메뉴 건너뛰기




Volumn 71, Issue 2, 2000, Pages 230-236

Properties of the bimodal fluorescent protein produced by Photobacterium phosphoreum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BIMODAL FLUORESCENT PROTEIN; CHLORIDE; DIMER; FLAVINE MONONUCLEOTIDE; FLAVOPROTEIN; GUANIDIUM CHLORIDE; MYRISTIC ACID; QUERCETIN; UNCLASSIFIED DRUG;

EID: 0034143195     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2000)071<0230:POTBFP>2.0.CO;2     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 0001568333 scopus 로고
    • Planktonic marine luminous bacteria: Species distribution in the water column
    • Ruby, E. G., E. P. Greenberg and J. W. Hastings (1980) Planktonic marine luminous bacteria: species distribution in the water column. Appl. Environ. Microbiol. 39, 302-306.
    • (1980) Appl. Environ. Microbiol. , vol.39 , pp. 302-306
    • Ruby, E.G.1    Greenberg, E.P.2    Hastings, J.W.3
  • 3
    • 0000802647 scopus 로고
    • The biochemistry and molecular biology of bacterial bioluminescence
    • Edited by F. Muller. CRC Press, Boca Raton, FL
    • Baldwin, T. O. and M. M. Ziegler (1992) The biochemistry and molecular biology of bacterial bioluminescence. In Chemistry and Biochemistry of Flavoenzymes, Vol. 3 (Edited by F. Muller), pp. 467-530. CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 467-530
    • Baldwin, T.O.1    Ziegler, M.M.2
  • 4
    • 0017363555 scopus 로고
    • A luminous bacterium that emits yellow light
    • Ruby, E. G. and K. H. Nealson (1977) A luminous bacterium that emits yellow light. Science 196, 432-434.
    • (1977) Science , vol.196 , pp. 432-434
    • Ruby, E.G.1    Nealson, K.H.2
  • 5
    • 84989723713 scopus 로고
    • Sensitization by lumazine proteins of the bioluminescence emission from the reaction of bacterial luciferases
    • Lee, J. (1982) Sensitization by lumazine proteins of the bioluminescence emission from the reaction of bacterial luciferases. Photochem. Photobiol. 36, 689-697.
    • (1982) Photochem. Photobiol. , vol.36 , pp. 689-697
    • Lee, J.1
  • 6
    • 0025100922 scopus 로고
    • A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system: Energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1
    • Eckstein, J. W., K. W. Cho, P. Colepicolo, S. Ghisla, J. W. Hastings and T. Wilson (1990) A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system: energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1. Proc. Natl. Acad. Sci. USA 87, 1466-1470.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1466-1470
    • Eckstein, J.W.1    Cho, K.W.2    Colepicolo, P.3    Ghisla, S.4    Hastings, J.W.5    Wilson, T.6
  • 7
    • 0002591422 scopus 로고
    • Purification and characterization of an unusual non-fluorescent flavoprotein from Photobacterium leiognathi
    • Edited by D. E. Edmondson and D. B. McCormick. Walter de Gruyter, Berlin, New York
    • O'Kane, D. J., J. Vervoort, F. Muller and J. Lee (1987) Purification and characterization of an unusual non-fluorescent flavoprotein from Photobacterium leiognathi. In Flavins and Flavoproteins (Edited by D. E. Edmondson and D. B. McCormick), pp. 641-645. Walter de Gruyter, Berlin, New York.
    • (1987) Flavins and Flavoproteins , pp. 641-645
    • O'Kane, D.J.1    Vervoort, J.2    Muller, F.3    Lee, J.4
  • 8
    • 0001971562 scopus 로고
    • 390 from P. phosphoreum
    • Edited by D. E. Edmondson and D. B. McCormick. Walter de Gruyter, Berlin, New York
    • 390 from P. phosphoreum. In Flavins and Flavoproteins (Edited by D. E. Edmondson and D. B. McCormick), pp. 647-650. Walter de Gruyter, Berlin, New York.
    • (1987) Flavins and Flavoproteins , pp. 647-650
    • Kasai, S.1    Matsui, K.2    Nakamura, T.3
  • 9
    • 0001971562 scopus 로고
    • 390 including its prosthetic group (Q-flavin): Physiological significance of light emitting reaction in luminous bacteria
    • Edited by B. Curti, S. Ronchi and G. Zanetti. Walter de Gruyter, Berlin, New York
    • 390 including its prosthetic group (Q-flavin): physiological significance of light emitting reaction in luminous bacteria. In Flavins and Flavoproteins (Edited by B. Curti, S. Ronchi and G. Zanetti), pp. 285-288. Walter de Gruyter, Berlin, New York.
    • (1991) Flavins and Flavoproteins , pp. 285-288
    • Kasai, S.1    Fujii, S.2    Miura, R.3    Odani, S.4    Nakaya, T.5    Matsui, K.6
  • 10
    • 0024300311 scopus 로고
    • A new lux gene in bioluminescent bacteria codes for a protein homologous to the bacterial luciferase subunits
    • Soly, R. R., J. A. Mancini, S. R. Ferri, M. Boylan and E. A. Meighen (1988) A new lux gene in bioluminescent bacteria codes for a protein homologous to the bacterial luciferase subunits. Biochem. Biophys. Res. Commun. 155, 351-358.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 351-358
    • Soly, R.R.1    Mancini, J.A.2    Ferri, S.R.3    Boylan, M.4    Meighen, E.A.5
  • 11
    • 0024279297 scopus 로고
    • Cloning and expression of the Photobacterium phosphoreum luminescence system demonstrates a unique lux gene organization
    • Mancini, J. A., M. Boylan, R. R. Soly, A. F. Graham and E. A. Meighen (1988) Cloning and expression of the Photobacterium phosphoreum luminescence system demonstrates a unique lux gene organization. J. Biol. Chem. 263, 14308-14314.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14308-14314
    • Mancini, J.A.1    Boylan, M.2    Soly, R.R.3    Graham, A.F.4    Meighen, E.A.5
  • 12
    • 0024692881 scopus 로고
    • The complete nucleotide sequence of the lux regulon of Vibrio fischeri and the luxABN region of Photobacterium leiognathi and the mechanism of control of bacterial bioluminescence
    • Baldwin, T. O., J. H. Devine, R. C. Heckel, J.-W. Lin and G. S. Shadel (1989) The complete nucleotide sequence of the lux regulon of Vibrio fischeri and the luxABN region of Photobacterium leiognathi and the mechanism of control of bacterial bioluminescence. J. Biolumin. Chemilumin. 4, 326-341.
    • (1989) J. Biolumin. Chemilumin. , vol.4 , pp. 326-341
    • Baldwin, T.O.1    Devine, J.H.2    Heckel, R.C.3    Lin, J.-W.4    Shadel, G.S.5
  • 13
    • 0025064130 scopus 로고
    • Isolation of bioluminescent functions from Photobacterium leiognathi: Analysis of luxA, luxB, luxG and neighboring genes
    • Illarionov, B. A., V. M. Blinov, A. P. Donchenko, M. V. Protopopova, V. A. Karginov, N. P. Mertvetsov and J. I. Gitelson (1990) Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes. Gene 86, 89-94.
    • (1990) Gene , vol.86 , pp. 89-94
    • Illarionov, B.A.1    Blinov, V.M.2    Donchenko, A.P.3    Protopopova, M.V.4    Karginov, V.A.5    Mertvetsov, N.P.6    Gitelson, J.I.7
  • 14
    • 0027310218 scopus 로고
    • Crystal structure of a flavoprotein related to the subunits of bacterial luciferase
    • Moore, S. A., M. N. G. James, D. J. O'Kane and J. Lee (1993) Crystal structure of a flavoprotein related to the subunits of bacterial luciferase. EMBO J. 12, 1767-1774.
