메뉴 건너뛰기




Volumn 1706, Issue 1-2, 2005, Pages 81-87

Reconstitution of phycobilisome core-membrane linker, L CM, by autocatalytic chromophore binding to ApcE

Author keywords

Allophycocyanin; ApcE; Biosynthesis; Core membrane linker (L CM); Cyanobacteria; Energy transfer; Fluorescence labeling; Photosynthesis; Phycobilisome; Phycocyanobilin attachment

Indexed keywords

ALLOPHYCOCYANIN; APOLIPOPROTEIN E; CYSTEINE; LYASE; MEMBRANE PROTEIN; PHYTOCHROME; PROTEIN LCM; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; UREA;

EID: 11144306461     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.09.008     Document Type: Article
Times cited : (68)

References (42)
  • 2
    • 0003123963 scopus 로고
    • Phycobilisome and phycobiliprotein structures
    • D.A. Bryant Kluwer Dordrecht
    • W.A. Sidler Phycobilisome and phycobiliprotein structures D.A. Bryant The Molecular Biology of Cyanobacteria 1994 Kluwer Dordrecht 139 216
    • (1994) The Molecular Biology of Cyanobacteria , pp. 139-216
    • Sidler, W.A.1
  • 3
    • 0000370919 scopus 로고
    • Adaptive variations in Phycobilisome structure
    • A.N. Glazer Adaptive variations in Phycobilisome structure Adv. Mol. Cell Biol. 10 1994 119 149
    • (1994) Adv. Mol. Cell Biol. , vol.10 , pp. 119-149
    • Glazer, A.N.1
  • 4
    • 0242686975 scopus 로고
    • Allophycocyanin I and the 95 kDa polypeptide. The bridge between phycobilisomes and membranes
    • M. Rusckowski, and B.A. Zilinskas Allophycocyanin I and the 95 kDa polypeptide. The bridge between phycobilisomes and membranes Plant Physiol. 70 1982 1055 1059
    • (1982) Plant Physiol. , vol.70 , pp. 1055-1059
    • Rusckowski, M.1    Zilinskas, B.A.2
  • 5
    • 4243139477 scopus 로고
    • Investigations on the arrangement of Porphyridium cruentum phycobilisomes
    • G. Wanner, and H.-P. Köst Investigations on the arrangement of Porphyridium cruentum phycobilisomes Protoplasma 102 1980 97 109
    • (1980) Protoplasma , vol.102 , pp. 97-109
    • Wanner, G.1    Köst, H.-P.2
  • 6
    • 0019778784 scopus 로고
    • A terminal energy acceptor of the Phycobilisome-the 75 kDa polypeptide of Synechococcus 6301 Phycobilisomes-a new Biliprotein
    • D.J. Lundell, G. Yamanaka, and A.N. Glazer A terminal energy acceptor of the Phycobilisome-the 75 kDa polypeptide of Synechococcus 6301 Phycobilisomes-a new Biliprotein J. Cell Biol. 91 1981 315 319
    • (1981) J. Cell Biol. , vol.91 , pp. 315-319
    • Lundell, D.J.1    Yamanaka, G.2    Glazer, A.N.3
  • 9
    • 11144262093 scopus 로고    scopus 로고
    • Structure-function studies on the extended phytochrome family of bilin lyases
    • F. Gasparro N.L. Oleinick F. Hearst J.E. Urbach American Society of Photobiology San Francisco
    • J.C. Lagarias, S.H. Wu, and L. Eng Structure-function studies on the extended phytochrome family of bilin lyases F. Gasparro N.L. Oleinick F. Hearst J.E. Urbach 13th Intl. Congress on photobiology 2000 American Society of Photobiology San Francisco 146 Abstract 443
    • (2000) 13th Intl. Congress on Photobiology , pp. 146
    • Lagarias, J.C.1    Wu, S.H.2    Eng, L.3
  • 10
    • 0002323237 scopus 로고    scopus 로고
    • Biosynthesis of Phycobiliproteins in Cyanobacteria
    • G.A. Peschek W. Löffelhardt G. Schmetterer Kluwer/Plenum New York
    • W.M. Schluchter, and A.N. Glazer Biosynthesis of Phycobiliproteins in Cyanobacteria G.A. Peschek W. Löffelhardt G. Schmetterer The Phototrophic Prokaryotes 1999 Kluwer/Plenum New York 83 95
