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Volumn 12, Issue 7, 2013, Pages 1144-1157

Distance-tree analysis, distribution and co-presence of bilin- and flavin-binding prokaryotic photoreceptors for visible light

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEA; BACTERIA (MICROORGANISMS); BACTEROIDETES/CHLOROBI GROUP; CYANOBACTERIA; POLYOMMATINAE; PROKARYOTA;

EID: 84882631370     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/c3pp25404f     Document Type: Article
Times cited : (42)

References (66)
  • 1
    • 80052968825 scopus 로고    scopus 로고
    • Function, structure and mechanism of bacterial photosensory LOV proteins
    • J. Herrou S. Crosson Function, structure and mechanism of bacterial photosensory LOV proteins Nat. Rev. Microbiol. 2011 9 713 723
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 713-723
    • Herrou, J.1    Crosson, S.2
  • 4
    • 84872256330 scopus 로고    scopus 로고
    • The evolution of Flavin-binding photoreceptors: An ancient chromophore serving trendy blue-light sensors
    • A. Losi W. Gärtner The evolution of Flavin-binding photoreceptors: an ancient chromophore serving trendy blue-light sensors Annu. Rev. Plant Biol. 2012 63 49 72
    • (2012) Annu. Rev. Plant Biol. , vol.63 , pp. 49-72
    • Losi, A.1    Gärtner, W.2
  • 5
    • 53749091743 scopus 로고    scopus 로고
    • Bacterial bilin- and flavin-binding photoreceptors
    • A. Losi W. Gärtner Bacterial bilin- and flavin-binding photoreceptors Photochem. Photobiol. Sci. 2008 7 1168 1178
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1168-1178
    • Losi, A.1    Gärtner, W.2
  • 6
    • 79955469910 scopus 로고    scopus 로고
    • Old chromophores, new photoactivation paradigms, trendy applications: Flavins in blue light-sensing photoreceptors
    • A. Losi W. Gärtner Old chromophores, new photoactivation paradigms, trendy applications: flavins in blue light-sensing photoreceptors Photochem. Photobiol. 2011 87 491 510
    • (2011) Photochem. Photobiol. , vol.87 , pp. 491-510
    • Losi, A.1    Gärtner, W.2
  • 10
    • 80755179274 scopus 로고    scopus 로고
    • The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria
    • D. Kirilovsky C. A. Kerfeld The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria Biochim. Biophys. Acta, Bioenerg. 2012 1817 158 166
    • (2012) Biochim. Biophys. Acta, Bioenerg. , vol.1817 , pp. 158-166
    • Kirilovsky, D.1    Kerfeld, C.A.2
  • 12
    • 79961030921 scopus 로고    scopus 로고
    • Phytochrome signaling: Solving the Gordian knot with microbial relatives
    • R. D. Vierstra J. Zhang Phytochrome signaling: solving the Gordian knot with microbial relatives Trends Plant Sci. 2011 16 417 426
    • (2011) Trends Plant Sci. , vol.16 , pp. 417-426
    • Vierstra, R.D.1    Zhang, J.2
  • 13
    • 53749101663 scopus 로고    scopus 로고
    • Cyanobacteriochromes: A new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria
    • M. Ikeuchi T. Ishizuka Cyanobacteriochromes: a new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria Photochem. Photobiol. Sci. 2008 7 1159 1167
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1159-1167
    • Ikeuchi, M.1    Ishizuka, T.2
  • 14
    • 0036996263 scopus 로고    scopus 로고
    • A history of ultraviolet photobiology for humans, animals and microorganisms
    • P. E. Hockberger A history of ultraviolet photobiology for humans, animals and microorganisms Photochem. Photobiol. 2002 76 561 579
    • (2002) Photochem. Photobiol. , vol.76 , pp. 561-579
    • Hockberger, P.E.1
  • 15
    • 58149505604 scopus 로고    scopus 로고
    • Discovering functional novelty in metagenomes: Examples from light-mediated processes
    • A. H. Singh T. Doerks I. Letunic J. Raes P. BORK Discovering functional novelty in metagenomes: examples from light-mediated processes J. Bacteriol. 2009 191 32 41
    • (2009) J. Bacteriol. , vol.191 , pp. 32-41
    • Singh, A.H.1    Doerks, T.2    Letunic, I.3    Raes, J.4    Bork, P.5
  • 17
    • 72249087161 scopus 로고    scopus 로고
    • Distribution and phylogeny of light-oxygen-voltage-blue-light-signaling proteins in the three kingdoms of life
    • U. Krauss B. Q. Minh A. Losi W. Gärtner T. Eggert A. von Haeseler K. E. Jaeger Distribution and phylogeny of light-oxygen-voltage-blue-light- signaling proteins in the three kingdoms of life J. Bacteriol. 2009 191 7234 7242
    • (2009) J. Bacteriol. , vol.191 , pp. 7234-7242
    • Krauss, U.1    Minh, B.Q.2    Losi, A.3    Gärtner, W.4    Eggert, T.5    Von Haeseler, A.6    Jaeger, K.E.7
  • 18
    • 65349159321 scopus 로고    scopus 로고
    • Evolution of mutation rates: Phylogenomic analysis of the photolyase/cryptochrome family
    • J. I. Lucas-Lledo M. Lynch Evolution of mutation rates: phylogenomic analysis of the photolyase/cryptochrome family Mol. Biol. Evol. 2009 26 1143 1153
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 1143-1153
    • Lucas-Lledo, J.I.1    Lynch, M.2
  • 20
    • 79955480102 scopus 로고    scopus 로고
    • Indication for a radical intermediate preceding the signaling state in the LOV domain photocycle
    • C. Bauer C. R. Rabl J. Heberle T. Kottke Indication for a radical intermediate preceding the signaling state in the LOV domain photocycle Photochem. Photobiol. 2011 87 548 553
    • (2011) Photochem. Photobiol. , vol.87 , pp. 548-553
    • Bauer, C.1    Rabl, C.R.2    Heberle, J.3    Kottke, T.4
  • 21
    • 36249024090 scopus 로고    scopus 로고
    • Flavin-based blue-light photosensors: A photobiophysics update
    • A. Losi Flavin-based blue-light photosensors: a photobiophysics update Photochem. Photobiol. 2007 83 1283 1300
    • (2007) Photochem. Photobiol. , vol.83 , pp. 1283-1300
    • Losi, A.1
  • 22
    • 79955917653 scopus 로고    scopus 로고
    • Strong donation of the hydrogen bond of tyrosine during photoactivation of the BLUF domain
    • T. Iwata A. Watanabe M. Iseki M. Watanabe H. Kandori Strong donation of the hydrogen bond of tyrosine during photoactivation of the BLUF domain J. Phys. Chem. Lett. 2011 2 1015 1019
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 1015-1019
    • Iwata, T.1    Watanabe, A.2    Iseki, M.3    Watanabe, M.4    Kandori, H.5
  • 24
    • 44849105177 scopus 로고    scopus 로고
    • Femtosecond kinetics of photoconversion of the higher plant photoreceptor phytochrome carrying native and modified chromophores
    • M. Müller I. Lindner I. Martin W. Gärtner A. R. Holzwarth Femtosecond kinetics of photoconversion of the higher plant photoreceptor phytochrome carrying native and modified chromophores Biophys. J. 2008 94 4370 4382
    • (2008) Biophys. J. , vol.94 , pp. 4370-4382
    • Müller, M.1    Lindner, I.2    Martin, I.3    Gärtner, W.4    Holzwarth, A.R.5
  • 26
    • 77951166118 scopus 로고    scopus 로고
    • A brief history of phytochromes
    • N. C. Rockwell J. C. Lagarias A brief history of phytochromes ChemPhysChem 2010 11 1172 1180
    • (2010) ChemPhysChem , vol.11 , pp. 1172-1180
    • Rockwell, N.C.1    Lagarias, J.C.2
  • 27
    • 27844461604 scopus 로고    scopus 로고
    • A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome
    • J. R. Wagner J. S. Brunzelle K. T. Forest R. D. Vierstra A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome Nature 2005 438 325 331
    • (2005) Nature , vol.438 , pp. 325-331
    • Wagner, J.R.1    Brunzelle, J.S.2    Forest, K.T.3    Vierstra, R.D.4
  • 29
