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Volumn 186, Issue 21, 2004, Pages 7420-7428

AplA, a member of a new class of phycobiliproteins lacking a traditional role in photosynthetic light harvesting

Author keywords

[No Author keywords available]

Indexed keywords

ALLOPHYCOCYANIN; AMINO ACID; DIMER; PHYCOBILIPROTEIN; PROTEIN APLA; UNCLASSIFIED DRUG;

EID: 6044223542     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.21.7420-7428.2004     Document Type: Article
Times cited : (16)

References (53)
  • 4
    • 0242606199 scopus 로고    scopus 로고
    • CotB is essential for complete activation of green light-induced genes during complementary chromatic adaptation in Fremyella diplosiphon
    • Balabas, B. E., B. L. Montgomery, L. E. Ong, and D. M. Kehoe. 2003. CotB is essential for complete activation of green light-induced genes during complementary chromatic adaptation in Fremyella diplosiphon. Mol. Microbiol. 50:781-793.
    • (2003) Mol. Microbiol. , vol.50 , pp. 781-793
    • Balabas, B.E.1    Montgomery, B.L.2    Ong, L.E.3    Kehoe, D.M.4
  • 6
    • 0031006022 scopus 로고    scopus 로고
    • One century of protein crystallography, the phycobiliproteins
    • Betz, M. 1997. One century of protein crystallography, the phycobiliproteins. Biol. Chem. 378:167-176.
    • (1997) Biol. Chem. , vol.378 , pp. 167-176
    • Betz, M.1
  • 8
    • 0027210117 scopus 로고
    • Spatial expression and auto-regulation of hetR. A gene involved in the control of heterocyst development in Anabaena
    • Black, T. A., Y. P. Cai, and C. P. Wolk. 1993. Spatial expression and auto-regulation of hetR. a gene involved in the control of heterocyst development in Anabaena. Mol. Microbiol. 9:77-84.
    • (1993) Mol. Microbiol. , vol.9 , pp. 77-84
    • Black, T.A.1    Cai, Y.P.2    Wolk, C.P.3
  • 9
    • 0029037179 scopus 로고
    • Isolation, crystallization, crystal-structure analysis and refinement of allophycocyanin from the cyanobacterium Spindina 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 Spindina platensis at 2.3 Å resolution. J. Mol. Biol. 249:424-40.
    • (1995) J. Mol. Biol. , vol.249 , pp. 424-440
    • Brejc, K.1    Ficner, R.2    Huber, R.3    Steinbacher, S.4
  • 10
    • 0025311083 scopus 로고
    • Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences
    • Cai, Y., and C. P. Wolk. 1990. Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences. J. Bacteriol. 172:3138-3145.
    • (1990) J. Bacteriol. , vol.172 , pp. 3138-3145
    • Cai, Y.1    Wolk, C.P.2
  • 11
    • 0030854071 scopus 로고    scopus 로고
    • Suppression of mutants aberrant in light intensity responses of complementary chromatic adaptation
    • Casey, E. S., D. M. Kehoe, and A. R. Grossman. 1997. Suppression of mutants aberrant in light intensity responses of complementary chromatic adaptation. J. Bacteriol. 179:4599-4606.