    • (1999) The Phototrophic Prokaryotes , pp. 83-95
    • Schluchter, W.M.1    Glazer, A.N.2
  • 12
    • 0020827097 scopus 로고
    • Fluorescent tandem phycobiliprotein conjugates. Emission wavelength shifting by energy transfer
    • A.N. Glazer, and L. Stryer Fluorescent tandem phycobiliprotein conjugates. Emission wavelength shifting by energy transfer Biophys. J. 43 1983 383 386
    • (1983) Biophys. J. , vol.43 , pp. 383-386
    • Glazer, A.N.1    Stryer, L.2
  • 13
    • 0020329336 scopus 로고
    • Fluorescent phycobiliprotein conjugates for analyses of cells and molecules
    • V.T. Oi, A.N. Glazer, and L. Stryer Fluorescent phycobiliprotein conjugates for analyses of cells and molecules J. Cell Biol. 93 1982 981 986
    • (1982) J. Cell Biol. , vol.93 , pp. 981-986
    • Oi, V.T.1    Glazer, A.N.2    Stryer, L.3
  • 14
    • 0024202010 scopus 로고
    • Phycobiliproteins
    • A.N. Glazer Phycobiliproteins Methods Enzymol. 167 1988 291 303
    • (1988) Methods Enzymol. , vol.167 , pp. 291-303
    • Glazer, A.N.1
  • 15
    • 0034619430 scopus 로고    scopus 로고
    • Defining the Bilin Lyase Domain: Lessons from the Extended Phytochrome Superfamily
    • S.-H. Wu, and J.C. Lagarias Defining the Bilin Lyase Domain: lessons from the Extended Phytochrome Superfamily Biochemistry 39 2000 13487 13495
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.-H.1    Lagarias, J.C.2
  • 16
    • 0024279623 scopus 로고
    • In vitro attachment of Bilins to Apophycocyanin: 2. Determination of the structures of tryptic Bilin peptides derived from the Phycocyanobilin adduct
    • D.M. Arciero, J.L. Dallas, and A.N. Glazer In vitro attachment of Bilins to Apophycocyanin: 2. Determination of the structures of tryptic Bilin peptides derived from the Phycocyanobilin adduct J. Biol. Chem. 263 1988 18350 18357
    • (1988) J. Biol. Chem. , vol.263 , pp. 18350-18357
    • Arciero, D.M.1    Dallas, J.L.2    Glazer, A.N.3
  • 17
    • 3242705066 scopus 로고    scopus 로고
    • Non-enzymatic chromophore attachment in biliproteins: Conformational control by the detergent Triton X-100
    • K.H. Zhao, J.P. Zhu, B. Song, M. Zhou, M. Storf, S. Böhm, C. Bubenzer, and H. Scheer Non-enzymatic chromophore attachment in biliproteins: conformational control by the detergent Triton X-100 Biochim. Biophys. Acta 1657 2004 131 145
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 131-145
    • Zhao, K.H.1    Zhu, J.P.2    Song, B.3    Zhou, M.4    Storf, M.5    Böhm, S.6    Bubenzer, C.7    Scheer, H.8
  • 19
    • 0026705171 scopus 로고
    • Core mutations of Synechococcus sp. PCC 7002 phycobilisomes: A spectroscopic study
    • Y.M. Gindt, J. Zhou, D.A. Bryant, and K. Sauer Core mutations of Synechococcus sp. PCC 7002 phycobilisomes: a spectroscopic study J. Photochem. Photobiol., B Biol. 15 1992 75 89
    • (1992) J. Photochem. Photobiol., B Biol. , vol.15 , pp. 75-89
    • Gindt, Y.M.1    Zhou, J.2    Bryant, D.A.3    Sauer, K.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriopharge T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriopharge T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029038122 scopus 로고
    • Continuous fluorescence assay ofphytochrome assembly in vitro
    • L. Li, J.T. Murphy, and J.C. Lagarias Continuous fluorescence assay ofphytochrome assembly in vitro Biochemistry 34 1995 7923 7930
    • (1995) Biochemistry , vol.34 , pp. 7923-7930
    • Li, L.1    Murphy, J.T.2    Lagarias, J.C.3
