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Volumn 10, Issue 6, 2011, Pages 931-938

Triple substitution G216N/A217L/S398M leads to the active and thermostable Luciola mingrelica firefly luciferase

Author keywords

[No Author keywords available]

Indexed keywords

HOTARIA PARVULA; LUCIOLA MINGRELICA;

EID: 79958032989     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/c0pp00318b     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 39049098131 scopus 로고    scopus 로고
    • Firefly luminescence: A historical perspective and recent developments
    • DOI 10.1039/b719181b
    • H. Fraga Firefly luminescence: A historical perspective and recent developments Photochem. Photobiol. Sci. 2008 7 146 158 (Pubitemid 351248642)
    • (2008) Photochemical and Photobiological Sciences , vol.7 , Issue.2 , pp. 146-158
    • Fraga, H.1
  • 3
    • 0000372063 scopus 로고
    • Spectral emission and quantum yield of firefly bioluminescence
    • H. H. Seliger W. D. McElroy Spectral emission and quantum yield of firefly bioluminescence Arch. Biochem. Biophys. 1960 88 136 141
    • (1960) Arch. Biochem. Biophys. , vol.88 , pp. 136-141
    • Seliger, H.H.1    McElroy, W.D.2
  • 4
    • 0033935718 scopus 로고    scopus 로고
    • Use of firefly luciferase in ATP-related assays of biomass, enzymes, and metabolites
    • A. Lundin Use of firefly luciferase in ATP-related assays of biomass, enzymes, and metabolites Methods Enzymol. 2000 305 346 370 (Pubitemid 30421277)
    • (2000) Methods in Enzymology , vol.305 , pp. 346-370
    • Lundin, A.1
  • 5
    • 84889468913 scopus 로고    scopus 로고
    • Beetle Luciferases: Colorful Lights on Biological Processes and Diseases, in
    • S. Daunert and S. K. Deo, Wiley-VCH, Weinheim
    • V. R. Viviani and Y. Ohmiya, Beetle Luciferases: Colorful Lights on Biological Processes and Diseases, in Photoproteins in Bioanalysis, ed., S. Daunert, and, S. K. Deo, Wiley-VCH, Weinheim, 2006, pp. 49-63
    • (2006) Photoproteins in Bioanalysis, Ed. , pp. 49-63
    • Viviani, V.R.1    Ohmiya, Y.2
  • 6
    • 65449167679 scopus 로고    scopus 로고
    • Engineered luciferases for molecular sensing in living cells
    • B. Binkowski F. Fan K. Wood Engineered luciferases for molecular sensing in living cells Curr. Opin. Biotechnol. 2009 20 14 18
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 14-18
    • Binkowski, B.1    Fan, F.2    Wood, K.3
  • 7
    • 0037334448 scopus 로고    scopus 로고
    • Method enabling firefly luciferase-based bioluminometric assays at elevated temperatures
    • DOI 10.1016/S0003-2697(02)00647-4
    • J. Eriksson T. Nordstrom P. Nyren Method enabling firefly luciferase-based bioluminometric assays at elevated temperatures Anal. Biochem. 2003 314 158 161 (Pubitemid 36299033)
    • (2003) Analytical Biochemistry , vol.314 , Issue.1 , pp. 158-161
    • Eriksson, J.1    Nordstrom, T.2    Nyren, P.3
  • 8
    • 44349116656 scopus 로고    scopus 로고
    • Stabilization of ATP reagents containing firefly L. mingrelica luciferase by polyols
    • N. Moroz D. Gurskii N. Ugarova Stabilization of ATP reagents containing firefly L. mingrelica luciferase by polyols Moscow Univ. Chem. Bull. 2008 63 67 70
    • (2008) Moscow Univ. Chem. Bull. , vol.63 , pp. 67-70
    • Moroz, N.1    Gurskii, D.2    Ugarova, N.3
  • 10
    • 0038654305 scopus 로고    scopus 로고
    • Creation of a thermostable firefly luciferase with pH-insensitive luminescent color
    • A. Kitayama H. Yoshizaki Y. Ohmiya H. Ueda T. Nagamune Creation of a thermostable firefly luciferase with pH-insensitive luminescent color Photochem. Photobiol. 2003 77 333 338
    • (2003) Photochem. Photobiol. , vol.77 , pp. 333-338
    • Kitayama, A.1    Yoshizaki, H.2    Ohmiya, Y.3    Ueda, H.4    Nagamune, T.5
  • 11
    • 33746075234 scopus 로고    scopus 로고
    • Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance
    • DOI 10.1042/BJ20051847
    • G. H. Law O. A. Gandelman L. C. Tisi C. R. Lowe J. A. Murray Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH tolerance Biochem. J. 2006 397 305 312 (Pubitemid 44076900)
    • (2006) Biochemical Journal , vol.397 , Issue.2 , pp. 305-312
    • Law, G.H.E.1    Gandelman, O.A.2    Tisi, L.C.3    Lowe, C.R.4    Murray, J.A.H.5
  • 12
    • 77954995716 scopus 로고    scopus 로고
    • Design and introduction of a disulfide bridge in firefly luciferase: Increase of thermostability and decrease of pH sensitivity
    • M. Imani S. Hosseinkhani S. Ahmadian M. Nazari Design and introduction of a disulfide bridge in firefly luciferase: increase of thermostability and decrease of pH sensitivity Photochem. Photobiol. Sci. 2010 9 1167 1177
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1167-1177
    • Imani, M.1    Hosseinkhani, S.2    Ahmadian, S.3    Nazari, M.4
  • 13
    • 0027768880 scopus 로고
    • Thermostabilization of firefly luciferase by a single amino acid substitution at position 217
    • DOI 10.1021/bi00213a007
    • N. Kajiyama E. Nakano Thermostabilization of firefly luciferase by a single amino acid substitution at position 217 Biochemistry 1993 32 13795 13799 (Pubitemid 24018229)
    • (1993) Biochemistry , vol.32 , Issue.50 , pp. 13795-13799
    • Kajiyama, N.1    Nakano, E.2
  • 14
    • 0029825395 scopus 로고    scopus 로고
    • Improved thermostability of the North American firefly luciferase: Saturation mutagenesis at position 354
    • P. J. White D. J. Squirrell P. Arnaud C. R. Lowe J. A. Murray Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354 Biochem. J. 1996 319 343 350 (Pubitemid 26372188)
    • (1996) Biochemical Journal , vol.319 , Issue.2 , pp. 343-350
    • White, P.J.1    Squirrell, D.J.2    Arnaud, P.3    Lowe, C.R.4    Murray, J.A.H.5
  • 16
    • 79958063999 scopus 로고    scopus 로고
    • Thermostability enhancement of Luciola mingrelica firefly luciferase by in vivo directed evolution
    • M. I. Koksharov N. N. Ugarova Thermostability enhancement of Luciola mingrelica firefly luciferase by in vivo directed evolution Luminescence 2010 25 135 136
    • (2010) Luminescence , vol.25 , pp. 135-136
    • Koksharov, M.I.1    Ugarova, N.N.2
  • 18
    • 21144438190 scopus 로고    scopus 로고
    • An improved system for competent cell preparation and high efficiency plasmid transformation using different Escherichia coli strains
    • Z. Tu G. He K. X. Li M. J. Chen J. Chang L. Chen Q. Yao D. P. Liu H. Ye J. Shi X. Wu An improved system for competent cell preparation and high efficiency plasmid transformation using different Escherichia coli strains Electron. J. Biotechnol. 2005 8 113 120 (Pubitemid 40721110)
    • (2005) Electronic Journal of Biotechnology , vol.8 , Issue.1 , pp. 113-120
    • Tu, Z.1    He, G.2    Li, K.X.3    Chen, M.J.4    Chang, J.5    Chen, L.6    Yao, Q.7    Liu, D.P.8    Ye, H.9    Shi, J.10    Wu, X.11
  • 19
    • 50849086704 scopus 로고    scopus 로고
    • Random mutagenesis of Luciola mingrelica firefly luciferase. Mutant enzymes whose bioluminescence spectra show low pH-sensitivity
    • M. I. Koksharov N. N. Ugarova Random mutagenesis of Luciola mingrelica firefly luciferase. Mutant enzymes whose bioluminescence spectra show low pH-sensitivity Biochemistry (Moscow) 2008 73 862 869
    • (2008) Biochemistry (Moscow) , vol.73 , pp. 862-869
    • Koksharov, M.I.1    Ugarova, N.N.2
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • S. N. Ho H. D. Hunt R. M. Horton J. K. Pullen L. R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 1989 77 51 59 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • T. A. Hall BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT Nucl. Acids. Symp. Ser. 1999 41 95 98
    • (1999) Nucl. Acids. Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 22
    • 0028454414 scopus 로고
    • Enhancement of thermostability of firefly luciferase from Luciola lateralis by a single amino acid substitution
    • N. Kajiyama E. Nakano Enhancement of thermostability of firefly luciferase from Luciola lateralis by a single amino acid substitution Biosci., Biotechnol., Biochem. 1994 58 1170 1171
    • (1994) Biosci., Biotechnol., Biochem. , vol.58 , pp. 1170-1171
    • Kajiyama, N.1    Nakano, E.2
  • 23
    • 0001829592 scopus 로고    scopus 로고
    • Genetic engineering of firefly luciferase towards its use as a label in gene probe assays and immunoassays, in
    • J. W. Hastings, L. J. Kricka and P. E. Stanley, John Wiley & Sons, Chichester
    • R. Price, D. Squirrell, M. Murphy and P. White, Genetic engineering of firefly luciferase towards its use as a label in gene probe assays and immunoassays, in Bioluminescence and Chemiluminescence: Molecular Reporting with Photons, ed., J. W. Hastings, L. J. Kricka, and, P. E. Stanley, John Wiley & Sons, Chichester, 1997, pp. 220-223
    • (1997) Bioluminescence and Chemiluminescence: Molecular Reporting with Photons, Ed. , pp. 220-223
    • Price, R.1    Squirrell, D.2    Murphy, M.3    White, P.4
  • 25
    • 0024697665 scopus 로고
    • Luciferase of Luciola mingrelica fireflies. Kinetics and regulation mechanism
    • N. N. Ugarova Luciferase of Luciola mingrelica fireflies. Kinetics and regulation mechanism J. Biolumin. Chemilumin. 1989 4 406 418
    • (1989) J. Biolumin. Chemilumin. , vol.4 , pp. 406-418
    • Ugarova, N.N.1
  • 26
    • 0036865977 scopus 로고    scopus 로고
    • The origin, diversity, and structure function relationships of insect luciferases
    • DOI 10.1007/PL00012509
    • V. R. Viviani The origin, diversity, and structure function relationships of insect luciferases Cell. Mol. Life Sci. 2002 59 1833 1850 (Pubitemid 36015859)
    • (2002) Cellular and Molecular Life Sciences , vol.59 , Issue.11 , pp. 1833-1850
    • Viviani, V.R.1
  • 27
    • 0002468820 scopus 로고
    • The Colors of Firefly Bioluminescence: Enzyme Configuration and Species Specificity
    • H. H. Seliger W. D. McElroy The Colors of Firefly Bioluminescence: Enzyme Configuration and Species Specificity Proc. Natl. Acad. Sci. U. S. A. 1964 52 75 81
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.52 , pp. 75-81
    • Seliger, H.H.1    McElroy, W.D.2
  • 28
    • 0036726517 scopus 로고    scopus 로고
    • