메뉴 건너뛰기




Volumn 4, Issue , 2013, Pages

Far-red light photoactivatable near-infrared fluorescent proteins engineered from a bacterial phytochrome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BILIVERDIN; PHOTOACTIVATABLE NEAR INFRARED FLUORESCENT PROTEIN 1; PHOTOACTIVATABLE NEAR INFRARED FLUORESCENT PROTEIN 2; PHYTOCHROME; UNCLASSIFIED DRUG;

EID: 84880296970     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3153     Document Type: Article
Times cited : (108)

References (46)
  • 1
    • 1642453927 scopus 로고    scopus 로고
    • Photoreceptor proteins 'star actors of modern times' a review of the functional dynamics in the structure of representative members of six different photoreceptor families
    • van der Horst, M. A. & Hellingwerf, K. J. Photoreceptor proteins, 'star actors of modern times': a review of the functional dynamics in the structure of representative members of six different photoreceptor families. Acc. Chem. Res. 37, 13-20 (2004).
    • (2004) Acc. Chem. Res , vol.37 , pp. 13-20
    • Van Der Horst, M.A.1    Hellingwerf, K.J.2
  • 2
    • 77951166118 scopus 로고    scopus 로고
    • A brief history of phytochromes
    • Rockwell, N. C. & Lagarias, J. C. A brief history of phytochromes. Chem. Phys. Chem. 11, 1172-1180 (2010).
    • (2010) Chem. Phys. Chem , vol.11 , pp. 1172-1180
    • Rockwell, N.C.1    Lagarias, J.C.2
  • 4
    • 33745938554 scopus 로고    scopus 로고
    • Phytochrome structure and signaling mechanisms
    • DOI 10.1146/annurev.arplant.56.032604.144208
    • Rockwell, N. C., Su, Y. S. & Lagarias, J. C. Phytochrome structure and signaling mechanisms. Annu. Rev. Plant Biol. 57, 837-858 (2006). (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
  • 5
    • 80053896548 scopus 로고    scopus 로고
    • Phytochrome structure and photochemistry: Recent advances toward a complete molecular picture
    • Ulijasz, A. T. & Vierstra, R. D. Phytochrome structure and photochemistry: recent advances toward a complete molecular picture. Curr. Opin. Plant Biol. 14, 498-506 (2011).
    • (2011) Curr. Opin. Plant Biol , vol.14 , pp. 498-506
    • Ulijasz, A.T.1    Vierstra, R.D.2
  • 6
    • 78049254337 scopus 로고    scopus 로고
    • Phytochrome structural basis for its functions
    • Nagatani, A. Phytochrome: structural basis for its functions. Curr. Opin. Plant Biol. 13, 565-570 (2010).
    • (2010) Curr. Opin. Plant Biol , vol.13 , pp. 565-570
    • Nagatani, A.1
  • 7
    • 53849142165 scopus 로고    scopus 로고
    • Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms
    • Dammeyer, T. & Frankenberg-Dinkel, N. Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms. Photochem. Photobiol. Sci. 7, 1121-1130 (2008).
    • (2008) Photochem. Photobiol. Sci , vol.7 , pp. 1121-1130
    • Dammeyer, T.1    Frankenberg-Dinkel, N.2
  • 9
    • 77957369354 scopus 로고    scopus 로고
    • Bathy phytochromes in rhizobial soil bacteria
    • Rottwinkel, G., Oberpichler, I. & Lamparter, T. Bathy phytochromes in rhizobial soil bacteria. J. Bacteriol. 192, 5124-5133 (2010).
    • (2010) J. Bacteriol , vol.192 , pp. 5124-5133
    • Rottwinkel, G.1    Oberpichler, I.2    Lamparter, T.3
  • 10
    • 0037418282 scopus 로고    scopus 로고
    • The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties
    • DOI 10.1073/pnas.0437914100
    • Karniol, B. & Vierstra, R. D. The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties. Proc. Natl Acad. Sci. USA 100, 2807-2812 (2003). (Pubitemid 36297580)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.5 , pp. 2807-2812
    • Karniol, B.1    Vierstra, R.D.2
  • 11
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang, X., Kuk, J. & Moffat, K. Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proc. Natl Acad. Sci. USA 105, 14715-14720 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 12
    • 0017521004 scopus 로고
    • Phototransformations of phytochrome
    • Kendrick, R. E. & Spruit, C. J. Phototransformations of phytochrome. Photochem. Photobiol. 26, 201-214 (1977).