    • (1997) J. Bacteriol. , vol.179 , pp. 4599-4606
    • Casey, E.S.1    Kehoe, D.M.2    Grossman, A.R.3
  • 12
    • 0036016816 scopus 로고    scopus 로고
    • CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the cyanobacterium fremyella diplosiphon and is encoded in the phycoerythrin linker-polypeptide operon (cpeCDESTR)
    • Cobley, J. G., A. C. Clark, S. Weerasurya, F. A. Queseda, J. Y. Xiao, N. Bandrapali, I. D'Silva, M. Thounaojam, J. F. Oda, T. Sumiyoshi, and M. H. Chu. 2002. CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the cyanobacterium fremyella diplosiphon and is encoded in the phycoerythrin linker-polypeptide operon (cpeCDESTR). Mol. Microbiol. 44:1517-1531.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1517-1531
    • Cobley, J.G.1    Clark, A.C.2    Weerasurya, S.3    Queseda, F.A.4    Xiao, J.Y.5    Bandrapali, N.6    D'Silva, I.7    Thounaojam, M.8    Oda, J.F.9    Sumiyoshi, T.10    Chu, M.H.11
  • 13
    • 0027209903 scopus 로고
    • Construction of shuttle plasmids which can be efficiently mobilized from Escherichia coli into the chromatically adapting cyanobacterium, Fremyella diplosiphon
    • Cobley, J. G., and R. D. Miranda. 1993. Construction of shuttle plasmids which can be efficiently mobilized from Escherichia coli into the chromatically adapting cyanobacterium, Fremyella diplosiphon. Plasmid 30:90-105.
    • (1993) Plasmid , vol.30 , pp. 90-105
    • Cobley, J.G.1    Miranda, R.D.2
  • 14
    • 0026703943 scopus 로고
    • Chlorosis induced by nutrient deprivation in Synechococcus sp. strain PCC 7942: Not all bleaching is the same
    • Collier, J. L., and A. R. Grossman. 1992. Chlorosis induced by nutrient deprivation in Synechococcus sp. strain PCC 7942: not all bleaching is the same. J. Bacteriol. 174:4718-4726.
    • (1992) J. Bacteriol. , vol.174 , pp. 4718-4726
    • Collier, J.L.1    Grossman, A.R.2
  • 15
    • 0024999332 scopus 로고
    • Improved detection of helix-turn-helix DNA-binding motifs in protein sequences
    • Dodd, I. B., and J. B. Egan. 1990. Improved detection of helix-turn-helix DNA-binding motifs in protein sequences. Nucleic Acids Res. 18:5019-5026.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5019-5026
    • Dodd, I.B.1    Egan, J.B.2
  • 16
    • 0026674274 scopus 로고
    • Characterization of a light-regulated gene encoding a new phycoerythrin-associated linker protein from the cyanobacterium Fremyella diplosiphon
    • Federspiel, N. A., and L. Scott. 1992. Characterization of a light-regulated gene encoding a new phycoerythrin-associated linker protein from the cyanobacterium Fremyella diplosiphon. J. Bacteriol. 174:5994-5998.
    • (1992) J. Bacteriol. , vol.174 , pp. 5994-5998
    • Federspiel, N.A.1    Scott, L.2
  • 17
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition: Combining sequence derived properties with evolutionary information
    • World Scientific, Honolulu, Hawaii
    • Fischer, D. 2000. Hybrid fold recognition: combining sequence derived properties with evolutionary information, p. 119-130. In Proceedings of the Pacific Symposium on Biocomputing 2000. World Scientific, Honolulu, Hawaii.
    • (2000) Proceedings of the Pacific Symposium on Biocomputing 2000 , pp. 119-130
    • Fischer, D.1
  • 18
    • 0029874551 scopus 로고    scopus 로고
    • Protein fold recognition using sequence-derived predictions
    • Fischer, D., and D. Eisenberg. 1996. Protein fold recognition using sequence-derived predictions. Protein Sci. 5:947-955.
    • (1996) Protein Sci. , vol.5 , pp. 947-955
    • Fischer, D.1    Eisenberg, D.2
  • 20
    • 0026705171 scopus 로고
    • Core mutations of Synechococcus sp. PCC 7002 phycobilisomes: A spectroscopic study
    • Gindt, Y. M., J. H. Zhou, D. A. Bryant, and K. Sauer. 1992. Core mutations of Synechococcus sp. PCC 7002 phycobilisomes: a spectroscopic study. J. Photochem. Photobiol. B 15:75-89.
