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Volumn 289, Issue 35, 2014, Pages 24573-24587

Crystallographic and electron microscopic analyses of a bacterial phytochrome reveal local and global rearrangements during photoconversion

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMOPHORES; DIGITAL STORAGE; VISION;

EID: 84906860684     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.571661     Document Type: Article
Times cited : (100)

References (50)
  • 2
    • 33745938554 scopus 로고    scopus 로고
    • Phytochrome structure and signaling mechanisms
    • DOI 10.1146/annurev.arplant.56.032604.144208
    • Rockwell, N. C., Su, Y. S., and Lagarias, J. C. (2006) Phytochrome structure and signaling mechanisms. Annu. Rev. Plant Biol. 57, 837-858 (Pubitemid 44061047)
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 837-858
    • Rockwell, N.C.1    Su, Y.-S.2    Lagarias, J.C.3
  • 3
    • 79961030921 scopus 로고    scopus 로고
    • Phytochrome signaling: Solving the Gordian knot with microbial relatives
    • Vierstra, R. D., and Zhang, J. (2011) Phytochrome signaling: solving the Gordian knot with microbial relatives. Trends Plant Sci. 16, 417-426
    • (2011) Trends Plant Sci. , vol.16 , pp. 417-426
    • Vierstra, R.D.1    Zhang, J.2
  • 4
    • 72049106410 scopus 로고    scopus 로고
    • Phytochrome functions in Arabidopsis development
    • Franklin, K. A., and Quail, P. H. (2010) Phytochrome functions in Arabidopsis development. J. Exp. Bot. 61, 11-24
    • (2010) J. Exp. Bot. , vol.61 , pp. 11-24
    • Franklin, K.A.1    Quail, P.H.2
  • 5
    • 84856408849 scopus 로고    scopus 로고
    • Emerging perspectives on the mechanisms, regulation, and distribution of light color acclimation in cyanobacteria
    • Gutu, A., and Kehoe, D. M. (2012) Emerging perspectives on the mechanisms, regulation, and distribution of light color acclimation in cyanobacteria. Mol. Plant 5, 1-13
    • (2012) Mol. Plant , vol.5 , pp. 1-13
    • Gutu, A.1    Kehoe, D.M.2
  • 6
    • 84906872724 scopus 로고    scopus 로고
    • (Flores, E., and Herrero, A., eds) Caister Academic Press, Poole, UK
    • Bussell, A. N., and Kehoe, D. M. (2014) in The Cell Biology of Cyanobacteria (Flores, E., and Herrero, A., eds) pp. 149-170, Caister Academic Press, Poole, UK
    • (2014) The Cell Biology of Cyanobacteria , pp. 149-170
    • Bussell, A.N.1    Kehoe, D.M.2
  • 7
    • 1642276701 scopus 로고    scopus 로고
    • The Biliverdin Chromophore Binds Covalently to a Conserved Cysteine Residue in the N-Terminus of Agrobacterium Phytochrome Agp1
    • DOI 10.1021/bi035693l
    • Lamparter, T., Carrascal, M., Michael, N., Martinez, E., Rottwinkel, G., and Abian, J. (2004) The biliverdin chromophore binds covalently to a conserved cysteine residue in the N terminus of Agrobacterium phytochrome Agp1. Biochemistry 43, 3659-3669 (Pubitemid 38391720)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3659-3669
    • Lamparter, T.1    Carrascal, M.2    Michael, N.3    Martinez, E.4    Rottwinkel, G.5    Abian, J.6
  • 8
    • 29144528857 scopus 로고    scopus 로고
    • Genetic and molecular analysis of phytochromes from the filamentous fungus Neurospora crassa
    • DOI 10.1128/EC.4.12.2140-2152.2005
    • Froehlich, A. C., Noh, B., Vierstra, R. D., Loros, J., and Dunlap, J. C. (2005) Genetic and molecular analysis of phytochromes from the filamentous fungus Neurospora crassa. Eukaryot. Cell 4, 2140-2152 (Pubitemid 41798319)
    • (2005) Eukaryotic Cell , vol.4 , Issue.12 , pp. 2140-2152
    • Froehlich, A.C.1    Noh, B.2    Vierstra, R.D.3    Loros, J.4    Dunlap, J.C.5
  • 9
    • 0030865349 scopus 로고    scopus 로고
    • A cyanobacterial phytochrome two-component light sensory system
    • DOI 10.1126/science.277.5331.1505
    • Yeh, K. C., Wu, S. H., Murphy, J. T., and Lagarias, J. C. (1997) A cyanobacterial phytochrome two-component light sensory system. Science 277, 1505-1508 (Pubitemid 27449238)
    • (1997) Science , vol.277 , Issue.5331 , pp. 1505-1508
    • Yeh, K.-C.1    Wu, S.-H.2    Murphy, J.T.3    Lagarias, J.C.4
  • 10
    • 55749108535 scopus 로고    scopus 로고