    • (1993) EMBO J. , vol.12 , pp. 1767-1774
    • Moore, S.A.1    James, M.N.G.2    O'Kane, D.J.3    Lee, J.4
  • 16
    • 0029078856 scopus 로고
    • Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 Å resolution
    • Moore, S. A. and M. N. G. James (1995) Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 Å resolution. J. Mol. Biol. 249, 195-214.
    • (1995) J. Mol. Biol. , vol.249 , pp. 195-214
    • Moore, S.A.1    James, M.N.G.2
  • 17
    • 0028955478 scopus 로고
    • 390 from a luminescent bacterium Photobacterium phosphoreum
    • 390 from a luminescent bacterium Photobacterium phosphoreum. J. Biochem. 117, 575-578.
    • (1995) J. Biochem. , vol.117 , pp. 575-578
    • Kita, A.1    Kasai, S.2    Miki, K.3
  • 18
    • 0030020428 scopus 로고    scopus 로고
    • 390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 Å resolution
    • 390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 Å resolution. Acta Crystallogr. D52, 77-86.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 77-86
    • Kita, A.1    Kasai, S.2    Miyata, M.3    Miki, K.4
  • 19
    • 0002282588 scopus 로고    scopus 로고
    • Isolation and characterization of a fluorescent protein from a marine luminous bacteria
    • Edited by J. W. Hastings, L. J. Kricka and P. E. Stanley. John Wiley & Sons, Chichester
    • Karatani, H., T. Konaka, Y. Kitao and S. Hirayama (1997) Isolation and characterization of a fluorescent protein from a marine luminous bacteria. In Bioluminescence and Chemiluminescence, Molecular Reporting with Photons (Edited by J. W. Hastings, L. J. Kricka and P. E. Stanley), pp. 54-57. John Wiley & Sons, Chichester.
    • (1997) Bioluminescence and Chemiluminescence, Molecular Reporting with Photons , pp. 54-57
    • Karatani, H.1    Konaka, T.2    Kitao, Y.3    Hirayama, S.4
  • 20
    • 77956986992 scopus 로고
    • Isolation, identification, and manipulation of luminous bacteria
    • Nealson, K. H. (1978) Isolation, identification, and manipulation of luminous bacteria. Methods Enzymol. 57, 153-166.
    • (1978) Methods Enzymol. , vol.57 , pp. 153-166
    • Nealson, K.H.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. and J. Doly (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7, 1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 24
    • 0028260179 scopus 로고
    • Preparation of P-flavin-bound and P-flavin-free luciferase and P-flavin-bound β-subunit of luciferase from Photobacterium phosphoreum
    • Kasai, S. (1994) Preparation of P-flavin-bound and P-flavin-free luciferase and P-flavin-bound β-subunit of luciferase from Photobacterium phosphoreum. J. Biochem. (Tokyo) 115, 670-674.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 670-674
    • Kasai, S.1
  • 25
    • 0013071789 scopus 로고
    • Structure of P-flavin from P. phosphoreum
    • Edited by V. Massey and C. H. Williams. Elsevier North Holland, New York, Amsterdam, Oxford
    • Kasai, S., K. Matsui and T. Nakamura (1982) Structure of P-flavin from P. phosphoreum. In Flavins and Flavoproteins (Edited by V. Massey and C. H. Williams), pp. 459-462. Elsevier North Holland, New York, Amsterdam, Oxford.
    • (1982) Flavins and Flavoproteins , pp. 459-462
    • Kasai, S.1    Matsui, K.2    Nakamura, T.3
  • 26
    • 0026182028 scopus 로고
    • Green flavoprotein from P. leiognathi: Purification, characterization and identification as the product of the lux G(N) gene
    • Raibekas, A. A. (1991) Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene. J. Biolumin. Chemilumin. 6, 169-176.
    • (1991) J. Biolumin. Chemilumin. , vol.6 , pp. 169-176
    • Raibekas, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.