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Volumn 152, Issue 1, 2005, Pages 28-35

Localization of the PsbH subunit in photosystem II from the Synechocystis 6803 using the His-tagged Ni-NTA Nanogold labeling

Author keywords

Electron microscopy; Immunogold labeling; Photosystem II; PsbH protein

Indexed keywords

DIMER; HISTIDINE; NICKEL; NITRILOTRIACETIC ACID; PROTEIN CP 47; PROTEIN PSBH; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 25644435750     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2005.08.001     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0017411320 scopus 로고
    • Phosphorylation of chloroplast membrane polypeptides
    • J. Bennet Phosphorylation of chloroplast membrane polypeptides Nature 269 1977 344 346
    • (1977) Nature , vol.269 , pp. 344-346
    • Bennet, J.1
  • 4
    • 3242816123 scopus 로고    scopus 로고
    • Structural characterization of photosystem II complex from red alga Porphyridium cruentum retaining extrinsic subunits of the oxygen-evolving complex
    • L. Bumba, H. Havelková-Doušová, M. Hušák, and F. Vácha Structural characterization of photosystem II complex from red alga Porphyridium cruentum retaining extrinsic subunits of the oxygen-evolving complex Eur. J. Biochem. 271 2004 2967 2975
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2967-2975
    • Bumba, L.1    Havelková-Doušová, H.2    Hušák, M.3    Vácha, F.4
  • 5
    • 0041875132 scopus 로고    scopus 로고
    • Electron microscopy in structural studies of photosystem II
    • L. Bumba, and F. Vácha Electron microscopy in structural studies of photosystem II Photosynth. Res. 77 2003 1 19
    • (2003) Photosynth. Res. , vol.77 , pp. 1-19
    • Bumba, L.1    Vácha, F.2
  • 6
    • 0003034011 scopus 로고
    • N-terminal sequence analysis of the 8-kDa protein in Chlamydomonas reinhardtii-localization of the phosphothreonine
    • N. Dedner, H.E. Meyer, C. Ashton, and G.F. Wildner N-terminal sequence analysis of the 8-kDa protein in Chlamydomonas reinhardtii-localization of the phosphothreonine FEBS Lett. 236 1988 77 82
    • (1988) FEBS Lett. , vol.236 , pp. 77-82
    • Dedner, N.1    Meyer, H.E.2    Ashton, C.3    Wildner, G.F.4
  • 8
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y.H. Li, M. Ladjadj, and A. Leith SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 10
    • 0344961712 scopus 로고    scopus 로고
    • Overexpression and purification of recombinant membrane PsbH protein in Escherichia coli
    • Z. Halbhuber, Z. Petrmichlová, K. Alexciev, E. Thulin, and D. Štys Overexpression and purification of recombinant membrane PsbH protein in Escherichia coli Protein Expr. Purif. 32 2003 18 27
    • (2003) Protein Expr. Purif. , vol.32 , pp. 18-27
    • Halbhuber, Z.1    Petrmichlová, Z.2    Alexciev, K.3    Thulin, E.4    Štys, D.5
  • 11
    • 0035979783 scopus 로고    scopus 로고
    • Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II
    • B. Hankamer, E.P. Morris, J. Nield, A. Carne, and J. Barber Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II FEBS Lett. 504 2001 142 151
    • (2001) FEBS Lett. , vol.504 , pp. 142-151
    • Hankamer, B.1    Morris, E.P.2    Nield, J.3    Carne, A.4    Barber, J.5
  • 12
    • 0035783236 scopus 로고    scopus 로고
    • Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy
    • B. Hankamer, E.P. Morris, J. Nield, C. Gerle, and J. Barber Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy J. Struct. Biol. 135 2001 262 269
    • (2001) J. Struct. Biol. , vol.135 , pp. 262-269
    • Hankamer, B.1    Morris, E.P.2    Nield, J.3    Gerle, C.4    Barber, J.5
  • 13
    • 0024213727 scopus 로고
    • Statistical image analysis of electron micrographs of ribosomal subunits
    • G. Harauz, E. Boekema, and M. van Heel Statistical image analysis of electron micrographs of ribosomal subunits Methods Enzymol. 164 1988 35 49
    • (1988) Methods Enzymol. , vol.164 , pp. 35-49
    • Harauz, G.1    Boekema, E.2    Van Heel, M.3
  • 14
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution
    • N. Kamiya, and J.R. Shen Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution Proc. Natl. Acad. Sci. USA 100 2003 98 103
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 15
    • 0029088399 scopus 로고
    • B site and dependent on protein-synthesis
    • B site and dependent on protein-synthesis Biochemistry 34 1995 9625 9631
    • (1995) Biochemistry , vol.34 , pp. 9625-9631
    • Komenda, J.1    Barber, J.2
  • 16
    • 0036161818 scopus 로고    scopus 로고
    • Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC6803
    • J. Komenda, L. Lupinkova, and J. Kopecky Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC6803 Eur. J. Biochem. 269 2002 610 619
    • (2002) Eur. J. Biochem. , vol.269 , pp. 610-619
    • Komenda, J.1    Lupinkova, L.2    Kopecky, J.3
  • 17
    • 10344256210 scopus 로고    scopus 로고
    • Accumulation of the D2 protein is a key regulatory step for assembly of the photosystem II reaction center complex in Synechocystis PCC6803
    • J. Komenda, V. Reisinger, B.C. Muller, M. Dobakova, B. Granvogl, and L.A. Eichacker Accumulation of the D2 protein is a key regulatory step for assembly of the photosystem II reaction center complex in Synechocystis PCC6803 J. Biol. Chem. 279 2004 48620 48629
    • (2004) J. Biol. Chem. , vol.279 , pp. 48620-48629
    • Komenda, J.1    Reisinger, V.2    Muller, B.C.3    Dobakova, M.4    Granvogl, B.5    Eichacker, L.A.6
  • 19
    • 0000932046 scopus 로고    scopus 로고
    • Localization of cyanobacterial photosystem II donor-side subunits by electron microscopy and the supramolecular organization of photosystem II in the thylakoid membrane
    • H. Kuhl, M. Rogner, J.F.L. van Breemen, and E.J. Boekema Localization of cyanobacterial photosystem II donor-side subunits by electron microscopy and the supramolecular organization of photosystem II in the thylakoid membrane Eur. J. Biochem. 266 1999 453 459
    • (1999) Eur. J. Biochem. , vol.266 , pp. 453-459
    • Kuhl, H.1    Rogner, M.2    Van Breemen, J.F.L.3    Boekema, E.J.4
  • 20
    • 0033986505 scopus 로고    scopus 로고
    • Increased production of zeaxanthin and other pigments by application of genetic engineering techniques to Synechocystis sp. strain PCC6803
    • D. Lagarde, L. Beuf, and W. Vermaas Increased production of zeaxanthin and other pigments by application of genetic engineering techniques to Synechocystis sp. strain PCC6803 Appl. Environ. Microbiol. 66 2000 64 72
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 64-72
    • Lagarde, D.1    Beuf, L.2    Vermaas, W.3
  • 21
    • 0026210319 scopus 로고
    • Primary structure of the psbN-psbH-petC-petA gene cluster of the cyanobacterium Synechocystis PCC6803
    • S.R. Mayes, and J. Barber Primary structure of the psbN-psbH-petC-petA gene cluster of the cyanobacterium Synechocystis PCC6803 Plant Mol. Biol. 17 1991 289 293
    • (1991) Plant Mol. Biol. , vol.17 , pp. 289-293
    • Mayes, S.R.1    Barber, J.2
  • 22
    • 0027404905 scopus 로고
    • Further characterization of the psbH locus of Synechocystis sp. PCC 6803-inactivation of psbH impairs Q(A) to Q(B) electron-transport in photosystem 2
    • S.R. Mayes, J.M. Dubbs, I. Vass, E. Hideg, L. Nagy, and J. Barber Further characterization of the psbH locus of Synechocystis sp. PCC 6803-inactivation of psbH impairs Q(A) to Q(B) electron-transport in photosystem 2 Biochemistry 32 1993 1454 1465
    • (1993) Biochemistry , vol.32 , pp. 1454-1465
    • Mayes, S.R.1    Dubbs, J.M.2    Vass, I.3    Hideg, E.4    Nagy, L.5    Barber, J.6
  • 23
    • 0345476429 scopus 로고
    • Identification of the phosphorylation site of an 8.3 kDa protein from photosystem II of spinach
    • H.P. Michel, and J. Bennett Identification of the phosphorylation site of an 8.3 kDa protein from photosystem II of spinach FEBS Lett. 212 1987 1123 1130
    • (1987) FEBS Lett. , vol.212 , pp. 1123-1130
    • Michel, H.P.1    Bennett, J.2
  • 24
    • 0034623285 scopus 로고    scopus 로고
