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Volumn 289, Issue 29, 2014, Pages 20150-20157

Cross-linking evidence for multiple interactions of the PsbP and PsbQ proteins in a higher plant photosystem II supercomplex

Author keywords

[No Author keywords available]

Indexed keywords

CROSSLINKING; MASS SPECTROMETRY;

EID: 84904488777     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.574822     Document Type: Article
Times cited : (45)

References (44)
  • 1
    • 57849146011 scopus 로고    scopus 로고
    • Photosystem II: The machinery of photosynthetic water splitting
    • DOI 10.1007/s11120-008-9345-7
    • Renger, G., and Renger, T. (2008) Photosystem II: The machinery of photosynthetic water splitting. Photosynth. Res. 98, 53-80 (Pubitemid 50289510)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 53-80
    • Renger, G.1    Renger, T.2
  • 2
    • 84878349958 scopus 로고    scopus 로고
    • Photosystem II: The reaction center of oxygenic photosynthesis
    • Vinyard, D. J., Ananyev, G. M., and Dismukes, G. C. (2013) Photosystem II: the reaction center of oxygenic photosynthesis. Annu. Rev. Biochem. 82, 577-606
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 577-606
    • Vinyard, D.J.1    Ananyev, G.M.2    Dismukes, G.C.3
  • 4
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Umena, Y., Kawakami, K., Shen, J.-R., and Kamiya, N. (2011) Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å. Nature 473, 55-60
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 5
    • 0027410134 scopus 로고
    • Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II
    • Shen, J.-R., and Inoue, Y. (1993) Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II. Biochemistry 32, 1825-1832 (Pubitemid 23066457)
    • (1993) Biochemistry , vol.32 , Issue.7 , pp. 1825-1832
    • Shen, J.-R.1    Inoue, Y.2
  • 6
    • 0032502005 scopus 로고    scopus 로고
    • Functional characterization of Synechocystis sp. PCC 6803 deltapsbU and deltapsbV mutants reveals important roles of cytochrome c-550 in cyanobacterial oxygen evolution
    • DOI 10.1021/bi971676i
    • Shen, J.-R., Qian, M., Inoue, Y., and Burnap, R. L. (1998) Functional characterization of Synechocystis sp. PCC 6803 delta psbU and delta psbV mutants reveals important roles of cytochrome c-550 in cyanobacterial oxygen evolution. Biochemistry 37, 1551-1558 (Pubitemid 28093670)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1551-1558
    • Shen, J.-R.1    Qian, M.2    Inoue, Y.3    Burnap, R.L.4
  • 7
    • 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
    • DOI 10.1021/bi026012+
    • 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. PCC6803 reveals the presence of novel polypeptides. Biochemistry 41, 8004-8012 (Pubitemid 34655167)
    • (2002) Biochemistry , vol.41 , Issue.25 , 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
  • 8
    • 4043148624 scopus 로고    scopus 로고
    • Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem II activity in the cyanobacterium Synechocystis 6803 W inside box sign
    • DOI 10.1105/tpc.104.023515
    • Thornton, L. E., Ohkawa, H., Roose, J. L., Kashino, Y., Keren, N., and Pakrasi, H. B. (2004) Homologs of Plant PsbP and PsbQ proteins are necessary for regulation of photosystem II activity in cyanobacterium Synechosistis 6803. Plant Cell 16, 2164-2175 (Pubitemid 39059735)
    • (2004) Plant Cell , vol.16 , Issue.8 , pp. 2164-2175
    • Thomton, L.E.1    Ohkawa, H.2    Roose, J.L.3    Kashino, Y.4    Keren, N.5    Pakrasi, H.B.6
  • 9
    • 0142057153 scopus 로고    scopus 로고
    • Extrinsic proteins of photosystem II: An intermediate member of the PsbQ protein family in red algal PS II