    • 17444391234 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of the bacterial phytochrome of Pseudomonas aeruginosa
    • R. Tasler T. Moises N. Frankenberg-Dinkel Biochemical and spectroscopic characterization of the bacterial phytochrome of Pseudomonas aeruginosa FEBS J. 2005 272 1927 1936
    • (2005) FEBS J. , vol.272 , pp. 1927-1936
    • Tasler, R.1    Moises, T.2    Frankenberg-Dinkel, N.3
  • 30
    • 84872573710 scopus 로고    scopus 로고
    • Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism
    • R. Narikawa T. Ishizuka N. Muraki T. Shiba G. Kurisu M. Ikeuchi Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism Proc. Natl. Acad. Sci. U. S. A. 2013 110 918 923
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 918-923
    • Narikawa, R.1    Ishizuka, T.2    Muraki, N.3    Shiba, T.4    Kurisu, G.5    Ikeuchi, M.6
  • 31
    • 84872126119 scopus 로고    scopus 로고
    • A photo-labile thioether linkage to phycoviolobilin provides the foundation for the blue/green photocycles in DXCF-cyanobacteriochromes
    • E. Burgie J. Walker J. Phillips R. Vierstra A photo-labile thioether linkage to phycoviolobilin provides the foundation for the blue/green photocycles in DXCF-cyanobacteriochromes Structure 2013 21 88 97
    • (2013) Structure , vol.21 , pp. 88-97
    • Burgie, E.1    Walker, J.2    Phillips, J.3    Vierstra, R.4
  • 32
  • 33
    • 84857406217 scopus 로고    scopus 로고
    • Phycoviolobilin formation and spectral tuning in the DXCF cyanobacteriochrome subfamily
    • N. C. Rockwell S. S. Martin A. G. Gulevich J. C. Lagarias Phycoviolobilin formation and spectral tuning in the DXCF cyanobacteriochrome subfamily Biochemistry 2012 51 1449 1463
    • (2012) Biochemistry , vol.51 , pp. 1449-1463
    • Rockwell, N.C.1    Martin, S.S.2    Gulevich, A.G.3    Lagarias, J.C.4
  • 34
    • 84867580557 scopus 로고    scopus 로고
    • A rising tide of blue-absorbing biliprotein photoreceptors: Characterization of seven such bilin-binding GAF domains in Nostoc sp. PCC7120
    • Q. Ma H. H. Hua Y. Chen B. B. Liu A. L. Krämer H. Scheer K. H. Zhao M. Zhou A rising tide of blue-absorbing biliprotein photoreceptors: characterization of seven such bilin-binding GAF domains in Nostoc sp. PCC7120 FEBS J. 2012 279 4095 4108
    • (2012) FEBS J. , vol.279 , pp. 4095-4108
    • Ma, Q.1    Hua, H.H.2    Chen, Y.3    Liu, B.B.4    Krämer, A.L.5    Scheer, H.6    Zhao, K.H.7    Zhou, M.8
  • 35
    • 84855913595 scopus 로고    scopus 로고
    • Femtosecond photodynamics of the red/green cyanobacteriochrome NpR6012g4 from Nostoc punctiforme. 1. Forward dynamics
    • P. W. Kim L. H. Freer N. C. Rockwell S. S. Martin J. C. Lagarias D. S. Larsen Femtosecond photodynamics of the red/green cyanobacteriochrome NpR6012g4 from Nostoc punctiforme. 1. Forward dynamics Biochemistry 2012 51 608 618
    • (2012) Biochemistry , vol.51 , pp. 608-618
    • Kim, P.W.1    Freer, L.H.2    Rockwell, N.C.3    Martin, S.S.4    Lagarias, J.C.5    Larsen, D.S.6
  • 36
    • 84855968782 scopus 로고    scopus 로고
    • Femtosecond photodynamics of the red/green cyanobacteriochrome NpR6012g4 from Nostoc punctiforme. 2. Reverse dynamics
    • P. W. Kim L. H. Freer N. C. Rockwell S. S. Martin J. C. Lagarias D. S. Larsen Femtosecond photodynamics of the red/green cyanobacteriochrome NpR6012g4 from Nostoc punctiforme. 2. Reverse dynamics Biochemistry 2012 51 619 630
    • (2012) Biochemistry , vol.51 , pp. 619-630
    • Kim, P.W.1    Freer, L.H.2    Rockwell, N.C.3    Martin, S.S.4    Lagarias, J.C.5    Larsen, D.S.6
  • 39
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • A. Losi E. Polverini B. Quest W. Gärtner First evidence for phototropin-related blue-light receptors in prokaryotes Biophys. J. 2002 82 2627 2634