    • The structure of a complete phytochrome sensory module in the Pr ground state
    • Essen, L. O., Mailliet, J., and Hughes, J. (2008) The structure of a complete phytochrome sensory module in the Pr ground state. Proc. Natl. Acad. Sci. U.S.A. 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
  • 11
    • 84904307885 scopus 로고    scopus 로고
    • Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome
    • Burgie, E. S., Bussell, A. N., Walker, J. M., Dubiel, K., and Vierstra, R. D. (2014) Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome. Proc. Natl. Acad. Sci. U.S.A. 111, 10179-10184
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 10179-10184
    • Burgie, E.S.1    Bussell, A.N.2    Walker, J.M.3    Dubiel, K.4    Vierstra, R.D.5
  • 12
    • 0000249480 scopus 로고
    • Chromopeptides from phytochrome. The structure and linkage of the Pr form of the phytochrome chromophore
    • Lagarias, J. C., and Rapoport, H. (1980) Chromopeptides from phytochrome. The structure and linkage of the Pr form of the phytochrome chromophore. J. Am. Chem. Soc. 102, 4821-4828
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 4821-4828
    • Lagarias, J.C.1    Rapoport, H.2
  • 13
    • 79952754070 scopus 로고    scopus 로고
    • Two ground state isoforms and a chromophore D-ring photoflip triggering extensive intramolecular changes in a canonical phytochrome
    • Song, C., Psakis, G., Lang, C., Mailliet, J., Gärtner, W., Hughes, J., and Matysik, J. (2011) Two ground state isoforms and a chromophore D-ring photoflip triggering extensive intramolecular changes in a canonical phytochrome. Proc. Natl. Acad. Sci. U.S.A. 108, 3842-3847
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3842-3847
    • Song, C.1    Psakis, G.2    Lang, C.3    Mailliet, J.4    Gärtner, W.5    Hughes, J.6    Matysik, J.7
  • 14
    • 81555214075 scopus 로고    scopus 로고
    • Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome
    • Yang, X., Ren, Z., Kuk, J., and Moffat, K. (2011) Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Nature 479, 428-432
    • (2011) Nature , vol.479 , pp. 428-432
    • Yang, X.1    Ren, Z.2    Kuk, J.3    Moffat, K.4
  • 18
    • 27144507187 scopus 로고    scopus 로고
    • Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors
    • DOI 10.1042/BJ20050826
    • Karniol, B., Wagner, J. R., Walker, J. M., and Vierstra, R. D. (2005) Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors. Biochem. J. 392, 103-116 (Pubitemid 41689406)
    • (2005) Biochemical Journal , vol.392 , Issue.1 , pp. 103-116
    • Karniol, B.1    Wagner, J.R.2    Walker, J.M.3    Vierstra, R.D.4
  • 19
    • 84864860526 scopus 로고    scopus 로고
    • Structure of a bacteriophytochrome and light-stimulated protomer swapping with a gene repressor
    • Bellini, D., and Papiz, M. Z. (2012) Structure of a bacteriophytochrome and light-stimulated protomer swapping with a gene repressor. Structure 20, 1436-1446
    • (2012) Structure , vol.20 , pp. 1436-1446
    • Bellini, D.1    Papiz, M.Z.2
  • 20
    • 84881085900 scopus 로고    scopus 로고
    • Control of a four-color sensing photoreceptor by a two-color sensing photoreceptor reveals complex light regulation in cyanobacteria
    • Bussell, A. N., and Kehoe, D. M. (2013) Control of a four-color sensing photoreceptor by a two-color sensing photoreceptor reveals complex light regulation in cyanobacteria. Proc. Natl. Acad. Sci. U.S.A. 110, 12834 -12839
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 12834-12839
    • Bussell, A.N.1    Kehoe, D.M.2
  • 21
    • 84890381658 scopus 로고    scopus 로고
    • Structure of the cyanobacterial phytochrome 2 photo-sensor implies a tryptophan switch for phytochrome signaling
    • Anders, K., Daminelli-Widany, G., Mroginski, M. A., von Stetten, D., and Essen, L. O. (2013) Structure of the cyanobacterial phytochrome 2 photo-sensor implies a tryptophan switch for phytochrome signaling. J. Biol. Chem. 288, 35714-35725
    • (2013) J. Biol. Chem. , vol.288 , pp. 35714-35725
    • Anders, K.1    Daminelli-Widany, G.2    Mroginski, M.A.3    Von Stetten, D.4    Essen, L.O.5
  • 23
    • 84893467710 scopus 로고    scopus 로고