    • (1992) J. Photochem. Photobiol. B , vol.15 , pp. 75-89
    • Gindt, Y.M.1    Zhou, J.H.2    Bryant, D.A.3    Sauer, K.4
  • 21
  • 22
    • 0026547479 scopus 로고
    • Three C-phycoerythrin-associated linker polypeptides in the phycobilisome of green-light-grown Calothrix sp. PCC 7601 (cyanobacteria)
    • Glauser, M., W. A. Sidler, K. W. Graham, D. A. Bryant, G. Frank, E. Wehrli, and H. Zuber. 1992. Three C-phycoerythrin-associated linker polypeptides in the phycobilisome of green-light-grown Calothrix sp. PCC 7601 (cyanobacteria). FEES Lett. 297:19-23.
    • (1992) FEES Lett. , vol.297 , pp. 19-23
    • Glauser, M.1    Sidler, W.A.2    Graham, K.W.3    Bryant, D.A.4    Frank, G.5    Wehrli, E.6    Zuber, H.7
  • 23
    • 0002271831 scopus 로고
    • Phycobilisome. A macromolecular complex optimized for light energy transfer
    • Glazer, A. N. 1984. Phycobilisome. A macromolecular complex optimized for light energy transfer. Biochim. Biophys. Acta 768:29-51.
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 29-51
    • Glazer, A.N.1
  • 24
    • 0016593468 scopus 로고
    • max 671,618 nm). A new cyanobacterial phycobiliprotein
    • max 671,618 nm). A new cyanobacterial phycobiliprotein. Arch. Microbiol. 104:15-22.
    • (1975) Arch. Microbiol. , vol.104 , pp. 15-22
    • Glazer, A.N.1    Bryant, D.A.2
  • 25
    • 0029559935 scopus 로고
    • Light-harvesting complexes in oxygenic photosynthesis: Diversity, control, and evolution
    • Grossman, A. R., D, Bhaya, K. E. Apt, and D. M. Kehoe. 1995. Light-harvesting complexes in oxygenic photosynthesis: diversity, control, and evolution. Annu. Rev. Genet. 291:231-288.
    • (1995) Annu. Rev. Genet. , vol.291 , pp. 231-288
    • Grossman, A.R.1    Bhaya, D.2    Apt, K.E.3    Kehoe, D.M.4
  • 28
    • 0024195534 scopus 로고
    • Genes encoding core components of the phycobilisome in the cyanobacterium Calothrix sp. strain PCC 7601: Occurrence of a multigene family
    • Houmard, J., V. Capuano, T. Coursin, and N. Tandeau de Marsac. 1988. Genes encoding core components of the phycobilisome in the cyanobacterium Calothrix sp. strain PCC 7601: occurrence of a multigene family. J. Bacteriol. 170:5512-5521.
    • (1988) J. Bacteriol. , vol.170 , pp. 5512-5521
    • Houmard, J.1    Capuano, V.2    Coursin, T.3    Tandeau De Marsac, N.4
  • 29
    • 0023754639 scopus 로고
    • Isolation and molecular characterization of the gene encoding allophycocyanin B, a terminal energy acceptor in cyanobacterial phycobilisomes
    • Houmard, J., V. Capuano, T. Coursin, and N. Tandeau de Marsac. 1988. Isolation and molecular characterization of the gene encoding allophycocyanin B, a terminal energy acceptor in cyanobacterial phycobilisomes. Mol. Microbiol. 2:101-107.
    • (1988) Mol. Microbiol. , vol.2 , pp. 101-107
    • Houmard, J.1    Capuano, V.2    Coursin, T.3    Tandeau De Marsac, N.4
  • 30
    • 0028526272 scopus 로고
    • Complementary chromatic adaptation: Photoperception to gene regulation
    • Kehoe, D. M., and A. R. Grossman. 1994. Complementary chromatic adaptation: photoperception to gene regulation. Semin. Cell Biol. 5:303-313.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 303-313
    • Kehoe, D.M.1    Grossman, A.R.2
  • 31
    • 0030912553 scopus 로고    scopus 로고
    • New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system
    • Kehoe, D. M., and A. R. Grossman. 1997. New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system. J. Bacteriol. 179:3914-3921.