  • 24
    • 0015935166 scopus 로고
    • Chromophore content of blue-green algal phycobiliproteins
    • A.N. Glazer, and S. Fang Chromophore content of blue-green algal phycobiliproteins J. Biol. Chem. 248 1973 659 662
    • (1973) J. Biol. Chem. , vol.248 , pp. 659-662
    • Glazer, A.N.1    Fang, S.2
  • 25
    • 0002359730 scopus 로고
    • Chlorophyll fluorescence as a physiological probe of the photosynthetic apparatus
    • H. Scheer CRC Press Boca Raton
    • K.K. Karukstis Chlorophyll fluorescence as a physiological probe of the photosynthetic apparatus H. Scheer Chlorophylls 1991 CRC Press Boca Raton 769 796
    • (1991) Chlorophylls , pp. 769-796
    • Karukstis, K.K.1
  • 26
    • 0034619430 scopus 로고    scopus 로고
    • Defining the Bilin Lyase Domain: Lessons from the Extended Phytochrome Superfamily
    • S.-H. Wu, and J.C. Lagarias Defining the Bilin Lyase Domain: lessons from the Extended Phytochrome Superfamily Biochemistry 39 2000 13487 13495
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.-H.1    Lagarias, J.C.2
  • 27
    • 0031466353 scopus 로고    scopus 로고
    • Phytochrome photochromism probed by site-directed mutations and chromophore esterification
    • S.H. Bhoo, T. Hirano, H. Jeong, J. Lee, M. Furuya, and P. Song Phytochrome photochromism probed by site-directed mutations and chromophore esterification J. Am. Chem. Soc. 119 1997 11717 11718
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11717-11718
    • Bhoo, S.H.1    Hirano, T.2    Jeong, H.3    Lee, J.4    Furuya, M.5    Song, P.6
  • 28
    • 0035725360 scopus 로고    scopus 로고
    • Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure
    • T. Lamparter, B. Esteban, and J. Hughes Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure Eur. J. Biochem. 268 2001 4720 4730
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4720-4730
    • Lamparter, T.1    Esteban, B.2    Hughes, J.3
  • 29
    • 0028245818 scopus 로고
    • Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase
    • C.D. Fairchild, and A.N. Glazer Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase J. Biol. Chem. 269 1994 8686 8694
    • (1994) J. Biol. Chem. , vol.269 , pp. 8686-8694
    • Fairchild, C.D.1    Glazer, A.N.2
  • 30
    • 0036379292 scopus 로고    scopus 로고
    • Characterization of phycoviolobilin phycoerythrocyanin-α84-cystein- lyase-(isomerizing) from Mastigocladus laminosus
    • K.-H. Zhao, D. Wu, L. Wang, M. Zhou, M. Storf, C. Bubenzer, B. Strohmann, and H. Scheer Characterization of phycoviolobilin phycoerythrocyanin-α84- cystein-lyase-(isomerizing) from Mastigocladus laminosus Eur. J. Biochem. 269 2002 4542 4550
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4542-4550
    • Zhao, K.-H.1    Wu, D.2    Wang, L.3    Zhou, M.4    Storf, M.5    Bubenzer, C.6    Strohmann, B.7    Scheer, H.8
  • 31
    • 0002427093 scopus 로고
    • Phycobiliproteins: Molecular aspects of photosynthetic antenna systems
    • F.K. Fong Springer Berlin
    • H. Scheer Phycobiliproteins: molecular aspects of photosynthetic antenna systems F.K. Fong Light Reaction Path of Photosynthesis 1982 Springer Berlin 7 45
    • (1982) Light Reaction Path of Photosynthesis , pp. 7-45
    • Scheer, H.1
  • 32
    • 4444326150 scopus 로고    scopus 로고
    • Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120: Lyase activities, chromophore exchange and photochromism in phytochrome AphA
