P.4    Wydrzynski, T.5    Willmitzer, L.6
  • 19
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes
    • Berthold D.A., Babcock G.T., and Yocum C.F. A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. FEBS Lett. 134 (1981) 231-236
    • (1981) FEBS Lett. , vol.134 , pp. 231-236
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 20
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficient and simultaneous equations for assaying chlorophyll a and b with four different solvents: verification of the concentration of chlorophyll by atomic absorption spectroscopy
    • Porra R.J., Thompson W.A., and Kriedemann P.E. Determination of accurate extinction coefficient and simultaneous equations for assaying chlorophyll a and b with four different solvents: verification of the concentration of chlorophyll by atomic absorption spectroscopy. Biochim. Biophys. Acta 975 (1989) 384-394
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 21
    • 0034730066 scopus 로고    scopus 로고
    • Photosystem II in different parts of the thylakoid membrane: a functional comparison between different domains
    • Mamedov F., Stefansson H., Albetrtsson P.-A., and Styring S. Photosystem II in different parts of the thylakoid membrane: a functional comparison between different domains. Biochemistry 39 (2000) 10478-10486
    • (2000) Biochemistry , vol.39 , pp. 10478-10486
    • Mamedov, F.1    Stefansson, H.2    Albetrtsson, P.-A.3    Styring, S.4
  • 22
    • 0033613068 scopus 로고    scopus 로고
    • UV-B radiation-induced donor- and acceptor-side modifications of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803
    • Vass I., Kirilovsky D., and Etienne A.L. UV-B radiation-induced donor- and acceptor-side modifications of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803. Biochemistry 39 (1999) 12786-12794
    • (1999) Biochemistry , vol.39 , pp. 12786-12794
    • Vass, I.1    Kirilovsky, D.2    Etienne, A.L.3
  • 23
    • 78651153734 scopus 로고
    • Etude cinètique de la reaction photochimique libèrant l'oxygène au cours de la photosynthèse
    • Joliot A., and Joliot P. Etude cinètique de la reaction photochimique libèrant l'oxygène au cours de la photosynthèse. C.R. Acad. Sci. 258 (1964) 4622-4625
    • (1964) C.R. Acad. Sci. , vol.258 , pp. 4622-4625
    • Joliot, A.1    Joliot, P.2
  • 24
    • 0026604580 scopus 로고
    • Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation
    • Vass I., Styring S., Hundal T., Koivuniemi A., Aro EM., and Andersson B. Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 1408-1412
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1408-1412
    • Vass, I.1    Styring, S.2    Hundal, T.3    Koivuniemi, A.4    Aro, EM.5    Andersson, B.6
  • 25
    • 0026025417 scopus 로고
    • A guide to electron paramagnetic resonance spectroscopy of photosystem II membrane
    • Miller A.-F., and Brudvig G.W. A guide to electron paramagnetic resonance spectroscopy of photosystem II membrane. Biochim. Biophys. Acta 1056 (1991) 1-18
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 1-18
    • Miller, A.-F.1    Brudvig, G.W.2
  • 26
    • 21744452290 scopus 로고    scopus 로고
    • Interruption of the Calvin cycle inhibits the repair of Photosystem II from photodamage
    • Takahashi S., and Murata N. Interruption of the Calvin cycle inhibits the repair of Photosystem II from photodamage. Biochim. Biophys. Acta 1708 (2005) 352-361
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 352-361
    • Takahashi, S.1    Murata, N.2
  • 29
    • 0027489759 scopus 로고
    • A functional model for the role of cytochrome b559 in the protection against donor and acceptor side photoinhibition
    • Barber J., and De Las Rivas J. A functional model for the role of cytochrome b559 in the protection against donor and acceptor side photoinhibition. Proc. Natl. Acad. Sci. U. S. A. 23 (1993) 10942-10946
