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Volumn 76, Issue 9, 2010, Pages 2729-2739

Biosynthesis of cyanobacterial phycobiliproteins in escherichia coli: Chromophorylation efficiency and specificity of all bilin lyases from synechococcus sp. strain PCC 7002

Author keywords

[No Author keywords available]

Indexed keywords

ALLOPHYCOCYANIN; BETA SUBUNIT; BILIN CHROMOPHORE; BIOSYNTHETIC PATHWAY; CO-EXPRESSION SYSTEMS; CYANOBACTERIUM; CYSTEINE RESIDUES; HETEROLOGOUS EXPRESSION; IN-VIVO; LIGHT-HARVESTING; LYASE ACTIVITY; N-TERMINALS; PHYCOBILIPROTEINS; PHYCOCYANIN; SYNECHOCOCCUS; TETRAPYRROLES; THIOETHER LINKAGES;

EID: 77951570324     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03100-09     Document Type: Article
Times cited : (61)

References (78)
  • 1
    • 0032104835 scopus 로고    scopus 로고
    • Construction and characterization of a phycobiliprotein-less mutant of Synechocystis sp. PCC 6803
    • Ajlani, G., and C. Vernotte. 1998. Construction and characterization of a phycobiliprotein-less mutant of Synechocystis sp. PCC 6803. Plant Mol. Biol. 37:577-580.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 577-580
    • Ajlani, G.1    Vernotte, C.2
  • 2
    • 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. 257:154-159.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 154-159
    • Ajlani, G.1    Vernotte, C.2
  • 3
    • 0024279594 scopus 로고
    • Vitro attachment of bilins to apophycocyanin I: Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin
    • Arciero, D. M., D. A. Bryant, and A. N. Glazer. 1988. In vitro attachment of bilins to apophycocyanin I: specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin. J. Biol. Chem. 263:18343-18349.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18343-18349
    • Arciero, D.M.1    Bryant, D.A.2    Glazer, A.N.3
  • 4
    • 0024279623 scopus 로고
    • Vitro attachment of bilins to apophycocyanin. II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct
    • Arciero, D. M., J. L. Dallas, and A. N. Glazer. 1988. In vitro attachment of bilins to apophycocyanin. II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct. J. Biol. Chem. 263:18350-18357.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18350-18357
    • Arciero, D.M.1    Dallas, J.L.2    Glazer, A.N.3
  • 5
    • 0032724125 scopus 로고    scopus 로고
    • The role of ApcD and ApcF in energy transfer from phycobilisomes to PSI and PSII in a cyanobacterium
    • Ashby, M. K., and C. W. Mullineaux. 1999. The role of ApcD and ApcF in energy transfer from phycobilisomes to PSI and PSII in a cyanobacterium. Photosynth. Res. 61:169-179.
    • (1999) Photosynth. Res. , vol.61 , pp. 169-179
    • Ashby, M.K.1    Mullineaux, C.W.2
  • 6
    • 33751391261 scopus 로고
    • Energy-transfer and exciton-state relaxation processes in allophycocyanin
    • Beck, W. F., and K. Sauer. 1992. Energy-transfer and exciton-state relaxation processes in allophycocyanin. J. Phys. Chem. 96:4658-4666.
    • (1992) J. Phys. Chem. , vol.96 , pp. 4658-4666
    • Beck, W.F.1    Sauer, K.2
  • 7
    • 0022486877 scopus 로고
    • Visualization of bilin-linked peptides and proteins in Polyacrylamide gels
    • Berkelman, T. R., and J. C. Lagarias. 1986. Visualization of bilin-linked peptides and proteins in Polyacrylamide gels. Anal. Biochem. 156:194-201.
    • (1986) Anal. Biochem. , vol.156 , pp. 194-201
    • Berkelman, T.R.1    Lagarias, J.C.2
  • 8
    • 0028518755 scopus 로고
    • Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and their inactivation in Synechococcus sp. PCC 7942
    • Bhalerao, R. P., L. K. Kind, and P. Gustafsson. 1994. Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and their inactivation in Synechococcus sp. PCC 7942. Plant Mol. Biol. 26:313-326.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 313-326
    • Bhalerao, R.P.1    Kind, L.K.2    Gustafsson, P.3
  • 10
    • 44649188496 scopus 로고    scopus 로고
    • Complementation of a phycocyanin-bilin lyase from Synechocystis sp. PCC 6803 with a nucleomorph-encoded open reading frame from the cryptophyte Guillardia theta
    • Bolte, K., O. Kawach, J. Prechtl, N. Gruenheit, J. Nyalwidhe, and U. G. Maier. 2008. Complementation of a phycocyanin-bilin lyase from Synechocystis sp. PCC 6803 with a nucleomorph-encoded open reading frame from the cryptophyte Guillardia theta, BMC Plant Biol. 8:56.
    • (2008) BMC Plant Biol. , vol.8 , pp. 56
    • Bolte, K.1    Kawach, O.2    Prechtl, J.3    Gruenheit, N.4    Nyalwidhe, J.5    Maier, U.G.6
  • 11
    • 0029037179 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 Å resolution
    • Brejc, K., R. Ficner, R. Huber, and S. Steinbacher. 1995. Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 Å resolution. J. Mol. Biol. 249:424-440.
    • (1995) J. Mol. Biol. , vol.249 , pp. 424-440
    • Brejc, K.1    Ficner, R.2    Huber, R.3    Steinbacher, S.4
  • 12
    • 0000765229 scopus 로고
    • Cyanobacterial phycobilisomes: Progress toward complete structural and functional analysis via molecular genetics
    • L. Bogarad and I. L. Vasil (ed.), Academic Press, San Diego, CA.
    • Bryant, D. A. 1991. Cyanobacterial phycobilisomes: progress toward complete structural and functional analysis via molecular genetics, p. 257-300. In L. Bogarad and I. L. Vasil (ed.), Cell culture and somatic cell genetics of plants, vol.7B. Academic Press, San Diego, CA.
    • (1991) Cell Culture and Somatic Cell Genetics of Plants , vol.7 B , pp. 257-300
    • Bryant, D.A.1
  • 13
    • 0025882840 scopus 로고
    • The "anchor polypeptide" of cyanobacterial phycobilisomes: Molecular characterization of the Synechococcus sp. PCC 6301 apce gene
    • 13. Capuano, V., A. S. Braux, N. Tandeau de Marsac, and J. Houmard. 1991. The "anchor polypeptide" of cyanobacterial phycobilisomes. Molecular characterization of the Synechococcus sp. PCC 6301 apcE gene. J. Biol. Chem. 266:7239-7247. (Pubitemid 21906358)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.11 , pp. 7239-7247
    • Capuano, V.1    Braux, A.-S.2    De Marsac, N.T.3    Houmard, J.4
  • 15
    • 0032127571 scopus 로고    scopus 로고
    • Phytobilin biosynthesis: Cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803
    • DOI 10.1046/j.1365-313X.1998.00186.x
    • 15. Cornejo, J., R. D. Willows, and S. I. Beale. 1998. Fhytobilin biosynthesis: cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803. Plant J. 15:99-107. (Pubitemid 28356021)
    • (1998) Plant Journal , vol.15 , Issue.1 , pp. 99-107
    • Cornejo, J.1    Willows, R.D.2    Beale, S.I.3
  • 16
    • 67649488067 scopus 로고    scopus 로고
    • ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem i and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp. PCC 7002
    • Dong, C., A. Tang, J. Zhao, C. W. Mullineaux, G. Shen, and D. A. Bryant. 2009. ApcD is necessary for efficient energy transfer from phycobilisomes to photosystem I and helps to prevent photoinhibition in the cyanobacterium Synechococcus sp. PCC 7002. Biochim. Biophys. Acta Bioenerget. 1787:1122-1128.
    • (2009) Biochim. Biophys. Acta Bioenerget. , vol.1787 , pp. 1122-1128
    • Dong, C.1    Tang, A.2    Zhao, J.3    Mullineaux, C.W.4    Shen, G.5    Bryant, D.A.6
  • 17
    • 0028201784 scopus 로고
    • The complete amino acid sequence of R-phycocyanin-I α and β subunits from the red alga Porphyridium cmentum: Structural and phylogenetic relationships of the phycocyanins within the phycobiliproteins families
    • Ducret, A., W. Sidler, G. Frank, and H. Zuber. 1994. The complete amino acid sequence of R-phycocyanin-I α and β subunits from the red alga Porphyridium cmentum: structural and phylogenetic relationships of the phycocyanins within the phycobiliproteins families. Eur. J. Biochem. 221:563-580.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 563-580
    • Ducret, A.1    Sidler, W.2    Frank, G.3    Zuber, H.4
  • 18
    • 0028046145 scopus 로고
    • Nonenzymatic bilin addition to the α subunit of an apophycoerythrin
    • Fairchild, C. D., and A. N. Glazer. 1994. Nonenzymatic bilin addition to the α subunit of an apophycoerythrin. J. Biol. Chem. 269:28988-28996.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28988-28996
    • Fairchild, C.D.1    Glazer, A.N.2
  • 19
    • 0028245818 scopus 로고
    • Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase
    • Fairchild, C. D., and A. N. Glazer. 1994. Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase. J. Biol. Chem. 269:8686-8694.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8686-8694
    • Fairchild, C.D.1    Glazer, A.N.2
  • 21
    • 0037999874 scopus 로고    scopus 로고
    • Phycocyanobilin:ferredoxin oxidoreductase of Anabaena sp. PCC 7120: Biochemical and spectroscopic characterization
    • Frankenberg, N., and J. C. Lagarias. 2003. Phycocyanobilin:ferredoxin oxidoreductase of Anabaena sp. PCC 7120: biochemical and spectroscopic characterization. J. Biol. Chem. 278:9219-9226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9219-9226
    • Frankenberg, N.1    Lagarias, J.C.2
  • 22
    • 0035032642 scopus 로고    scopus 로고
    • Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
    • DOI 10.1105/tpc.13.4.965
    • 22. Frankenberg, N., K. K. Mukougawa, and J. C. Lagarias. 2001. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13:965-978. (Pubitemid 32375914)
    • (2001) Plant Cell , vol.13 , Issue.4 , pp. 965-978
    • Frankenberg, N.1    Mukougawa, K.2    Kohchi, T.3    Lagarias, J.C.4
  • 23
    • 0018462850 scopus 로고
    • Mass-spectral identification and purification of phycoerythrobilin and phycocyanobilin
    • Fu, E., L. Friedman, and H. W. Siegelman. 1979. Mass-spectral identification and purification of phycoerythrobilin and phycocyanobilin. Biochem. J. 179:1-6.
    • (1979) Biochem. J. , vol.179 , pp. 1-6
    • Fu, E.1    Friedman, L.2    Siegelman, H.W.3
  • 24
    • 0023322812 scopus 로고
    • Allophycocyanin complexes of the phycobilisome from Mastigocladus laminosus - Influence of the linker polypeptide-L-8.9c on the spectral properties of the phycobiliprotein subunits
    • Fuglistaller, P., M. Mimuro, F. Suter, and H. Zuber. 1987. Allophycocyanin complexes of the phycobilisome from Mastigocladus laminosus - influence of the linker polypeptide-L-8.9c on the spectral properties of the phycobiliprotein subunits. Biol. Chem. Hoppe-Seyler 368:353-367.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 353-367
    • Fuglistaller, P.1    Mimuro, M.2    Suter, F.3    Zuber, H.4
  • 25
    • 61349086817 scopus 로고    scopus 로고
    • Functional biosynthesis of an allophycocyanin beta subunit in Escherichia coli
    • Ge, B., H. Sun, Y. Feng, J. Yang, and S. Qin. 2009. Functional biosynthesis of an allophycocyanin beta subunit in Escherichia coli. J. Biosci. Bioeng. 107:246-249.
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 246-249
    • Ge, B.1    Sun, H.2    Feng, Y.3    Yang, J.4    Qin, S.5
  • 27
    • 0024961673 scopus 로고
    • Light guides: Directional energy transfer in a photosynthetic antenna
    • Glazer, A. N. 1989. Light guides: directional energy transfer in a photosynthetic antenna. J. Biol. Chem. 264:1-4.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1-4
    • Glazer, A.N.1
  • 28
    • 0024202010 scopus 로고
    • Phycobiliproteins
    • Glazer, A. N. 1988 Phycobiliproteins. Methods Enzymol. 167:291-303.
    • (1988) Methods Enzymol. , vol.167 , pp. 291-303
    • Glazer, A.N.1
  • 29
    • 0016593468 scopus 로고
    • Allophycocyanin B (lambda max 671, 618 nm) - New cyanobacterial phycobiliprotein
    • Glazer, A. N., and D. A. Bryant. 1975. Allophycocyanin B (lambda max 671, 618 nm) - new cyanobacterial phycobiliprotein. Arch. Microbiol. 104:15-22.
    • (1975) Arch. Microbiol. , vol.104 , pp. 15-22
    • Glazer, A.N.1    Bryant, D.A.2
  • 30
    • 0016260827 scopus 로고
    • Isolation and characterization of allophycocyanin from the thermophilic blue-green alga Mastigocladus laminosus cohn
    • Gysi, J., and H. Zuber. 1974. Isolation and characterization of allophycocyanin from the thermophilic blue-green alga Mastigocladus laminosus cohn. FEBS Lett. 48:209-213.
    • (1974) FEBS Lett. , vol.48 , pp. 209-213
    • Gysi, J.1    Zuber, H.2
  • 31
    • 0018710509 scopus 로고
    • Properties of allophycocyanin II and its alpha- And beta-subunits from the thermophilic blue-green alga Mastigocladus laminosus
    • Gysi, J. R., and H. Zuber. 1979. Properties of allophycocyanin II and its alpha- and beta-subunits from the thermophilic blue-green alga Mastigocladus laminosus. Biochem. J. 181:577-583.
    • (1979) Biochem. J. , vol.181 , pp. 577-583
    • Gysi, J.R.1    Zuber, H.2
  • 32
    • 33646574960 scopus 로고    scopus 로고
    • Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp. isolate M097
    • Hou, Y. H., S. Qin, Y. X. Li, F. C. Li, H. Z. Xia, and F. Q. Zhao. 2006. Heterologous expression and purification of recombinant allophycocyanin in marine Streptomyces sp. isolate M097. World J. Microbiol. Biotechnol. 22:525-529.
    • (2006) World J. Microbiol. Biotechnol. , vol.22 , pp. 525-529
    • Hou, Y.H.1    Qin, S.2    Li, Y.X.3    Li, F.C.4    Xia, H.Z.5    Zhao, F.Q.6
  • 33
    • 33745055223 scopus 로고    scopus 로고
    • Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalytic bilin attachment
    • Hu, I. C., T. R. Lee, H. F. Lin, C. C. Chiueh, and P. C. Lyu. 2006. Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalytic bilin attachment. Biochemistiy 45:7092-7099.
    • (2006) Biochemistiy , vol.45 , pp. 7092-7099
    • Hu, I.C.1    Lee, T.R.2    Lin, H.F.3    Chiueh, C.C.4    Lyu, P.C.5
  • 35
    • 0023665403 scopus 로고
    • Gamma-N-methylasparagine in phycobiliproteins. occurrence, location, and biosynthesis
    • Klotz, A. V., and A. N. Glazer. 1987. Gamma-N-methylasparagine in phycobiliproteins. occurrence, location, and biosynthesis. J. Biol. Chem. 262:17350-17355.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17350-17355
    • Klotz, A.V.1    Glazer, A.N.2
  • 36
    • 0023024145 scopus 로고
    • Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin
    • Klotz, A. V., J. A. Leary, and A. N. Glazer. 1986. Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin. J. Biol. Chem. 261:15891-15894.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15891-15894
    • Klotz, A.V.1    Leary, J.A.2    Glazer, A.N.3
  • 37
    • 4344699140 scopus 로고    scopus 로고
    • Evolution of cyanobacterial and plant phytochromes
    • Lamparter, T. 2004. Evolution of cyanobacterial and plant phytochromes. FEBS Lett. 573:1-5.
    • (2004) FEBS Lett. , vol.573 , pp. 1-5
    • Lamparter, T.1
  • 39
    • 0019880685 scopus 로고
    • The relationship of the quaternary structure of allophycocyanin to its spectrum
    • MacColl, R., D. Csatorday, D. S. Berns, and E. Traeger. 1981. The relationship of the quaternary structure of allophycocyanin to its spectrum. Arch. Biochem. Biophys. 208:42-48.
    • (1981) Arch. Biochem. Biophys. , vol.208 , pp. 42-48
    • MacColl, R.1    Csatorday, D.2    Berns, D.S.3    Traeger, E.4
  • 40
    • 0024979196 scopus 로고
    • Spectroscopic studies of cyanobacterial phycobilisomes lacking core polypeptides
    • Maxson, P., K. Sauer, J. Zhou, D. A. Bryant, and A. N. Glazer. 1989. Spectroscopic studies of cyanobacterial phycobilisomes lacking core polypeptides. Biochim. Biophys. Acta 977:40-51.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 40-51
    • Maxson, P.1    Sauer, K.2    Zhou, J.3    Bryant, D.A.4    Glazer, A.N.5
  • 42
    • 0036676141 scopus 로고    scopus 로고
    • Phytochrome ancestry: Sensors of bilins and light
    • DOI 10.1016/S1360-1385(02)02304-X, PII S136013850202304X
    • 42. Montgomery, B., and J. Lagarias. 2002. Fhytochrome ancestry: sensors of bilins and light. Trends Plant Sci. 7:357-366. (Pubitemid 36726503)
    • (2002) Trends in Plant Science , vol.7 , Issue.8 , pp. 357-366
    • Montgomery, B.L.1    Lagarias, J.C.2
  • 44
    • 46849086738 scopus 로고    scopus 로고
    • A second conserved GAF domain cysteine is required for the blue/green photoreversibility of cyanobacteriochrome Tlr0924 from Thermosynechococcus elongatus
    • Rockwell, N. C., S. L. Njuguna, L. Roberts, E. Castillo, V. L. Parson, S. Dwojak, J. C. Lagarias, and S. C. Spiller. 2008. A second conserved GAF domain cysteine is required for the blue/green photoreversibility of cyanobacteriochrome Tlr0924 from Thermosynechococcus elongatus. Biochemistry 47:7304-7316.
    • (2008) Biochemistry , vol.47 , pp. 7304-7316
    • Rockwell, N.C.1    Njuguna, S.L.2    Roberts, L.3    Castillo, E.4    Parson, V.L.5    Dwojak, S.6    Lagarias, J.C.7    Spiller, S.C.8
  • 45
    • 38249035074 scopus 로고
    • γ-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix
    • Rümbeli, R., F. Suter, M. Wirth, W. Sidler, and H. Zuber. 1987. γ-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix. FEBS Lett. 221:1-2.
    • (1987) FEBS Lett. , vol.221 , pp. 1-2
    • Rümbeli, R.1    Suter, F.2    Wirth, M.3    Sidler, W.4    Zuber, H.5
  • 46
    • 41049116313 scopus 로고    scopus 로고
    • Biogenesis of phycobiliproteins. II. CpcS-I and CpcU comprise the heterodimeric bilin lyase that attaches phycocyanobilin to Cys-82 of beta-phy- Cocyanin and Cys-81 of allophycocyanin subunits in Synechococcus sp. PCC 7002
    • Saunée, N. A., S. R. Williams, D. A. Bryant, and W. M. Schluchter. 2008. Biogenesis of phycobiliproteins. II. CpcS-I and CpcU comprise the heterodimeric bilin lyase that attaches phycocyanobilin to Cys-82 of beta-phy- cocyanin and Cys-81 of allophycocyanin subunits in Synechococcus sp. PCC 7002. J. Biol. Chem. 283:7513-7522.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7513-7522
    • Saunée, N.A.1    Williams, S.R.2    Bryant, D.A.3    Schluchter, W.M.4
  • 47
    • 33845353161 scopus 로고    scopus 로고
    • The pigments
    • B. R. Green and W. W. Parson (ed.), Kluwer Academic Publishers, Dordrecht, Netherlands
    • Scheer, H. 2003. The pigments, p. 29-81. In B. R. Green and W. W. Parson (ed.), Light-harvesting antennas in photosynthesis, vol.13. Kluwer Academic Publishers, Dordrecht, Netherlands.
    • (2003) Light-harvesting Antennas in Photosynthesis , vol.13 , pp. 29-81
    • Scheer, H.1
  • 48
    • 77951607522 scopus 로고    scopus 로고
    • Phycocyanobilin-CpeS lyase complex, an intermediate for phycobiliprotein chromophorylation
    • Scheer, H., K. Zhao, J. Tu, J. Zhang, M. Kupka, M. Zhou, and S. Bohm. 2007. Phycocyanobilin-CpeS lyase complex, an intermediate for phycobiliprotein chromophorylation. Photosynth. Res. 91:207.
    • (2007) Photosynth. Res. , vol.91 , pp. 207
    • Scheer, H.1    Zhao, K.2    Tu, J.3    Zhang, J.4    Kupka, M.5    Zhou, M.6    Bohm, S.7
  • 49
    • 41049108095 scopus 로고    scopus 로고
    • Biliprotein maturation: The chromophore attachment
    • Scheer, H., and K. H. Zhao. 2008. Biliprotein maturation: the chromophore attachment. Mol. Microbiol. 68:263-276.
    • (2008) Mol. Microbiol. , vol.68 , pp. 263-276
    • Scheer, H.1    Zhao, K.H.2
  • 50
    • 0023053285 scopus 로고
    • Crystal structure analysis and refinement at 2.5 Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadmplicatum: The molecular model and its implications from light-harvesting
    • Schirmer, T., R. Huber, M. Schneider, W. Bode, M. Miller, and M. L. Hackert. 1986. Crystal structure analysis and refinement at 2.5 Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadmplicatum: the molecular model and its implications from light-harvesting. J. Mol. Biol. 188:651-676.
    • (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
  • 51
    • 47249163806 scopus 로고    scopus 로고
    • CpcM post-translationally methylates asparagine-71/72 of phycobiliprotein beta subunits in Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803
    • Shen, G., H. S. Leonard, W. M. Schluchter, and D. A. Bryant. 2008. CpcM post-translationally methylates asparagine-71/72 of phycobiliprotein beta subunits in Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803. J. Bacteriol. 190:4808-4817.
    • (2008) J. Bacteriol. , vol.190 , pp. 4808-4817
    • Shen, G.1    Leonard, H.S.2    Schluchter, W.M.3    Bryant, D.A.4
  • 52
    • 33745853781 scopus 로고    scopus 로고
    • Identification and characterization of a new class of bilin lyase: The cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta subunit of phycocyanin in Synechococcus sp. PCC 7002
    • Shen, G., N. A. Saunee, S. R. Williams, E. F. Gallo, W. M. Schluchter, and D. A. Bryant. 2006. Identification and characterization of a new class of bilin lyase: the cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta subunit of phycocyanin in Synechococcus sp. PCC 7002. J. Biol. Chem. 281:17768-17778.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17768-17778
    • Shen, G.1    Saunee, N.A.2    Williams, S.R.3    Gallo, E.F.4    Schluchter, W.M.5    Bryant, D.A.6
  • 53
    • 41049105972 scopus 로고    scopus 로고
    • Biogenesis of phycobiliproteins. I. cpcS-I and cpcU mutants of the cyanobacterium Synechococcus sp. PCC 7002 define a heterodimeric phycocaynobilin lyase specific for beta-phycocyanin and allophycocyanin subunits
    • Shen, G., W. M. Schluchter, and D. A. Bryant. 2008. Biogenesis of phycobiliproteins. I. cpcS-I and cpcU mutants of the cyanobacterium Synechococcus sp. PCC 7002 define a heterodimeric phycocaynobilin lyase specific for beta-phycocyanin and allophycocyanin subunits. J. Biol. Chem. 28:7503-7512.
    • (2008) J. Biol. Chem. , vol.28 , pp. 7503-7512
    • Shen, G.1    Schluchter, W.M.2    Bryant, D.A.3
  • 54
    • 0003123963 scopus 로고
    • Phycobilisome and phycobiliprotein structure
    • D. A. Bryant (ed.), Kluwer Academic, Dordrecht, Netherlands
    • Sidler, W. A. 1994. Phycobilisome and phycobiliprotein structure, p. 139-216. In D. A. Bryant (ed.), The molecular biology of cyanobacteria, vol.1. Kluwer Academic, Dordrecht, Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , vol.1 , pp. 139-216
    • Sidler, W.A.1
  • 56
    • 0035899996 scopus 로고    scopus 로고
    • Chromophore attachment to biliproteins: Specificity of PecE/PecF, a lyase-isomerase for the photoactive 3(1)-cys-alpha 84-phycoviolobilin chromophore of phycoerythrocyanin
    • Storf, M., A. Parbel, M. Meyer, B. Strohmann, H. Scheer, M. G. Deng, M. Zheng, M. Zhou, and K. H. Zhao. 2001. Chromophore attachment to biliproteins: specificity of PecE/PecF, a lyase-isomerase for the photoactive 3(1)-cys-alpha 84-phycoviolobilin chromophore of phycoerythrocyanin. Biochemistry 40:12444-12456.
    • (2001) Biochemistry , vol.40 , pp. 12444-12456
    • Storf, M.1    Parbel, A.2    Meyer, M.3    Strohmann, B.4    Scheer, H.5    Deng, M.G.6    Zheng, M.7    Zhou, M.8    Zhao, K.H.9
  • 57
    • 0025046568 scopus 로고
    • Phycobiliprotein methylation: Effect of the γ-N-methylasparagine residue on energy transfer in phycocyanin and the phycobilisome
    • Swanson, R., and A. Glazer. 1990. Phycobiliprotein methylation: effect of the γ-N-methylasparagine residue on energy transfer in phycocyanin and the phycobilisome. J. Mol. Biol. 214:787-796.
    • (1990) J. Mol. Biol. , vol.214 , pp. 787-796
    • Swanson, R.1    Glazer, A.2
  • 58
    • 0026775908 scopus 로고
    • Characterization of phycocyanin produced by cpcE and cpcF mutants and identification of an intergenic suppressor of the defect in bilin attachment
    • Swanson, R. V., J. Zhou, J. A. Leary, T. Williams, R. de Lorimier, D. A. Bryant, and A. N. Glazer. 1992. Characterization of phycocyanin produced by cpcE and cpcF mutants and identification of an intergenic suppressor of the defect in bilin attachment. J. Biol. Chem. 267:16146-16154.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16146-16154
    • Swanson, R.V.1    Zhou, J.2    Leary, J.A.3    Williams, T.4    De Lorimier, R.5    Bryant, D.A.6    Glazer, A.N.7
  • 59
    • 0027191448 scopus 로고
    • Fost-translational methylation of phycobilisomes and oxygen evolution efficiency in cyanobacteria
    • Thomas, B. A., T. M. Bricker, and A. V. Klotz. 1993. Fost-translational methylation of phycobilisomes and oxygen evolution efficiency in cyanobacteria. Biochim. Biophys. Acta 1143:104-108.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 104-108
    • Thomas, B.A.1    Bricker, T.M.2    Klotz, A.V.3
  • 60
    • 77951613850 scopus 로고
    • Gamma-N-methylasparagine - A posttradiational modification that improves energy-transfer efficiency in phycobiliproteins
    • Thomas, B. A., L. P. McMahon, and A. V. Klotz. 1994. Gamma-N- methylasparagine - a posttradiational modification that improves energy-transfer efficiency in phycobiliproteins Biophys. J. 66:A164-A164.
    • (1994) Biophys. J. , vol.66
    • Thomas, B.A.1    McMahon, L.P.2    Klotz, A.V.3
  • 61
    • 0035845538 scopus 로고    scopus 로고
    • Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-α subunit in a heterologous host
    • Tooley, A., Y. Cai, and A. Glazer. 2001. Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-α subunit in a heterologous host. Proc. Natl. Acad. Sci. U. S. A. 98:10560-10565.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10560-10565
    • Tooley, A.1    Cai, Y.2    Glazer, A.3
  • 62
    • 0036719288 scopus 로고    scopus 로고
    • Biosynthesis of the cyanobacterial light- Harvesting polypeptide phycoerythrocyanin holo-alpha subunit in a heterologous host
    • Tooley, A., and A. Glazer. 2002. Biosynthesis of the cyanobacterial light- harvesting polypeptide phycoerythrocyanin holo-alpha subunit in a heterologous host. J. Bacteriol. 184:4666-4671.
    • (2002) J. Bacteriol. , vol.184 , pp. 4666-4671
    • Tooley, A.1    Glazer, A.2
  • 64
    • 0029910197 scopus 로고    scopus 로고
    • Cryptomonad biliproteins: Bilin types and locations
    • Wedemayer, G. J., D. G. Kidd, and A. N. Glazer. 1996. Cryptomonad biliproteins: bilin types and locations. Photosynth. Res. 48:163-170.
    • (1996) Photosynth. Res. , vol.48 , pp. 163-170
    • Wedemayer, G.J.1    Kidd, D.G.2    Glazer, A.N.3
  • 65
    • 0024978592 scopus 로고
    • Postranslational modifications of the beta-subunit of a cryptomonad phycoerythrin - Sites of bilin attachment and asparagine methylation
    • Wilbanks, S. M., G. J. Wedemayer, and A. N. Glazer. 1989. Postranslational modifications of the beta-subunit of a cryptomonad phycoerythrin - sites of bilin attachment and asparagine methylation. J. Biol. Chem. 264:17860-17867.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17860-17867
    • Wilbanks, S.M.1    Wedemayer, G.J.2    Glazer, A.N.3
  • 66
    • 0034619430 scopus 로고    scopus 로고
    • Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily
    • Wu, S.-H., and J. C. Lagarias. 2000. Defining the bilin lyase domain: lessons from the extended phytochrome superfamily. Biochemistry 39:13487-13495.
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.-H.1    Lagarias, J.C.2
  • 67
    • 0029829267 scopus 로고    scopus 로고
    • The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome
    • Wu, S.-H., and J. C. Lagarias. 1996. The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome. Proc. Natl. Acad. Sci. U. S. A. 93:8989-8994.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8989-8994
    • Wu, S.-H.1    Lagarias, J.C.2
  • 68
    • 42549113974 scopus 로고    scopus 로고
    • Combinational biosynthesis of a fluorescent cyanobacterial holo-alpha-allophycocyanin in Escherichia coli
    • Yang, Y., B. S. Ge, X. Y. Guan, W. J. Zhang, and S. Qin. 2008. Combinational biosynthesis of a fluorescent cyanobacterial holo-alpha- allophycocyanin in Escherichia coli. Biotechnol. Lett. 30:1001-1004.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 1001-1004
    • Yang, Y.1    Ge, B.S.2    Guan, X.Y.3    Zhang, W.J.4    Qin, S.5
  • 69
    • 60549112892 scopus 로고    scopus 로고
    • Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalysis in Escherichia coli
    • Zhang, W. J., X. Y. Guan, Y. Yang, B. S. Ge, H. X. Chen, F. C. Li, and S. Qin. 2009. Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalysis in Escherichia coli. Biotechnol. Appl. Biochem. 52:135-140.
    • (2009) Biotechnol. Appl. Biochem. , vol.52 , pp. 135-140
    • Zhang, W.J.1    Guan, X.Y.2    Yang, Y.3    Ge, B.S.4    Chen, H.X.5    Li, F.C.6    Qin, S.7
  • 70
    • 0035371686 scopus 로고    scopus 로고
    • Photosystem stoichiometry and state transitions in a mutant of the cyanobacterium Synechococcus sp. PCC 7002 lacking phycocyanin
    • Zhao, J., G. Shen, and D. A. Bryant. 2001. Photosystem stoichiometry and state transitions in a mutant of the cyanobacterium Synechococcus sp. PCC 7002 lacking phycocyanin. Biochim. Biophys. Acta 1505:248-257.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 248-257
    • Zhao, J.1    Shen, G.2    Bryant, D.A.3
  • 71
    • 0002765159 scopus 로고
    • Energy transfer processes in phycobilisomes as deduced from analyses of mutants of Synechococcus sp. PCC 7002
    • N. Murata (ed.), Kluwer, Dordrecht, Netherlands
    • Zhao, J., J. Zhou, and D. A. Bryant. 1992. Energy transfer processes in phycobilisomes as deduced from analyses of mutants of Synechococcus sp. PCC 7002, p. 25-32. In N. Murata (ed.), Research in photosynthesis, vol.I. Kluwer, Dordrecht, Netherlands.