    • (2002) Biophys. J. , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 40
    • 16344389152 scopus 로고    scopus 로고
    • Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, Tll0078, of Thermosynechococcus elongatus BP-1
    • Y. Fukushima K. Okajima Y. Shibata M. Ikeuchi S. Itoh Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, Tll0078, of Thermosynechococcus elongatus BP-1 Biochemistry 2005 44 5149 5158
    • (2005) Biochemistry , vol.44 , pp. 5149-5158
    • Fukushima, Y.1    Okajima, K.2    Shibata, Y.3    Ikeuchi, M.4    Itoh, S.5
  • 41
    • 4444326150 scopus 로고    scopus 로고
    • Et al. 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. Bohm C. Bubenzer a. Scheer et al. Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120: lyase activities, chromophore exchange, and photochromism in phytochrome AphA Biochemistry 2004 43 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    Bohm, S.8    Bubenzer, C.9    Scheer, A.10
  • 43
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura D. Peterson N. Peterson G. Stecher M. Nei S. Kumar MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 2011 28 2731 2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 44
    • 44949173847 scopus 로고    scopus 로고
    • Maximum parsimony method for phylogenetic prediction
    • db
    • D. W. Mount, Maximum parsimony method for phylogenetic prediction, Cold Spring Harbor Protocols, 2008, 2008, db
    • (2008) Cold Spring Harbor Protocols , vol.2008
    • Mount, D.W.1
  • 46
    • 84866914570 scopus 로고    scopus 로고
    • Proteorhodopsin genes in giant viruses
    • N. Yutin E. Koonin Proteorhodopsin genes in giant viruses Biol. Direct 2012 7 34
    • (2012) Biol. Direct , vol.7 , pp. 34
    • Yutin, N.1    Koonin, E.2
  • 47
    • 77957358837 scopus 로고    scopus 로고
    • The PpaA/AerR regulators of photosynthesis gene expression from anoxygenic phototrophic proteobacteria contain heme-binding SCHIC domains
    • O. V. Moskvin M. A. Gilles-Gonzalez M. Gomelsky The PpaA/AerR regulators of photosynthesis gene expression from anoxygenic phototrophic proteobacteria contain heme-binding SCHIC domains J. Bacteriol. 2010 192 5253 5256
    • (2010) J. Bacteriol. , vol.192 , pp. 5253-5256
    • Moskvin, O.V.1    Gilles-Gonzalez, M.A.2    Gomelsky, M.3
  • 49
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • A. H. West A. M. Stock Histidine kinases and response regulator proteins in two-component signaling systems Trends Biochem. Sci. 2001 26 369 376
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 50
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • H. Szurmant R. A. White J. A. Hoch Sensor complexes regulating two-component signal transduction Curr. Opin. Struct. Biol. 2007 17 706 715
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 51
    • 39449102806 scopus 로고    scopus 로고
    • Plant-associated methylobacteria as co-evolved phytosymbionts: A hypothesis
    • U. Kutschera Plant-associated methylobacteria as co-evolved phytosymbionts: a hypothesis Plant Signaling Behav. 2007 2 74 78
    • (2007) Plant Signaling Behav. , vol.2 , pp. 74-78
    • Kutschera, U.1
  • 52
    • 27144507187 scopus 로고    scopus 로고
    • Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors
    • B. Karniol J. R. Wagner J. M. Walker R. D. Vierstra Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors Biochem. J. 2005 392 103 116
    • (2005) Biochem. J. , vol.392 , pp. 103-116
    • Karniol, B.1    Wagner, J.R.2    Walker, J.M.3    Vierstra, R.D.4
  • 54
    • 77955352382 scopus 로고    scopus 로고
    • Mixotrophic and photoheterotrophic metabolism in Cyanothece sp. ATCC 51142 under continuous light