    • DOI 10.1046/j.1432-1033.2003.03810.x
    • Ohta, H., Suzuki, T., Ueno, M., Okumura, A., Yoshihara, S., Shen, J.-R., and Enami, I. (2003) Extrinsic proteins of photosystem II: an intermediate member of PsbQ protein family in red algal PS II. Eur. J. Biochem. 270, 4156-4163 (Pubitemid 37281634)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.20 , pp. 4156-4163
    • Ohta, H.1    Suzuki, T.2    Ueno, M.3    Okumura, A.4    Yoshihara, S.5    Shen, J.-R.6    Enami, I.7
  • 10
    • 77956508715 scopus 로고    scopus 로고
    • Binding and functional properties of five extrinsic proteins in oxygen-evolving photosystem II from a marine centric diatom, Chaetoceros gracilis
    • Nagao, R., Moriguchi, A., Tomo, T., Niikura, A., Nakajima, S., Suzuki, T., Okumura, A., Iwai, M., Shen, J.-R., Ikeuchi, M., and Enami, I. (2010) Binding and functional properties of five extrinsic proteins in oxygen-evolving photosystem II from a marine centric diatom, Chaetoceros gracilis. J. Biol. Chem. 285, 29191-29199
    • (2010) J. Biol. Chem. , vol.285 , pp. 29191-29199
    • Nagao, R.1    Moriguchi, A.2    Tomo, T.3    Niikura, A.4    Nakajima, S.5    Suzuki, T.6    Okumura, A.7    Iwai, M.8    Shen, J.-R.9    Ikeuchi, M.10    Enami, I.11
  • 11
    • 29144456629 scopus 로고    scopus 로고
    • Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine
    • DOI 10.1039/b506874f
    • De Las Rivas, J., and Roman, A. (2005) Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine. Photochem. Photobiol. Sci. 4, 1003-1010 (Pubitemid 41811363)
    • (2005) Photochemical and Photobiological Sciences , vol.4 , Issue.12 , pp. 1003-1010
    • De Las, R.J.1    Roman, A.2
  • 13
    • 2442543556 scopus 로고    scopus 로고
    • Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
    • DOI 10.1038/sj.embor.7400113
    • Ifuku, K., Nakatsu, T., Kato, H., and Sato, F. (2004) Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum. EMBO Rep. 5, 362-367 (Pubitemid 38618277)
    • (2004) EMBO Reports , vol.5 , Issue.4 , pp. 362-367
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 14
    • 21744439800 scopus 로고    scopus 로고
    • The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region
    • DOI 10.1016/j.jmb.2005.05.044, PII S0022283605005991
    • Balsera, M., Arellano, J. B., Revuelta, J. L., de las Rivas, J., and Hermoso, J. A. (2005) The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region. J. Mol. Biol. 350, 1051-1060 (Pubitemid 40943461)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 1051-1060
    • Balsera, M.1    Arellano, J.B.2    Revuelta, J.L.3    De Las, R.J.4    Hermoso, J.A.5
  • 16
    • 33745585779 scopus 로고    scopus 로고
    • Refinement of the structural model for the Photosystem II supercomplex of higher plants
    • DOI 10.1016/j.bbabio.2006.03.019, PII S0005272806000740
    • Nield, J., and Barber, J. (2006) Refinement of the structural model for the photosystem II supercomplex of higher plants. Biochim. Biophys. Acta 1757, 353-361 (Pubitemid 43993853)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 353-361
    • Nield, J.1    Barber, J.2
  • 17
    • 79958002353 scopus 로고    scopus 로고
    • Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex
    • Ifuku, K., Ido, K., and Sato, F. (2011) Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex. J. Photochem. Photobiol. B 104, 158-164
    • (2011) J. Photochem. Photobiol. B , vol.104 , pp. 158-164
    • Ifuku, K.1    Ido, K.2    Sato, F.3
  • 18
    • 67650080532 scopus 로고    scopus 로고
    • FTIR evidence that the PsbP extrinsic protein induces protein conformational changes around the oxygen-evolving Mn cluster in photosystem II