    • (1997) J. Bacteriol. , vol.179 , pp. 3914-3921
    • Kehoe, D.M.1    Grossman, A.R.2
  • 32
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe, D. M., and A. R. Grossman. 1996. Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 273:1409-1412.
    • (1996) Science , vol.273 , pp. 1409-1412
    • Kehoe, D.M.1    Grossman, A.R.2
  • 33
    • 0031721898 scopus 로고    scopus 로고
    • Use of molecular genetics to investigate complementary chromatic adaptation: Advances in transformation and complementation
    • Kehoe, D. M., and A. R. Grossman. 1998. Use of molecular genetics to investigate complementary chromatic adaptation: advances in transformation and complementation. Methods Enzymol. 297:279-290.
    • (1998) Methods Enzymol. , vol.297 , pp. 279-290
    • Kehoe, D.M.1    Grossman, A.R.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0026649545 scopus 로고
    • Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility
    • Li, L., and J. C. Lagarias. 1992. Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility. J. Biol. Chem. 267:19204-19210.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19204-19210
    • Li, L.1    Lagarias, J.C.2
  • 37
    • 0020683752 scopus 로고
    • Molecular architecture of a light-harvesting antenna. Core substructure in Synechococcus 6301 phycobilisomes: Two new allophycocyanin and allophycocyanin B complexes
    • Lundell, D. J., and A. N. Glazer. 1983. Molecular architecture of a light-harvesting antenna. Core substructure in Synechococcus 6301 phycobilisomes: two new allophycocyanin and allophycocyanin B complexes. J. Biol. Chem. 258:902-908.
    • (1983) J. Biol. Chem. , vol.258 , pp. 902-908
    • Lundell, D.J.1    Glazer, A.N.2
  • 38
    • 0020697111 scopus 로고
    • Molecular architecture of a light-harvesting antenna. Structure of the 18 S core-rod subassembly of the Synechococcus 6301 phycobilisome
    • Lundell, D. J., and A. N. Glazer. 1983. Molecular architecture of a light-harvesting antenna. Structure of the 18 S core-rod subassembly of the Synechococcus 6301 phycobilisome. J. Biol. Chem. 258:894-901.
    • (1983) J. Biol. Chem. , vol.258 , pp. 894-901
    • Lundell, D.J.1    Glazer, A.N.2
  • 39
    • 0024979196 scopus 로고
    • Spectroscopic studies of cyanobacterial phycobilisomes lacking core polypeptides
    • Maxson, P., K. Sauer, J. H. 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.H.3    Bryant, D.A.4    Glazer, A.N.5
  • 40
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi, K., C. M. Deane, T. L. Blundell, and J. P. Overington. 1998. HOMSTRAD: a database of protein structure alignments for homologous families. Protein Sci. 7:2469-2471.
    • (1998) Protein Sci. , vol.7 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 42
    • 0036154464 scopus 로고    scopus 로고
    • A turquoise mutant genetically separates expression of genes encoding phycoerythrin and its associated linker peptides
    • Seib, L. O., and D. M. Kehoe. 2002. A turquoise mutant genetically separates expression of genes encoding phycoerythrin and its associated linker peptides. J. Bacteriol. 184:962-970.
    • (2002) J. Bacteriol. , vol.184 , pp. 962-970
    • Seib, L.O.1    Kehoe, D.M.2
  • 43
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi, J. Y., T. L. Blundell, and K. Mizuguchi. 2001. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310:243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.Y.1    Blundell, T.L.2    Mizuguchi, K.3
  • 44
    • 0003123963 scopus 로고
    • Phycobilisome and phycobiliprotein structures
    • D. A. Bryant (ed.). Kluwer, Dordrecht, The Netherlands
    • Sidler, W. A. 1994. Phycobilisome and phycobiliprotein structures, p. 139-216. In D. A. Bryant (ed.), The molecular biology of cyanobacteria. Kluwer, Dordrecht, The Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 139-216
    • Sidler, W.A.1
  • 45
    • 0041696940 scopus 로고    scopus 로고
    • Analysis of natural populations of Prochlorococcus spp. in the northern Red Sea using phycoerythrin gene sequences
    • Steglich, C., A. F. Post, and W. R. Hess. 2003. Analysis of natural populations of Prochlorococcus spp. in the northern Red Sea using phycoerythrin gene sequences. Environ. Microbiol. 5:681-690.