    • (1992) Research in Photosynthesis , vol.I , pp. 25-32
    • Zhao, J.1    Zhou, J.2    Bryant, D.A.3
  • 72
    • 35448978371 scopus 로고    scopus 로고
    • Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins
    • Zhao, K., P. Su, J. Tu, X. Wang, H. Liu, M. Ploscher, L. Eichacker, B. Yang, M. Zhou, and H. Scheer. 2007. Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins. Proc. Natl. Acad. Sci. U. S. A. 104:14300-14305.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 14300-14305
    • Zhao, K.1    Su, P.2    Tu, J.3    Wang, X.4    Liu, H.5    Ploscher, M.6    Eichacker, L.7    Yang, B.8    Zhou, M.9    Scheer, H.10
  • 73
    • 0034598956 scopus 로고    scopus 로고
    • Novel activity of a phycobiliprotein lyase: Both the attachment of phycocyanobilin and the isomerization to phycobiliviolin are catalyzed by the proteins PecE and PecF encoded by the phycoerythrocyanin operan
    • Zhao, K. H., M. G. Deng, M. Zheng, M. Zhou, A. Parbel, M. Storf, M. Meyer, B. Strohmann, and H. Scheer. 2000. Novel activity of a phycobiliprotein lyase: both the attachment of phycocyanobilin and the isomerization to phycobiliviolin are catalyzed by the proteins PecE and PecF encoded by the phycoerythrocyanin operan. FEBS Lett. 469:9-13.
    • (2000) FEBS Lett. , vol.469 , pp. 9-13
    • Zhao, K.H.1    Deng, M.G.2    Zheng, M.3    Zhou, M.4    Parbel, A.5    Storf, M.6    Meyer, M.7    Strohmann, B.8    Scheer, H.9
  • 74
    • 11144306461 scopus 로고    scopus 로고
    • Reconstitution of phycobilisome core-membrane linkerL-CM, by autocatalytic chromophore binding to ApcE
    • Zhao, K. H., S. Ping, S. Bohm, S. Bo, Z. Ming, C. Bubenzer, and H. Scheer. 2005. Reconstitution of phycobilisome core-membrane linker, L-CM, by autocatalytic chromophore binding to ApcE. Biochim. Biophys. Acta Bioenerget. 1706:81-87.
    • (2005) Biochim. Biophys. Acta Bioenerget. , Issue.1706 , pp. 81-87
    • Zhao, K.H.1    Ping, S.2    Bohm, S.3    Bo, S.4    Ming, Z.5    Bubenzer, C.6    Scheer, H.7
  • 75
    • 33646828526 scopus 로고    scopus 로고
    • Chromophore attachment to phycobiliprotein beta-subunits: Phycocyanobilin:cystein-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena sp. PCC7120
    • Zhao, K. H., P. Su, J. Li, J. M. Tu, M. Zhou, C. Bubenzer, and H. Scheer. 2006. Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cystein-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena sp. PCC7120. J. Biol. Chem. 281:8573-8581.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8573-8581
    • Zhao, K.H.1    Su, P.2    Li, J.3    Tu, J.M.4    Zhou, M.5    Bubenzer, C.6    Scheer, H.7
  • 76
    • 36348955171 scopus 로고    scopus 로고
    • Lyase activities of CpcSand CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits
    • Zhao, K. H., J. Zhang, J. M. Tu, S. Boehm, M. Ploescher, L. Eichacker, C. Bubenzer, H. Scheer, X. Wang, and M. Zhou. 2007. Lyase activities of CpcSand CpcT-like proteins from Nostoc PCC7120 and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin beta-subunits. J. Biol. Chem. 282:34093-34103.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34093-34103
    • Zhao, K.H.1    Zhang, J.2    Tu, J.M.3    Boehm, S.4    Ploescher, M.5    Eichacker, L.6    Bubenzer, C.7    Scheer, H.8    Wang, X.9    Zhou, M.10
  • 77
    • 3242705066 scopus 로고    scopus 로고
    • Nonenzymatic chromophore attachment in biliproteins: Conformational control by the detergent Triton X-100
    • Zhao, K. H., J. P. Zhu, B. Song, M. Zhou, M. Storf, S. Bohm, C. Bubenzer, and H. Scheer. 2004. Nonenzymatic chromophore attachment in biliproteins: conformational control by the detergent Triton X-100. Biochim. Biophys. Acta 1657:131-145.
    • (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    Bohm, S.6    Bubenzer, C.7    Scheer, H.8
  • 78
    • 0026784532 scopus 로고
    • The cpcE and cpcF genes of Synechococcus sp. PCC 7002: Construction and phenotypic characterization of interposon mutants
    • Zhou, J., G. E. Gasparich, V. L. Stirewalt, R. de Lorimier, and D. A. Bryant. 1992. The cpcE and cpcF genes of Synechococcus sp. PCC 7002: construction and phenotypic characterization of interposon mutants. J. Biol. Chem. 267:16138-16145.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16138-16145
    • Zhou, J.1    Gasparich, G.E.2    Stirewalt, V.L.3    De Lorimier, R.4    Bryant, D.A.5


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