    • Tomita, M., Ifuku, K., and Sato, F., and Noguchi, T. (2009) FTIR evidence that the PsbP extrinsic protein induces protein conformational changes around the oxygen-evolving Mn cluster in photosystem II. Biochemistry 48, 6318-6325
    • (2009) Biochemistry , vol.48 , pp. 6318-6325
    • Tomita, M.1    Ifuku, K.2    Sato, F.3    Noguchi, T.4
  • 19
    • 84862170882 scopus 로고    scopus 로고
    • The PsbQ protein stabilizes the functional binding of the PsbP protein to photosystem II in higher plants
    • Kakiuchi, S., Uno, C., Ido, K., Nishimura, T., Noguchi, T., Ifuku, K., and Sato, F. (2012) The PsbQ protein stabilizes the functional binding of the PsbP protein to photosystem II in higher plants. Biochim. Biophys. Acta 1817, 1346-1351
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1346-1351
    • Kakiuchi, S.1    Uno, C.2    Ido, K.3    Nishimura, T.4    Noguchi, T.5    Ifuku, K.6    Sato, F.7
  • 20
    • 67649390983 scopus 로고    scopus 로고
    • Knockdown of the PsbP protein does not prevent assembly of the dimeric PSII core complex but impairs accumulation of photosystem II supercomplexes in tobacco
    • Ido, K., Ifuku, K., Yamamoto, Y., Ishihara, S., Murakami, A., Takabe, K., Miyake, C., and Sato, F. (2009) Knockdown of the PsbP protein does not prevent assembly of the dimeric PSII core complex but impairs accumulation of photosystem II supercomplexes in tobacco. Biochim. Biophys. Acta 1787, 873-881
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 873-881
    • Ido, K.1    Ifuku, K.2    Yamamoto, Y.3    Ishihara, S.4    Murakami, A.5    Takabe, K.6    Miyake, C.7    Sato, F.8
  • 23
    • 0035831298 scopus 로고    scopus 로고
    • Importance of the N-terminal sequence of the extrinsic 23 kDa polypeptide in Photosystem II in ion retention in oxygen evolution
    • DOI 10.1016/S0167-4838(01)00139-X, PII S016748380100139X
    • Ifuku, K., and Sato, F. (2001) Importance of the N-terminal sequence of the extrinsic 23 kDa polypeptide in photosystem II in ion-retention in oxygenevolution. Biochim. Biophys. Acta 1546, 196-204 (Pubitemid 32217816)
    • (2001) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1546 , Issue.1 , pp. 196-204
    • Ifuku, K.1    Sato, F.2
  • 24
    • 63049105321 scopus 로고    scopus 로고
    • Mass Matrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H., and Freitas, M. A. (2009) Mass Matrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9, 1548-1555
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 25
    • 77954356041 scopus 로고    scopus 로고
    • Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry
    • Xu, H., Hsu, P. H., Zhang, L., Tsai, M. D., and Freitas, M. A. (2010) Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry, J. Proteome Res. 9, 3384-3393
    • (2010) J. Proteome Res. , vol.9 , pp. 3384-3393
    • Xu, H.1    Hsu, P.H.2    Zhang, L.3    Tsai, M.D.4    Freitas, M.A.5
  • 27
    • 84906306160 scopus 로고    scopus 로고
    • Proteomic characterization and three-dimensional electron microscopy study of PSII-LHCII supercomplexes from higher plants
    • 10.1016/j.bbabio.2013.11.004
    • Pagliano, C., Nield, J., Marsano, F., Pape, T., Barera, S., Saracco, G., and Barber, J. (2013) Proteomic characterization and three-dimensional electron microscopy study of PSII-LHCII supercomplexes from higher plants. Biochim. Biophys. Acta 10.1016/j.bbabio.2013.11.004
    • (2013) Biochim. Biophys. Acta
    • Pagliano, C.1    Nield, J.2    Marsano, F.3    Pape, T.4    Barera, S.5    Saracco, G.6    Barber, J.7
  • 29
    • 69849111184 scopus 로고    scopus 로고
    • Characterization and complementation of a psbR mutant in Arabidopsis thaliana