    • (1977) Photochem. Photobiol , vol.26 , pp. 201-214
    • Kendrick, R.E.1    Spruit, C.J.2
  • 13
  • 14
    • 0343889286 scopus 로고
    • Phytochrome intermediates in freeze-dried tissue
    • Spruit, C. J. P., Kendrick, R. E. & Cooke, R. J. Phytochrome intermediates in freeze-dried tissue. Planta 127, 121-132 (1975).
    • (1975) Planta , vol.127 , pp. 121-132
    • Spruit, C.J.P.1    Kendrick, R.E.2    Cooke, R.J.3
  • 16
    • 84989738176 scopus 로고
    • Low temperature spectroscopy of phytochrome: Pr, Pfr and intermediates
    • Rudiger, W. & Thummler, F. Low temperature spectroscopy of phytochrome: Pr, Pfr and intermediates. Physiologia Plantarum 60, 383-388 (1984).
    • (1984) Physiologia Plantarum , vol.60 , pp. 383-388
    • Rudiger, W.1    Thummler, F.2
  • 17
    • 0019879102 scopus 로고
    • Primary photoprocesses of undegraded phytochrome excited with red and blue light at 77K
    • Song, P.-S., Sarkar, H. K., Kim, I.-S. & Poff, K. L. Primary photoprocesses of undegraded phytochrome excited with red and blue light at 77K. Biochim. Biophys. Acta 635, 369-382 (1981).
    • (1981) Biochim. Biophys. Acta , vol.635 , pp. 369-382
    • Song, P.-S.1    Sarkar, H.K.2    Kim, I.-S.3    Poff, K.L.4
  • 18
    • 0017521912 scopus 로고
    • Phototransformation of phytocrome: The characterization of lumi-F and meta-Fa
    • Spruit, C. J. P. & Kendrick, R. E. Phototransformation of phytocrome: the characterization of lumi-F and meta-Fa. Photochem. Photobiol. 26, 133-138 (1977).
    • (1977) Photochem. Photobiol , vol.26 , pp. 133-138
    • Spruit, C.J.P.1    Kendrick, R.E.2
  • 19
    • 77951175058 scopus 로고    scopus 로고
    • Light-induced activation of bacterial phytochrome Agp1 monitored by static and time-resolved FTIR spectroscopy
    • Piwowarski, P. et al. Light-induced activation of bacterial phytochrome Agp1 monitored by static and time-resolved FTIR spectroscopy. Chem. Phys. Chem. 11, 1207-1214 (2010).
    • (2010) Chem. Phys. Chem , vol.11 , pp. 1207-1214
    • Piwowarski, P.1
  • 20
    • 79961182814 scopus 로고    scopus 로고
    • Bright and stable near-infrared fluorescent protein for in vivo imaging
    • Filonov, G. S. et al. Bright and stable near-infrared fluorescent protein for in vivo imaging. Nat. Biotechnol. 29, 757-761 (2011).
    • (2011) Nat. Biotechnol , vol.29 , pp. 757-761
    • Filonov, G.S.1
  • 21
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • Shu, X. et al. Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome. Science 324, 804-807 (2009).
    • (2009) Science , vol.324 , pp. 804-807
    • Shu, X.1
  • 22
    • 0033747389 scopus 로고    scopus 로고
    • Multiphoton microscopy in life sciences
    • Konig, K. Multiphoton microscopy in life sciences. J. Microsc. 200, 83-104 (2000).
    • (2000) J. Microsc , vol.200 , pp. 83-104
    • Konig, K.1
  • 23
    • 84863018064 scopus 로고    scopus 로고
    • Deep-tissue photoacoustic tomography of a genetically encoded near-infrared fluorescent probe
    • Filonov, G. S. et al. Deep-tissue photoacoustic tomography of a genetically encoded near-infrared fluorescent probe. Angew. Chem. Int. Ed. Engl. 51, 1448-1451 (2011).
