메뉴 건너뛰기




Volumn 140, Issue 4, 2006, Pages 467-474

Active-site properties of Phrixotrix railroad worm green and red bioluminescence-eliciting luciferases

Author keywords

Bioluminescence; Luciferases; Phrixotrix; Railroad worms

Indexed keywords

GREEN EMITTING LUCIFERASE; GUANIDINE; LUCIFERASE; LUCIFERIN; RED EMITTING LUCIFERASE;

EID: 33845314700     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj190     Document Type: Article
Times cited : (39)

References (45)
  • 1
    • 2442437836 scopus 로고    scopus 로고
    • Biotechnological applications of bioluminescence and chemiluminescence
    • Roda, A., Pasini, P., Michelini, E., and Guardigli, M. (2004) Biotechnological applications of bioluminescence and chemiluminescence. Trends Biotechnol. 22, 296-303
    • (2004) Trends Biotechnol. , vol.22 , pp. 296-303
    • Roda, A.1    Pasini, P.2    Michelini, E.3    Guardigli, M.4
  • 2
    • 0008380298 scopus 로고
    • Cloning of firefly luciferase cDNA and expression of active luciferase in Escherichia coli
    • De Wet, J.R., Wood, K.V., Helinsky, D.R., and DeLuca, M. (1985) Cloning of firefly luciferase cDNA and expression of active luciferase in Escherichia coli. Proc. Natl. Acad. Sci. USA 82, 7870-7873
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7870-7873
    • De Wet, J.R.1    Wood, K.V.2    Helinsky, D.R.3    DeLuca, M.4
  • 3
    • 0024653997 scopus 로고
    • Luciferase cDNA from Japanese firefly Luciola cruciata: Cloning, structure and expression in E. coli
    • Tatsumi, H., Masuda, T., Kajiyama, N., and Nakano, E. (1989) Luciferase cDNA from Japanese firefly Luciola cruciata: cloning, structure and expression in E. coli. J. Biolum. Chemilum. 3, 75-78
    • (1989) J. Biolum. Chemilum. , vol.3 , pp. 75-78
    • Tatsumi, H.1    Masuda, T.2    Kajiyama, N.3    Nakano, E.4
  • 4
    • 0026717564 scopus 로고
    • Molecular cloning and expression in E. coli of a cDNA encoding luciferase of a firefly Luciola lateralis
    • Tatsumi, H., Kajiyama, N., and Nakano, E. (1992) Molecular cloning and expression in E. coli of a cDNA encoding luciferase of a firefly Luciola lateralis. Biochem. Biophys. Acta 1131, 161-165
    • (1992) Biochem. Biophys. Acta , vol.1131 , pp. 161-165
    • Tatsumi, H.1    Kajiyama, N.2    Nakano, E.3
  • 5
    • 0027325309 scopus 로고
    • Luciferase from the East European firefly Luciola mingrelica: Cloning and nucleotide sequence of cDNA, overexpression in E. coli and purification of the enzyme
    • Devine, J.H., Kutuzova, G.D., Green, V.A., Ugarova, N.N., and Baldwin, T.O. (1993) Luciferase from the East European firefly Luciola mingrelica: cloning and nucleotide sequence of cDNA, overexpression in E. coli and purification of the enzyme. Biochem. Biophys. Acta 1173, 121-132
    • (1993) Biochem. Biophys. Acta , vol.1173 , pp. 121-132
    • Devine, J.H.1    Kutuzova, G.D.2    Green, V.A.3    Ugarova, N.N.4    Baldwin, T.O.5
  • 6
    • 0029347142 scopus 로고
    • Cloning, expression and sequence analysis of cDNA for the Japanese fireflies, Pyrocoelia miyako and Hotaria parvula
    • Ohmiya, Y., Ohba, N., Toh, H., and Tsuji, F.I. (1995) Cloning, expression and sequence analysis of cDNA for the Japanese fireflies, Pyrocoelia miyako and Hotaria parvula. Photochem. Photobiol. 62, 309-313
    • (1995) Photochem. Photobiol. , vol.62 , pp. 309-313
    • Ohmiya, Y.1    Ohba, N.2    Toh, H.3    Tsuji, F.I.4
  • 7
    • 0030034869 scopus 로고    scopus 로고
    • Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis
    • Sala-Newby, G.B., Thomson, C.M., and Campbell, A.K. (1996) Sequence and biochemical similarities between the luciferases of the glow-worm Lampyris noctiluca and the firefly Photinus pyralis. Biochem. J. 313, 761-767
    • (1996) Biochem. J. , vol.313 , pp. 761-767
    • Sala-Newby, G.B.1    Thomson, C.M.2    Campbell, A.K.3
  • 8
    • 0030895027 scopus 로고    scopus 로고
    • Cloning and sequencing of a cDNA for the firefly luciferase from Photuris pennsilvanica
    • Li Y., Buck, L.M., Scaeffer, H.J., and Leach, F.R. (1997) Cloning and sequencing of a cDNA for the firefly luciferase from Photuris pennsilvanica. Biochim. Biophys. Acta 1339, 39-52
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 39-52
    • Li, Y.1    Buck, L.M.2    Scaeffer, H.J.3    Leach, F.R.4
  • 10
    • 0002459201 scopus 로고
    • Chemistry of firefly bioluminescence
    • (Herring, P., ed.) Academic Press, New York
    • McElroy, W.D. and DeLuca, M. (1978) Chemistry of firefly bioluminescence in Bioluminescence in Action (Herring, P., ed.) pp. 109-127, Academic Press, New York
    • (1978) Bioluminescence in Action , pp. 109-127
    • McElroy, W.D.1    DeLuca, M.2
  • 11
    • 0024697665 scopus 로고
    • Luciferase of Luciola mingrelica fireflies: Kinetics and regulation mechanism
    • Ugarova, N.N. (1989) Luciferase of Luciola mingrelica fireflies: kinetics and regulation mechanism. J. Biolum. Chemilum. 4, 406-418
    • (1989) J. Biolum. Chemilum. , vol.4 , pp. 406-418
    • Ugarova, N.N.1
  • 12
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N.P., and Brick, P. (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 13
    • 0032480765 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Histidine 245 in firefly luciferase: A proposed model of the active site
    • Branchini, B.R., Magyar, R.A., Murtishaw, M.H., Anderson, S.M., and Zimmer, M. (1998) Site-directed mutagenesis of Histidine 245 in firefly luciferase: a proposed model of the active site. Biochemistry 37, 15311-15319
    • (1998) Biochemistry , vol.37 , pp. 15311-15319
    • Branchini, B.R.1    Magyar, R.A.2    Murtishaw, M.H.3    Anderson, S.M.4    Zimmer, M.5
  • 14
    • 0033173841 scopus 로고    scopus 로고
    • Model of the active site of firefly luciferase
    • Sandalova, T.P. and Ugarova, N.N. (1999) Model of the active site of firefly luciferase. Biochemistry (Moscow) 64, 962-967
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 962-967
    • Sandalova, T.P.1    Ugarova, N.N.2
  • 15
    • 0014443712 scopus 로고
    • Hydrophobic nature of the active site of firefly luciferase
    • DeLuca, M. (1969) Hydrophobic nature of the active site of firefly luciferase. Biochemistry 8, 160-166
    • (1969) Biochemistry , vol.8 , pp. 160-166
    • DeLuca, M.1
  • 16
    • 0036726517 scopus 로고    scopus 로고
    • Protein structure and bioluminescence spectra for firefly bioluminescence
    • Ugarova, N.N. and Brovko, L.Y. (2002) Protein structure and bioluminescence spectra for firefly bioluminescence. Luminescence 17, 321-330
    • (2002) Luminescence , vol.17 , pp. 321-330
    • Ugarova, N.N.1    Brovko, L.Y.2
  • 17
    • 0024967767 scopus 로고
    • Complementary DNA coding click beetle luciferases can elicit bioluminescence of different colors
    • Wood, K.W., Lam, Y.A., Seliger, H.H., and, W.D. McElroy (1989) Complementary DNA coding click beetle luciferases can elicit bioluminescence of different colors. Science 244, 700-702
    • (1989) Science , vol.244 , pp. 700-702
    • Wood, K.W.1    Lam, Y.A.2    Seliger, H.H.3    McElroy, A.W.D.4