    • Dynamic structural changes underpin photoconversion of a blue/green cyanobacteriochrome between its dark and photoactivated states
    • Cornilescu, C. C., Cornilescu, G., Burgie, E. S., Markley, J. L., Ulijasz, A. T., and Vierstra, R. D. (2014) Dynamic structural changes underpin photoconversion of a blue/green cyanobacteriochrome between its dark and photoactivated states. J. Biol. Chem. 289, 3055-3065
    • (2014) J. Biol. Chem. , vol.289 , pp. 3055-3065
    • Cornilescu, C.C.1    Cornilescu, G.2    Burgie, E.S.3    Markley, J.L.4    Ulijasz, A.T.5    Vierstra, R.D.6
  • 24
    • 84872573710 scopus 로고    scopus 로고
    • Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism
    • Narikawa, R., Ishizuka, T., Muraki, N., Shiba, T., Kurisu, G., and Ikeuchi, M. (2013) Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism. Proc. Natl. Acad. Sci. U.S.A. 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
  • 25
    • 84872126119 scopus 로고    scopus 로고
    • A photo-labile thioether linkage to phycoviolobilin provides the foundation for the blue/green photocycles in DXCF-cyanobacteriochromes
    • Burgie, E. S., Walker, J. M., Phillips, G. N., Jr., and Vierstra, R. D. (2013) A photo-labile thioether linkage to phycoviolobilin provides the foundation for the blue/green photocycles in DXCF-cyanobacteriochromes. Structure 21, 88-97
    • (2013) Structure , vol.21 , pp. 88-97
    • Burgie, E.S.1    Walker, J.M.2    Phillips Jr., G.N.3    Vierstra, R.D.4
  • 26
    • 52949096101 scopus 로고    scopus 로고
    • Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state
    • Cornilescu, G., Ulijasz, A. T., Cornilescu, C. C., Markley, J. L., and Vierstra, R. D. (2008) Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state. J. Mol. Biol. 383, 403-413
    • (2008) J. Mol. Biol. , vol.383 , pp. 403-413
    • Cornilescu, G.1    Ulijasz, A.T.2    Cornilescu, C.C.3    Markley, J.L.4    Vierstra, R.D.5
  • 27
    • 27844461604 scopus 로고    scopus 로고
    • A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome
    • DOI 10.1038/nature04118, PII N04118
    • Wagner, J. R., Brunzelle, J. S., Forest, K. T., and Vierstra, R. D. (2005) A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438, 325-331 (Pubitemid 41643944)
    • (2005) Nature , vol.438 , Issue.7066 , pp. 325-331
    • Wagner, J.R.1    Brunzelle, J.S.2    Forest, K.T.3    Vierstra, R.D.4
  • 28
    • 34547628072 scopus 로고    scopus 로고
    • Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion
    • DOI 10.1073/pnas.0701737104
    • Yang, X., Stojkovic, E. A., Kuk, J., and Moffat, K. (2007) Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion. Proc. Natl. Acad. Sci. U.S.A. 104, 12571-12576 (Pubitemid 47206179)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.30 , pp. 12571-12576
    • Yang, X.1    Stojkovic, E.A.2    Kuk, J.3    Moffat, K.4
  • 29
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang, X., Kuk, J., and Moffat, K. (2008) Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proc. Natl. Acad. Sci. U.S.A. 105, 14715-14720
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 31
    • 77954654259 scopus 로고    scopus 로고
    • Quaternary organization of a phytochrome dimer as revealed by cryoelectron microscopy
    • Li, H., Zhang, J., and Vierstra, R. D. (2010) Quaternary organization of a phytochrome dimer as revealed by cryoelectron microscopy. Proc. Natl. Acad. Sci. U.S.A. 107, 10872-10977
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10872-10977
    • Li, H.1    Zhang, J.2    Vierstra, R.D.3
  • 32
    • 34249728355 scopus 로고    scopus 로고
    • High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution
    • DOI 10.1074/jbc.M611824200
    • Wagner, J. R., Zhang, J., Brunzelle, J. S., Vierstra, R. D., and Forest, K. T. (2007) High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution. J. Biol. Chem. 282, 12298-12309 (Pubitemid 47100678)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12298-12309
    • Wagner, J.R.1    Zhang, J.2    Brunzelle, J.S.3    Vierstra, R.D.4    Forest, K.T.5
  • 33
    • 45549107695 scopus 로고    scopus 로고
    • Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes
    • Wagner, J. R., Zhang, J., von Stetten, D., Günther, M., Murgida, D. H., Mroginski, M. A., Walker, J. M., Forest, K. T., Hildebrandt, P., and Vierstra, R. D. (2008) Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes. J. Biol. Chem. 283, 12212-12226
    • (2008) J. Biol. Chem. , vol.283 , pp. 12212-12226
    • Wagner, J.R.1    Zhang, J.2    Von Stetten, D.3    Günther, M.4    Murgida, D.H.5    Mroginski, M.A.6    Walker, J.M.7    Forest, K.T.8    Hildebrandt, P.9    Vierstra, R.D.10
  • 34
    • 70349461175 scopus 로고    scopus 로고
    • Conformational differences between the Pfr and Pr states of Pseudomonas aeruginosa bacteriophytochrome
    • Yang, X., Kuk, J., and Moffat, K. (2009) Conformational differences between the Pfr and Pr states of Pseudomonas aeruginosa bacteriophytochrome. Proc. Natl. Acad. Sci. U.S.A. 106, 15639-15644
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 15639-15644
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 35
    • 0033601199 scopus 로고    scopus 로고
    • Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria
    • Davis, S. J., Vener, A. V., and Vierstra, R. D. (1999) Bacteriophytochromes: phytochrome-like photoreceptors from nonphotosynthetic eubacteria. Science 286, 2517-2520
    • (1999) Science , vol.286 , pp. 2517-2520
    • Davis, S.J.1    Vener, A.V.2    Vierstra, R.D.3
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. A 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976) A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32, 922-923
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 41
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 42
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., and Ludtke, S. J. (2007) EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 44
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore
    • DOI 10.1038/414776a
    • Bhoo, S. H., Davis, S. J., Walker, J., Karniol, B., and Vierstra, R. D. (2001) Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore. Nature 414, 776-779 (Pubitemid 34000778)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 776-779
    • Bhoo, S.-H.1    Davis, S.J.2    Walker, J.3    Karniol, B.4    Vierstra, R.D.5
  • 47
    • 84857715916 scopus 로고    scopus 로고
    • Structure-guided engineering enhances a phytochrome-based infrared fluorescent protein
    • Auldridge, M. E., Satyshur, K. A., Anstrom, D. M., and Forest, K. T. (2012) Structure-guided engineering enhances a phytochrome-based infrared fluorescent protein. J. Biol. Chem. 287, 7000-7009
    • (2012) J. Biol. Chem. , vol.287 , pp. 7000-7009
    • Auldridge, M.E.1    Satyshur, K.A.2    Anstrom, D.M.3    Forest, K.T.4
  • 48
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • Shu, X., Royant, A., Lin, M. Z., Aguilera, T. A., Lev-Ram, V., Steinbach, P. A., and Tsien, R. Y. (2009) Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome. Science 324, 804-807
    • (2009) Science , vol.324 , pp. 804-807
    • Shu, X.1    Royant, A.2    Lin, M.Z.3    Aguilera, T.A.4    Lev-Ram, V.5    Steinbach, P.A.6    Tsien, R.Y.7
  • 49
    • 80053313196 scopus 로고    scopus 로고
    • Spectroscopy and a high-resolution crystal structure of Tyr263 mutants of cyanobacterial phytochrome Cph1
    • Mailliet, J., Psakis, G., Feilke, K., Sineshchekov, V., Essen, L. O., and Hughes, J. (2011) Spectroscopy and a high-resolution crystal structure of Tyr263 mutants of cyanobacterial phytochrome Cph1. J. Mol. Biol. 413, 115-127
    • (2011) J. Mol. Biol. , vol.413 , pp. 115-127
    • Mailliet, J.1    Psakis, G.2    Feilke, K.3    Sineshchekov, V.4    Essen, L.O.5    Hughes, J.6
  • 50
    • 84874595646 scopus 로고    scopus 로고
    • Structure-guided engineering of plant phytochrome B with altered photochemistry and light signaling
    • Zhang, J., Stankey, R. J., and Vierstra, R. D. (2013) Structure-guided engineering of plant phytochrome B with altered photochemistry and light signaling. Plant Physiol. 161, 1445-1457
    • (2013) Plant Physiol. , vol.161 , pp. 1445-1457
    • Zhang, J.1    Stankey, R.J.2    Vierstra, R.D.3


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