    • (2011) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 1448-1451
    • Filonov, G.S.1
  • 25
    • 77955026080 scopus 로고    scopus 로고
    • Fused-gene approach to photoswitchable and fluorescent biliproteins
    • Zhang, J. et al. Fused-gene approach to photoswitchable and fluorescent biliproteins. Angew. Chem. Int. Ed. Engl. 49, 5456-5458 (2010).
    • (2010) Angew. Chem. Int. Ed. Engl , vol.49 , pp. 5456-5458
    • Zhang, J.1
  • 26
    • 34548309457 scopus 로고    scopus 로고
    • Light-independent phytochrome signaling mediated by dominant GAF domain tyrosine mutants of Arabidopsis phytochromes in transgenic plants
    • DOI 10.1105/tpc.107.051516
    • Su, Y. S. & Lagarias, J. C. Light-independent phytochrome signaling mediated by dominant GAF domain tyrosine mutants of Arabidopsis phytochromes in transgenic plants. Plant Cell 19, 2124-2139 (2007). (Pubitemid 47347457)
    • (2007) Plant Cell , vol.19 , Issue.7 , pp. 2124-2139
    • Su, Y.-S.1    Lagarias, J.C.2
  • 27
    • 84878742725 scopus 로고    scopus 로고
    • Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals
    • Piatkevich, K. D., Subach, F. V. & Verkhusha, V. V. Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals. Chem. Soc. Rev. 42, 3441-3452 (2013).
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3441-3452
    • Piatkevich, K.D.1    Subach, F.V.2    Verkhusha, V.V.3
  • 28
    • 79957843777 scopus 로고    scopus 로고
    • Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics
    • Wu, B., Piatkevich, K. D., Lionnet, T., Singer, R. H. & Verkhusha, V. V. Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics. Curr. Opin. Cell Biol. 23, 310-317 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 310-317
    • Wu, B.1    Piatkevich, K.D.2    Lionnet, T.3    Singer, R.H.4    Verkhusha, V.V.5
  • 29
    • 78751479869 scopus 로고    scopus 로고
    • Optical switch probes and optical lock-in detection (OLID) imaging microscopy: High-contrast fluorescence imaging within living systems
    • Yan, Y., Marriott, M. E., Petchprayoon, C. & Marriott, G. Optical switch probes and optical lock-in detection (OLID) imaging microscopy: high-contrast fluorescence imaging within living systems. Biochem. J. 433, 411-422 (2011).
    • (2011) Biochem. J , vol.433 , pp. 411-422
    • Yan, Y.1    Marriott, M.E.2    Petchprayoon, C.3    Marriott, G.4
  • 32
    • 65249186449 scopus 로고    scopus 로고
    • Assembly of agrobacterium phytochromes Agp1 and Agp2 with doubly locked bilin chromophores
    • Inomata, K. et al. Assembly of Agrobacterium phytochromes Agp1 and Agp2 with doubly locked bilin chromophores. Biochemistry 48, 2817-2827 (2009).
    • (2009) Biochemistry , vol.48 , pp. 2817-2827
    • Inomata, K.1
  • 33
    • 52749088861 scopus 로고    scopus 로고
    • Spectral properties of phytochrome Agp2 from Agrobacterium tumefaciens are specifically modified by a compound of the cell extract
    • Krieger, A., Molina, I., Oberpichler, I., Michael, N. & Lamparter, T. Spectral properties of phytochrome Agp2 from Agrobacterium tumefaciens are specifically modified by a compound of the cell extract. J. Photochem. Photobiol. B 93, 16-22 (2008).
    • (2008) J. Photochem. Photobiol. B , vol.93 , pp. 16-22
    • Krieger, A.1    Molina, I.2    Oberpichler, I.3    Michael, N.4    Lamparter, T.5
  • 34
    • 17444391234 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of the bacterial phytochrome of Pseudomonas aeruginosa
    • DOI 10.1111/j.1742-4658.2005.04623.x
    • Tasler, R., Moises, T. & Frankenberg-Dinkel, N. Biochemical and spectroscopic characterization of the bacterial phytochrome of Pseudomonas aeruginosa. FEBS J. 272, 1927-1936 (2005). (Pubitemid 40547249)
    • (2005) FEBS Journal , vol.272 , Issue.8 , pp. 1927-1936
    • Tasler, R.1    Moises, T.2    Frankenberg-Dinkel, N.3
  • 35
    • 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. et al. 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).