    • K.-H. Zhao, Y. Ran, M. Li, Y.-N. Sun, M. Zhou, M. Storf, M. Kupka, S. Böhm, C. Bubenzer, and H. Scheer Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120: lyase activities, chromophore exchange and photochromism in phytochrome AphA Biochemistry 43 2004 11576 11588
    • (2004) Biochemistry , vol.43 , pp. 11576-11588
    • Zhao, K.-H.1    Ran, Y.2    Li, M.3    Sun, Y.-N.4    Zhou, M.5    Storf, M.6    Kupka, M.7    Böhm, S.8    Bubenzer, C.9    Scheer, H.10
  • 35
    • 0028595909 scopus 로고
    • Femtosecond spectral and anisotropy study of excitation energy transfer between neighbouring alpha-80 and beta-81 chromophores of allophycocyanin trimers
    • A.V. Sharkov, I.V. Kryukov, E.V. Khoroshilov, P.G. Kryukov, R. Fischer, H. Scheer, and T. Gillbro Femtosecond spectral and anisotropy study of excitation energy transfer between neighbouring alpha-80 and beta-81 chromophores of allophycocyanin trimers Biochim. Biophys. Acta 1188 1994 349 356
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 349-356
    • Sharkov, A.V.1    Kryukov, I.V.2    Khoroshilov, E.V.3    Kryukov, P.G.4    Fischer, R.5    Scheer, H.6    Gillbro, T.7
  • 38
    • 0029037179 scopus 로고
    • Isolation, crystallization,crystal structure analysis and refinement of Allophycocyanin from the Cyanobacterium Spirulina platensis at 2.3 a resolution
    • K. Brejc, R. Ficner, R. Huber, and S. Steinbacher Isolation, crystallization,crystal structure analysis and refinement of Allophycocyanin from the Cyanobacterium Spirulina platensis at 2.3 A resolution J. Mol. Biol. 249 1995 424 440
    • (1995) J. Mol. Biol. , vol.249 , pp. 424-440
    • Brejc, K.1    Ficner, R.2    Huber, R.3    Steinbacher, S.4
  • 39
    • 0030695502 scopus 로고    scopus 로고
    • Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus
    • A. Parbel, K.H. Zhao, J. Breton, and H. Scheer Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus Photosynth. Res. 54 1997 25 34
    • (1997) Photosynth. Res. , vol.54 , pp. 25-34
    • Parbel, A.1    Zhao, K.H.2    Breton, J.3    Scheer, H.4
  • 40
    • 0032189050 scopus 로고    scopus 로고
    • CM subunit does not affect phycobilisome assembly or energy transfer functions in the cyanobacterium Synechocystis sp. PCC6714
    • CM subunit does not affect phycobilisome assembly or energy transfer functions in the cyanobacterium Synechocystis sp. PCC6714 Eur. J. Biochem. 257 1998 154 159
    • (1998) Eur. J. Biochem. , vol.257 , pp. 154-159
    • Ajlani, G.1    Vernotte, C.2
  • 41
    • 0023053285 scopus 로고
    • Crystal structure analysis and refinement at 2.5A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum
    • T. Schirmer, R. Huber, M. Schneider, W. Bode, M. Miller, and M.L. Hackert Crystal structure analysis and refinement at 2.5A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum J. Mol. Biol. 188 1986 651 676
    • (1986) J. Mol. Biol. , vol.188 , pp. 651-676
    • Schirmer, T.1    Huber, R.2    Schneider, M.3    Bode, W.4    Miller, M.5    Hackert, M.L.6
  • 42
    • 1642276701 scopus 로고    scopus 로고
    • The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1
    • T. Lamparter, M. Carrascal, N. Michael, E. Martinez, G. Rottwinkel, and J. Abian The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1 Biochemistry 43 2004 3659 3669
    • (2004) Biochemistry , vol.43 , pp. 3659-3669
    • Lamparter, T.1    Carrascal, M.2    Michael, N.3    Martinez, E.4    Rottwinkel, G.5    Abian, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.