  • 18
    • 0033174499 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the cDNA for the Brazilian larval click-beetle Pyrearinus termitilluminans luciferase
    • Viviani, V.R., Silva, A.C.R., Perez, G.L.O., Santelli, R.V., Bechara, E.J.H., and Reinach, F.C. (1999) Cloning and molecular characterization of the cDNA for the Brazilian larval click-beetle Pyrearinus termitilluminans luciferase. Photochem. Photobiol. 70, 254-260
    • (1999) Photochem. Photobiol. , vol.70 , pp. 254-260
    • Viviani, V.R.1    Silva, A.C.R.2    Perez, G.L.O.3    Santelli, R.V.4    Bechara, E.J.H.5    Reinach, F.C.6
  • 19
    • 0025412216 scopus 로고
    • Luc genes: Introduction of colors into bioluminescence assays
    • Wood, K.V. (1990) Luc genes: introduction of colors into bioluminescence assays. J. Biolum. Chemilum. 5, 107-114
    • (1990) J. Biolum. Chemilum. , vol.5 , pp. 107-114
    • Wood, K.V.1
  • 20
    • 0025879184 scopus 로고
    • Isolation and characterization of mutants of firefly luciferase which produce different colors of light
    • Kajiyama, N. and Nakano, E. (1991) Isolation and characterization of mutants of firefly luciferase which produce different colors of light. Protein Eng. 4, 691-693
    • (1991) Protein Eng. , vol.4 , pp. 691-693
    • Kajiyama, N.1    Nakano, E.2
  • 21
    • 0029881304 scopus 로고    scopus 로고
    • The structural origin of the color differences in the bioluminescence of firefly luciferase
    • Ohmiya, Y., Hirano, T., and Ohashi, T.M. (1996) The structural origin of the color differences in the bioluminescence of firefly luciferase. FEBS Lett. 384, 83-86
    • (1996) FEBS Lett. , vol.384 , pp. 83-86
    • Ohmiya, Y.1    Hirano, T.2    Ohashi, T.M.3
  • 22
    • 0029743320 scopus 로고    scopus 로고
    • Firefly luciferase: Alteration of the color of emitted light resulting from substitutions at position 286
    • Mamaev, S.V., Laikhter, A.L., Arslan, T., and Hecht, S.M. (1996) Firefly luciferase: Alteration of the color of emitted light resulting from substitutions at position 286. J. Am. Chem. Soc. 118, 7243-7244
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7243-7244
    • Mamaev, S.V.1    Laikhter, A.L.2    Arslan, T.3    Hecht, S.M.4
  • 23
    • 0035957085 scopus 로고    scopus 로고
    • The role of active site residue arginine 218 in firefly bioluminescence
    • Branchini, B.R., Magyar, R.A., Murtishaw, M.H., and Portier, N.C. (2001) The role of active site residue arginine 218 in firefly bioluminescence. Biochemistry 40, 2410-2418
    • (2001) Biochemistry , vol.40 , pp. 2410-2418
    • Branchini, B.R.1    Magyar, R.A.2    Murtishaw, M.H.3    Portier, N.C.4
  • 24
    • 0041817564 scopus 로고    scopus 로고
    • A mutagenesis study of the putative luciferin binding site residues of firefly luciferase
    • Branchini, B.R., Southworth, T.L., Murtishaw, M.H., Boije, H., and Fleet, S.E. (2003) A mutagenesis study of the putative luciferin binding site residues of firefly luciferase. Biochemistry 42, 10429-10436
    • (2003) Biochemistry , vol.42 , pp. 10429-10436
    • Branchini, B.R.1    Southworth, T.L.2    Murtishaw, M.H.3    Boije, H.4    Fleet, S.E.5
  • 25
    • 0016843233 scopus 로고
    • Modification of firefly luciferase with a luciferin analog. A red light producing enzyme
    • White, E.H. and Branchini, B. (1975) Modification of firefly luciferase with a luciferin analog. A red light producing enzyme. J. Am Chem. Soc. 97, 1243-1245
    • (1975) J. Am Chem. Soc. , vol.97 , pp. 1243-1245
    • White, E.H.1    Branchini, B.2
  • 27
    • 0037905684 scopus 로고    scopus 로고
    • Theoretical study of the amazing firefly bioluminescence: The formation and structure of the light emitters
    • Orlova, G., Goddard, J.D., and Brovko, L.Y. (2003) Theoretical study of the amazing firefly bioluminescence: the formation and structure of the light emitters. JACS 125, 6962-6971
    • (2003) JACS , vol.125 , pp. 6962-6971
    • Orlova, G.1    Goddard, J.D.2    Brovko, L.Y.3
  • 29
    • 0033614782 scopus 로고    scopus 로고
    • Cloning, sequence analysis, and expression of active Phrixothrix railroad-worms luciferases: Relationship between bioluminescence spectra and primary structures
    • Viviani, V.R., Bechara, E.J.H., and Ohmiya, Y. (1999) Cloning, sequence analysis, and expression of active Phrixothrix railroad-worms luciferases: relationship between bioluminescence spectra and primary structures. Biochemistry 38, 8271-8279
    • (1999) Biochemistry , vol.38 , pp. 8271-8279
    • Viviani, V.R.1    Bechara, E.J.H.2    Ohmiya, Y.3
  • 30
    • 0034256868 scopus 로고    scopus 로고
    • Bioluminescence color determinants of Phrixothrix railroad-worm luciferases: Chimeric luciferases, site-directed mutagenesis of Arg 215 and guanidine effect
    • Viviani, V.R. and Ohmiya, Y. (2000) Bioluminescence color determinants of Phrixothrix railroad-worm luciferases: chimeric luciferases, site-directed mutagenesis of Arg 215 and guanidine effect. Photochem. Photobiol. 72, 267-271
    • (2000) Photochem. Photobiol. , vol.72 , pp. 267-271
    • Viviani, V.R.1    Ohmiya, Y.2
  • 31
    • 0034811558 scopus 로고    scopus 로고
    • T226 is a key residue for bioluminescence spectra determination in beetle luciferases
    • Viviani, V.R., Uchida, A., Suenaga, N., Ryufuku, M., and Ohmiya, Y. (2001) T226 is a key residue for bioluminescence spectra determination in beetle luciferases. Biochem. Biophys. Res. Commun. 280, 1286-1291
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 1286-1291
    • Viviani, V.R.1    Uchida, A.2    Suenaga, N.3    Ryufuku, M.4    Ohmiya, Y.5
  • 32
    • 0036878430 scopus 로고    scopus 로고
    • The influence of Ala243(Gly247), Arg215 and Thr226(Asn230) on the bioluminescence spectra and pH-sensitivity of railroad worm, click beetle and firefly luciferases
    • Viviani, V.R., Uchida, A., Viviani, W., and Ohmiya, Y. (2002) The influence of Ala243(Gly247), Arg215 and Thr226(Asn230) on the bioluminescence spectra and pH-sensitivity of railroad worm, click beetle and firefly luciferases. Photochem. Photobiol. 76, 538-544
    • (2002) Photochem. Photobiol. , vol.76 , pp. 538-544
    • Viviani, V.R.1    Uchida, A.2    Viviani, W.3    Ohmiya, Y.4
  • 33
    • 1842815925 scopus 로고    scopus 로고
    • The influence of the region between residues 220 and 344 and beyond in Phrixotrix railroad worm luciferases green and red bioluminescence
    • Viviani, V.R., Silva Neto, A.J., and Ohmiya, Y. (2004) The influence of the region between residues 220 and 344 and beyond in Phrixotrix railroad worm luciferases green and red bioluminescence. Protein Eng. Des. Sel. 17, 113-117
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 113-117
    • Viviani, V.R.1    Silva Neto, A.J.2    Ohmiya, Y.3
  • 34
    • 9244254319 scopus 로고    scopus 로고
    • GroEL chaperone binding to beetle luciferases and the implications for refolding when co-expressed
    • Venkatesh, B., Arifuzzaman, M., Mori, H., Taguchi, T., and Ohmiya, Y. (2004) GroEL chaperone binding to beetle luciferases and the implications for refolding when co-expressed. Biosci. Biotechnol. Biochem. 68, 2096-2103
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 2096-2103
    • Venkatesh, B.1    Arifuzzaman, M.2    Mori, H.3    Taguchi, T.4    Ohmiya, Y.5
  • 36
    • 4544366731 scopus 로고    scopus 로고
    • Improved expression of novel red- and green-emitting luciferases of Phrixotrix railroad worms in mammalian cells
    • Nakajima, Y., Kimura, T., Suzuki, C., and Ohmiya, Y. (2004) Improved expression of novel red- and green-emitting luciferases of Phrixotrix railroad worms in mammalian cells. Biosci. Biotechnol. Biochem. 68, 948-951
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 948-951
    • Nakajima, Y.1    Kimura, T.2    Suzuki, C.3    Ohmiya, Y.4
  • 37
    • 2342660654 scopus 로고    scopus 로고
    • Bidirectional role of orphan nuclear receptor RORa in clock gene transcriptions demonstrated by a novel reporter assay system
    • Nakajima, Y., Ikeda, M., Kimura, T., Honma, S., Ohmiya, Y., and Honma, K. (2004) Bidirectional role of orphan nuclear receptor RORa in clock gene transcriptions demonstrated by a novel reporter assay system. FEBS Lett. 565, 122-126
    • (2004) FEBS Lett. , vol.565 , pp. 122-126
    • Nakajima, Y.1    Ikeda, M.2    Kimura, T.3    Honma, S.4    Ohmiya, Y.5    Honma, K.6
  • 38
    • 84980193682 scopus 로고
    • The quantum flux of isotopic sources
    • Hastings, J.W. and Weber, G. (1965) The quantum flux of isotopic sources. Photochem. Photobiol. 4, 1049-1050
    • (1965) Photochem. Photobiol. , vol.4 , pp. 1049-1050
    • Hastings, J.W.1    Weber, G.2
  • 40
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
    • Gulick, A.M., Starai, V.J., Horswill, A.R., Homick, K.M., and Escalante-Semerena, J.C. (2003) The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry 42, 2866-2873
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 41
    • 13444269219 scopus 로고    scopus 로고
    • Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain
    • [OLE8]
    • [OLE8] Branchini, B.R., Southworth, T.L., Murtishaw, M.H., Wilkinson, S.R., Khattak, N.F., Rosenberg, J.C., and Zimmer, M. (2005) Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain. Biochemistry 44, 1385-1393
    • (2005) Biochemistry , vol.44 , pp. 1385-1393
    • Branchini, B.R.1    Southworth, T.L.2    Murtishaw, M.H.3    Wilkinson, S.R.4    Khattak, N.F.5    Rosenberg, J.C.6    Zimmer, M.7
  • 43
    • 29144434664 scopus 로고    scopus 로고
    • Bioluminescence spectra of native and mutant firefly luciferases as a function of pH
    • Ugarova, N.N., Maloshenok, L.G., Uporow, I.V., and Kosharov, M.I. (2005) Bioluminescence spectra of native and mutant firefly luciferases as a function of pH. Biochemistry (Moscow) 70, 1262-1267
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 1262-1267
    • Ugarova, N.N.1    Maloshenok, L.G.2    Uporow, I.V.3    Kosharov, M.I.4
  • 44
    • 33747584162 scopus 로고    scopus 로고
    • Bovine serum albumin displays luciferase-like activity in presence of luciferyl-adenylate: Insights on the origin of protoluciferase activity and bioluminescence colors
    • (in press)
    • Viviani, V.R. and Ohmiya, Y. (2006) Bovine serum albumin displays luciferase-like activity in presence of luciferyl-adenylate: insights on the origin of protoluciferase activity and bioluminescence colors. Luminescence (in press)
    • (2006) Luminescence
    • Viviani, V.R.1    Ohmiya, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.