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.23 , pp. 10942-10946
    • Barber, J.1    De Las Rivas, J.2
  • 30
    • 0036438646 scopus 로고    scopus 로고
    • Influence of protein phosphorylation on the electron-transport properties of Photosystem II
    • Mamedov F., Rintamaki E., Aro E.M., Andersson B., and Styring S. Influence of protein phosphorylation on the electron-transport properties of Photosystem II. Photosynth. Res. 74 (2002) 61-72
    • (2002) Photosynth. Res. , vol.74 , pp. 61-72
    • Mamedov, F.1    Rintamaki, E.2    Aro, E.M.3    Andersson, B.4    Styring, S.5
  • 31
    • 0000400911 scopus 로고
    • Effect of salts and electron transport on the conformation of isolated chloroplasts. II. Electron microscopy
    • Izawa S., and Good N.E. Effect of salts and electron transport on the conformation of isolated chloroplasts. II. Electron microscopy. Plant Physiol. 41 (1966) 544-552
    • (1966) Plant Physiol. , vol.41 , pp. 544-552
    • Izawa, S.1    Good, N.E.2
  • 32
    • 0019273134 scopus 로고
    • Membrane surface charges and potentials in relation to photosynthesis
    • Barber J. Membrane surface charges and potentials in relation to photosynthesis. Biochim. Biophys. Acta 594 (1982) 253-308
    • (1982) Biochim. Biophys. Acta , vol.594 , pp. 253-308
    • Barber, J.1
  • 33
    • 0014686888 scopus 로고
    • Control of excitation transfer in photosynthesis. II. Magnesium ion-dependent distribution of excitation energy between two pigment systems in spinach chloroplasts
    • Murata N. Control of excitation transfer in photosynthesis. II. Magnesium ion-dependent distribution of excitation energy between two pigment systems in spinach chloroplasts. Biochim. Biophys. Acta 189 (1969) 171-181
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 171-181
    • Murata, N.1
  • 34
    • 0026569892 scopus 로고
    • Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster
    • Nixon P.J., and Diner B.A. Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster. Biochemistry 31 (1992) 942-948
    • (1992) Biochemistry , vol.31 , pp. 942-948
    • Nixon, P.J.1    Diner, B.A.2
  • 35
    • 0026741309 scopus 로고
    • Evidence from directed mutagenesis that aspartate 170 of the D1 polypeptide influences the assembly and/or stability of the manganese cluster in the photosynthetic water-splitting complex
    • Boerner R.J., Nguyen A.P., Barry B.A., and Debus R.J. Evidence from directed mutagenesis that aspartate 170 of the D1 polypeptide influences the assembly and/or stability of the manganese cluster in the photosynthetic water-splitting complex. Biochemistry 29 (1992) 60-72
    • (1992) Biochemistry , vol.29 , pp. 60-72
    • Boerner, R.J.1    Nguyen, A.P.2    Barry, B.A.3    Debus, R.J.4
  • 36
    • 4544283273 scopus 로고    scopus 로고
    • The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803
    • Allahverdiyeva Y., Deak Z., Szilard A., Diner B.A., Nixon P., and Vass I. The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803. Eur. J. Biochem. 17 (2004) 3523-3532
    • (2004) Eur. J. Biochem. , vol.17 , pp. 3523-3532
    • Allahverdiyeva, Y.1    Deak, Z.2    Szilard, A.3    Diner, B.A.4    Nixon, P.5    Vass, I.6
  • 37
    • 1642559319 scopus 로고    scopus 로고
    • Quantification of photosystem I and II in different parts of the thylakoid membrane from spinach
    • Danielsson R., Albertsson P.A., Mamedov F., and Styring S. Quantification of photosystem I and II in different parts of the thylakoid membrane from spinach. Biochim. Biophys. Acta. 1608 (2004) 53-61
    • (2004) Biochim. Biophys. Acta. , vol.1608 , pp. 53-61
    • Danielsson, R.1    Albertsson, P.A.2    Mamedov, F.3    Styring, S.4


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