    • (2008) J. Biol. Chem , vol.283 , pp. 12212-12226
    • Wagner, J.R.1
  • 36
    • 70349461175 scopus 로고    scopus 로고
    • Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome
    • Yang, X., Kuk, J. & Moffat, K. Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. Proc. Natl Acad. Sci. USA 106, 15639-15644 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15639-15644
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 37
    • 75149177129 scopus 로고    scopus 로고
    • Advances in engineering of fluorescent proteins and photoactivatable proteins with red emission
    • Piatkevich, K. D. & Verkhusha, V. V. Advances in engineering of fluorescent proteins and photoactivatable proteins with red emission. Curr. Opin. Chem. Biol. 14, 23-29 (2010).
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 23-29
    • Piatkevich, K.D.1    Verkhusha, V.V.2
  • 38
    • 80052281149 scopus 로고    scopus 로고
    • A photoswitchable orange-to-far-red fluorescent protein PSmOrange
    • Subach, O. M. et al. A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nat. Methods 8, 771-777 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 771-777
    • Subach, O.M.1
  • 39
    • 77955452640 scopus 로고    scopus 로고
    • Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET
    • Subach, F. V. et al. Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET. Chem. Biol. 17, 745-755 (2010).
    • (2010) Chem. Biol , vol.17 , pp. 745-755
    • Subach, F.V.1
  • 40
    • 77952059303 scopus 로고    scopus 로고
    • Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells
    • Subach, F. V., Patterson, G. H., Renz, M., Lippincott-Schwartz, J. & Verkhusha, V. V. Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J. Am. Chem. Soc. 132, 6481-6491 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6481-6491
    • Subach, F.V.1    Patterson, G.H.2    Renz, M.3    Lippincott-Schwartz, J.4    Verkhusha, V.V.5
  • 41
    • 82355188370 scopus 로고    scopus 로고
    • Directed molecular evolution to design advanced red fluorescent proteins
    • Subach, F. V., Piatkevich, K. D. & Verkhusha, V. V. Directed molecular evolution to design advanced red fluorescent proteins. Nat. Methods 8, 1019-1026 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 1019-1026
    • Subach, F.V.1    Piatkevich, K.D.2    Verkhusha, V.V.3
  • 42
    • 57049128693 scopus 로고    scopus 로고
    • Intravital imaging of metastatic behavior through a mammary imaging window
    • Kedrin, D. et al. Intravital imaging of metastatic behavior through a mammary imaging window. Nat. Methods 5, 1019-1021 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 1019-1021
    • Kedrin, D.1
  • 43
    • 39849098903 scopus 로고    scopus 로고
    • Optimization of an E. coli L-rhamnoseinducible expression vector: Test of various genetic module combinations
    • Wegerer, A., Sun, T. & Altenbuchner, J. Optimization of an E. coli L-rhamnoseinducible expression vector: test of various genetic module combinations. BMC Biotechnol. 8, 2 (2008).
    • (2008) BMC Biotechnol , vol.8 , pp. 2
    • Wegerer, A.1    Sun, T.2    Altenbuchner, J.3
  • 45
    • 77950400530 scopus 로고    scopus 로고
    • Monomeric red fluorescent proteins with a large Stokes shift
    • Piatkevich, K. D. et al. Monomeric red fluorescent proteins with a large Stokes shift. Proc. Natl Acad. Sci. USA 107, 5369-5374 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5369-5374
    • Piatkevich, K.D.1
  • 46
    • 78651403054 scopus 로고    scopus 로고
    • Fluorescence of phytochrome adducts with synthetic locked chromophores
    • Zienicke, B. et al. Fluorescence of phytochrome adducts with synthetic locked chromophores. J. Biol. Chem. 286, 1103-1113 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 1103-1113
    • Zienicke, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.