    • (2003) Environ. Microbiol. , vol.5 , pp. 681-690
    • Steglich, C.1    Post, A.F.2    Hess, W.R.3
  • 46
    • 0023268175 scopus 로고
    • Amino acid sequences of α-allophycocyanin B from Synechococcus 6301 and Mastigodadus laminosus
    • Suter, F., P. Fuglistaller, D. J. Lundell, A. N. Glazer, and H. Zuber. 1987. Amino acid sequences of α-allophycocyanin B from Synechococcus 6301 and Mastigodadus laminosus. FEBS Lett. 217:279-282.
    • (1987) FEBS Lett. , vol.217 , pp. 279-282
    • Suter, F.1    Fuglistaller, P.2    Lundell, D.J.3    Glazer, A.N.4    Zuber, H.5
  • 47
    • 0017371255 scopus 로고
    • Occurrence and nature of chromatic adaptation in cyanobacteria
    • Tandeau de Marsac, N. 1977. Occurrence and nature of chromatic adaptation in cyanobacteria. J. Bacteriol. 130:82-91.
    • (1977) J. Bacteriol. , vol.130 , pp. 82-91
    • Tandeau De Marsac, N.1
  • 48
    • 0000774691 scopus 로고
    • Phycobilisomes and complementary chromatic adaptation in cyanobacteria
    • Tandeau de Marsac, N. 1983. Phycobilisomes and complementary chromatic adaptation in cyanobacteria. Bull. Inst. Pasteur 81:201-254.
    • (1983) Bull. Inst. Pasteur , vol.81 , pp. 201-254
    • Tandeau De Marsac, N.1
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0020490516 scopus 로고
    • Molecular architecture of a light-harvesting antenna. Isolation and characterization of phycobilisome subassembly particles
    • Yamanaka, G., D. J. Lundell, and A. N. Glazer. 1982. Molecular architecture of a light-harvesting antenna. Isolation and characterization of phycobilisome subassembly particles. J. Biol. Chem. 257:4077-4086.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4077-4086
    • Yamanaka, G.1    Lundell, D.J.2    Glazer, A.N.3
  • 52
    • 0002765159 scopus 로고
    • Energy transfer process in phycobilisomes as deduced from analyses of mutants of Synechococcus sp. PCC 7002
    • N. Murata (ed.). Kluwer, Dordrecht, The Netherlands
    • Zhao, J., J. Zhou, and D. Bryant. 1992. Energy transfer process 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, The Netherlands.
    • (1992) Research in Photosynthesis , vol.1 , pp. 25-32
    • Zhao, J.1    Zhou, J.2    Bryant, D.3
  • 53
    • 0028967604 scopus 로고
    • Type I and type II reversible photochemistry of phycoerythrocyanin α-subunit from Mastigocladus laminosus both involve Z, E isomerization of phycoviolobilin chromophore and are controlled by sulfhydryls in apoprotein
    • Zhao, K.-H., and H. Scheer. 1995. Type I and type II reversible photochemistry of phycoerythrocyanin α-subunit from Mastigocladus laminosus both involve Z, E isomerization of phycoviolobilin chromophore and are controlled by sulfhydryls in apoprotein. Biochim. Biophys. Acta Bioenergetics 1228:244-253.
    • (1995) Biochim. Biophys. Acta Bioenergetics , vol.1228 , pp. 244-253
    • Zhao, K.-H.1    Scheer, H.2


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