    • 3D maps of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allow for comparison of their OEC organisation
    • J. Nield, O. Kruse, J. Ruprecht, P. da Fonseca, C. Buchel, and J. Barber 3D maps of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allow for comparison of their OEC organisation J. Biol. Chem. 275 2000 27940 27946
    • (2000) J. Biol. Chem. , vol.275 , pp. 27940-27946
    • Nield, J.1    Kruse, O.2    Ruprecht, J.3    Da Fonseca, P.4    Buchel, C.5    Barber, J.6
  • 25
    • 0032516010 scopus 로고    scopus 로고
    • The 9-kDa phosphoprotein of photosystem II. Generation and characterisation of Chlamydomonas mutants lacking PSII-H and a site-directed mutant lacking the phosphorylation site
    • H.E. O'Connor, S.V. Ruffle, A.J. Cain, Z. Deak, I. Vass, J.H.A. Nugent, and S. Purton The 9-kDa phosphoprotein of photosystem II. Generation and characterisation of Chlamydomonas mutants lacking PSII-H and a site-directed mutant lacking the phosphorylation site Biochim. Biophys. Acta 1364 1998 63 72
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 63-72
    • O'Connor, H.E.1    Ruffle, S.V.2    Cain, A.J.3    Deak, Z.4    Vass, I.5    Nugent, J.H.A.6    Purton, S.7
  • 26
    • 0034536337 scopus 로고    scopus 로고
    • The low molecular mass PsbW protein is involved in the stabilization of the dimeric photosystem II complex in Arabidopsis thaliana
    • L.X. Shi, Z.J. Lorkovic, R. Oelmuller, and W.P. Schröder The low molecular mass PsbW protein is involved in the stabilization of the dimeric photosystem II complex in Arabidopsis thaliana J. Biol. Chem. 275 2000 37945 37950
    • (2000) J. Biol. Chem. , vol.275 , pp. 37945-37950
    • Shi, L.X.1    Lorkovic, Z.J.2    Oelmuller, R.3    Schröder, W.P.4
  • 27
    • 1042290470 scopus 로고    scopus 로고
    • The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
    • L.X. Shi, and W.P. Schröder The low molecular mass subunits of the photosynthetic supracomplex, photosystem II Biochim. Biophys. Acta 1608 2004 75 96
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 75-96
    • Shi, L.X.1    Schröder, W.P.2
  • 29
    • 1842335752 scopus 로고    scopus 로고
    • Requirement for the H phosphoprotein in photosystem II of Chlamydomonas reinhardtii
    • E.J. Summer, V.H.R. Schmid, B.U. Bruns, and G.W. Schmidt Requirement for the H phosphoprotein in photosystem II of Chlamydomonas reinhardtii Plant Physiol. 113 1997 1359 1368
    • (1997) Plant Physiol. , vol.113 , pp. 1359-1368
    • Summer, E.J.1    Schmid, V.H.R.2    Bruns, B.U.3    Schmidt, G.W.4
  • 30
    • 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
    • M. Suorsa, R. Regel, V. Paakkarinen, N. Battchikova, R.G. Herrmann, and E.-M. Aro Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ Eur. J. Biochem. 271 2004 96 107
    • (2004) Eur. J. Biochem. , vol.271 , pp. 96-107
    • Suorsa, M.1    Regel, R.2    Paakkarinen, V.3    Battchikova, N.4    Herrmann, R.G.5    Aro, E.-M.6
  • 32
    • 0023090371 scopus 로고
    • Similarity between images
    • M. van Heel Similarity between images Ultramicroscopy 21 1987 95 100
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 33
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analyzing the images of biological macromolecules
    • M. van Heel, and J. Frank Use of multivariate statistics in analyzing the images of biological macromolecules Ultramicroscopy 6 1981 187 194
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • Van Heel, M.1    Frank, J.2
  • 34
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • A.V. Vener, A. Harms, M.R. Sussman, and R.D. Vierstra Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana J. Biol. Chem. 276 2001 6959 6966
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 35
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • A. Zouni, H.T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger, and P. Orth Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution Nature 409 2001 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.