    • X. Feng A. Bandyopadhyay B. Berla L. Page B. Wu H. B. Pakrasi Y. J. Tang Mixotrophic and photoheterotrophic metabolism in Cyanothece sp. ATCC 51142 under continuous light Microbiology 2010 156 2566 2574
    • (2010) Microbiology , vol.156 , pp. 2566-2574
    • Feng, X.1    Bandyopadhyay, A.2    Berla, B.3    Page, L.4    Wu, B.5    Pakrasi, H.B.6    Tang, Y.J.7
  • 56
    • 84859895795 scopus 로고    scopus 로고
    • Diversity and functional analysis of proteorhodopsin in marine flavobacteria
    • S. Yoshizawa A. Kawanabe H. Ito H. Kandori K. Kogure Diversity and functional analysis of proteorhodopsin in marine flavobacteria Environ. Microbiol. 2012 14 1240 1248
    • (2012) Environ. Microbiol. , vol.14 , pp. 1240-1248
    • Yoshizawa, S.1    Kawanabe, A.2    Ito, H.3    Kandori, H.4    Kogure, K.5
  • 57
    • 84859593279 scopus 로고    scopus 로고
    • Thiol-based photocycle of the blue and teal light-sensing cyanobacteriochrome Tlr1999
    • G. Enomoto Y. Hirose R. Narikawa M. Ikeuchi Thiol-based photocycle of the blue and teal light-sensing cyanobacteriochrome Tlr1999 Biochemistry 2012 51 3050 3058
    • (2012) Biochemistry , vol.51 , pp. 3050-3058
    • Enomoto, G.1    Hirose, Y.2    Narikawa, R.3    Ikeuchi, M.4
  • 59
    • 0001230325 scopus 로고    scopus 로고
    • Primary quantum yield and volume change of phytochrome-A phototransformation determined by laser-induced optoacoustic spectroscopy
    • T. Gensch M. S. Churio S. E. Braslavsky K. Schaffner Primary quantum yield and volume change of phytochrome-A phototransformation determined by laser-induced optoacoustic spectroscopy Photochem. Photobiol. 1996 63 719 725
    • (1996) Photochem. Photobiol. , vol.63 , pp. 719-725
    • Gensch, T.1    Churio, M.S.2    Braslavsky, S.E.3    Schaffner, K.4
  • 61
  • 62
    • 33847249975 scopus 로고    scopus 로고
    • Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors
    • R. P. Alexander I. B. Zhulin Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors Proc. Natl. Acad. Sci. U. S. A. 2007 104 2885 2890
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2885-2890
    • Alexander, R.P.1    Zhulin, I.B.2
  • 63
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity
    • S. M. Harper J. M. Christie K. H. Gardner Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity Biochemistry 2004 43 16184 16192
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 64
    • 18144372698 scopus 로고    scopus 로고
    • Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel fad-binding blue light sensor domain
    • A. Kita K. Okajima Y. Morimoto M. Ikeuchi K. Miki Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel fad-binding blue light sensor domain J. Mol. Biol. 2005 349 1 9
    • (2005) J. Mol. Biol. , vol.349 , pp. 1-9
    • Kita, A.1    Okajima, K.2    Morimoto, Y.3    Ikeuchi, M.4    Miki, K.5
  • 65
    • 84861402657 scopus 로고    scopus 로고
    • LOV domain-containing F-Box proteins: Light-dependent protein degradation modules in arabidopsis
    • S. Ito Y. H. Song T. Imaizumi LOV domain-containing F-Box proteins: light-dependent protein degradation modules in arabidopsis Mol. Plant 2012 5 573 582
    • (2012) Mol. Plant , vol.5 , pp. 573-582
    • Ito, S.1    Song, Y.H.2    Imaizumi, T.3
  • 66
    • 55749108535 scopus 로고    scopus 로고
    • The structure of a complete phytochrome sensory module in the Pr ground state
    • L. O. Essen J. Mailliet J. Hughes The structure of a complete phytochrome sensory module in the Pr ground state Proc. Natl. Acad. Sci. U. S. A. 2008 105 14709 14714
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14709-14714
    • Essen, L.O.1    Mailliet, J.2    Hughes, J.3


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