    • Liu, H., Frankel, L. K., and Bricker, T. M. (2009) Characterization and complementation of a psbR mutant in Arabidopsis thaliana. Arch. Biochem. Biophys. 489, 34-40
    • (2009) Arch. Biochem. Biophys. , vol.489 , pp. 34-40
    • Liu, H.1    Frankel, L.K.2    Bricker, T.M.3
  • 30
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • Caffarri, S., Kouril, R., Kereïche, S., Boekema, E. J., and Croce, R. (2009) Functional architecture of higher plant photosystem II supercomplexes. EMBO J. 28, 3052-3063
    • (2009) EMBO J. , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Kereïche, S.3    Boekema, E.J.4    Croce, R.5
  • 31
    • 1542314754 scopus 로고    scopus 로고
    • Identification of domains on the extrinsic 23 kDa protein possibly involved in electrostatic interaction with the extrinsic 33 kDa protein in spinach photosystem II
    • DOI 10.1111/j.1432-1033.2004.03998.x
    • Tohri, A., Dohmae, N., Suzuki, T., Ohta, H., Inoue, Y., and Enami, I. (2004) Identification of domains on the extrinsic 23-kDa protein possibly involved in electrostatic interaction with the extrinsic 33-kDa protein in spinach photosystem II. Eur. J. Biochem. 271, 962-971 (Pubitemid 38299650)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.5 , pp. 962-971
    • Tohri, A.1    Dohmae, N.2    Suzuki, T.3    Ohta, H.4    Inoue, Y.5    Enami, I.6
  • 32
    • 84906322592 scopus 로고    scopus 로고
    • Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II
    • 10.1016/j.bbabio.2013.12.012
    • Nishimura, T., Uno, C., Ido, K., Nagao, R., Noguchi, T., Sato, F., and Ifuku, K. (2014) Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II. Biochim. Biophys. Acta 10.1016/j.bbabio.2013.12.012
    • (2014) Biochim. Biophys. Acta
    • Nishimura, T.1    Uno, C.2    Ido, K.3    Nagao, R.4    Noguchi, T.5    Sato, F.6    Ifuku, K.7
  • 33
    • 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
    • DOI 10.1016/S0005-2728(89)80086-6
    • Miyao, M., and Murata, N. (1989) 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, 315-321 (Pubitemid 20004623)
    • (1989) Biochimica et Biophysica Acta - Bioenergetics , vol.977 , Issue.3 , pp. 315-321
    • Miyao, M.1    Murata, N.2
  • 35
    • 27944461037 scopus 로고    scopus 로고
    • Association of the 17-kDa extrinsic protein with photosystem II in higher plants
    • DOI 10.1021/bi051704u
    • Meades, G. D., Jr., McLachlan, A., Sallans, L., Limbach, P. A., Frankel, L. K., and Bricker, T. M. (2005) Association of the 17-kDa extrinsic protein with photosystem II in higher plants. Biochemistry 44, 15216-15221 (Pubitemid 41681455)
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15216-15221
    • Meades Jr., G.D.1    McLachlan, A.2    Sallans, L.3    Limbach, P.A.4    Frankel, L.K.5    Bricker, T.M.6
  • 36
    • 84896967401 scopus 로고    scopus 로고
    • MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II
    • Liu, H., Zhang, H., Weisz, D. A., Vidavsky, I., Gross, M. L., and Pakrasi, H. B. (2014) MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II. Proc. Natl. Acad. Sci. U.S.A. 111, 4638-4643
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 4638-4643
    • Liu, H.1    Zhang, H.2    Weisz, D.A.3    Vidavsky, I.4    Gross, M.L.5    Pakrasi, H.B.6
  • 37
    • 0024278052 scopus 로고
    • Organization of the oxygen-evolution enzyme complex studied by butanol/water phase partitioning of spinach photosystem II particles
    • Yamamoto, Y. (1988) Organization of the oxygen-evolution enzyme complex studied by butanol/water phase partitioning of spinach photosystem II particles. J. Biol. Chem. 263, 497-500
    • (1988) J. Biol. Chem. , vol.263 , pp. 497-500
    • Yamamoto, Y.1
  • 38
    • 0028964015 scopus 로고
    • The action of mercury on the binding of the extrinsic polypeptides associated with the water oxidizing complex of photosystem II
    • Bernier, M., and Carpentier, R. (1995) The action of mercury on the binding of the extrinsic polypeptides associated with the water oxidizing complex of photosystem II. FEBS Lett. 360, 251-254
    • (1995) FEBS Lett. , vol.360 , pp. 251-254
    • Bernier, M.1    Carpentier, R.2
  • 39
    • 33644867374 scopus 로고    scopus 로고
    • The 33 kDa protein can be removed without affecting the association of the 23 and 17 kDa proteins with the luminal side of PS II of spinach
    • DOI 10.1021/bi051604o
    • Yu, H., Xu, X., and Britt, R. D. (2006) The 33 kDa protein can be removed without affecting the association of the 23 and 17 kDa proteins with the luminal side of PS II of spinach. Biochemistry 45, 3404-3411 (Pubitemid 43376359)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3404-3411
    • Yu, H.1    Xu, X.2    Britt, R.D.3
  • 40
    • 77952384755 scopus 로고    scopus 로고
    • Topological analysis of the extrinsic PsbO, PsbP and PsbQ proteins in a green algal PSII complex by cross-linking with a water-soluble carbodiimide
    • Nagao, R., Suzuki, T., Okumura, A., Niikura, A., Iwai, M., Dohmae, N., Tomo, T., Shen, J.-R., Ikeuchi, M., and Enami, I. (2010) Topological analysis of the extrinsic PsbO, PsbP and PsbQ proteins in a green algal PSII complex by cross-linking with a water-soluble carbodiimide. Plant Cell Physiol. 51, 718-727
    • (2010) Plant Cell Physiol. , vol.51 , pp. 718-727
    • Nagao, R.1    Suzuki, T.2    Okumura, A.3    Niikura, A.4    Iwai, M.5    Dohmae, N.6    Tomo, T.7    Shen, J.-R.8    Ikeuchi, M.9    Enami, I.10
  • 41
    • 34548297894 scopus 로고    scopus 로고
    • The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana
    • DOI 10.1074/jbc.M705011200
    • Yi, X., Hargett, S. R., Liu, H., Frankel, L. K., and Bricker, T. M. (2007) The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana. J. Biol. Chem. 282, 24833-24841 (Pubitemid 47347527)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24833-24841
    • Yi, X.1    Hargett, S.R.2    Liu, H.3    Frankel, L.K.4    Bricker, T.M.5
  • 42
    • 33748751106 scopus 로고    scopus 로고
    • The PsbQ protein is required in Arabidopsis for photosystem II assembly/stability and photoautotrophy under low light conditions
    • DOI 10.1074/jbc.M603582200
    • Yi, X., Hargett, S. R., Frankel, L. K., and Bricker, T. M. (2006) The PsbQ protein is required in Arabidopsis for photosystem II assembly/stability and photoautotrophy under low light conditions. J. Biol. Chem. 281, 26260-26267 (Pubitemid 44401834)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26260-26267
    • Yi, X.1    Hargett, S.R.2    Frankel, L.K.3    Bricker, T.M.4
  • 43
    • 0028142413 scopus 로고
    • Expression of the 23 kDa protein from the oxygenevolving complex of higher plants in Escherichia coli
    • Seidler, A. (1994) Expression of the 23 kDa protein from the oxygenevolving complex of higher plants in Escherichia coli. Biochim. Biophys. Acta 1187, 73-79
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 73-79
    • Seidler, A.1
  • 44
    • 0001472568 scopus 로고
    • Partial degradation of the extrinsic 23-kDa protein of the Photosystem II complex of spinach
    • Miyao, M., Fujimura, Y., and Murata, N. (1988) Partial degradation of the extrinsic 23-kDa protein of the Photosystem II complex of spinach. Biochim. Biophys. Acta 936, 465-474
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 465-474
    • Miyao, M.1    Fujimura, Y.2    Murata, N.3


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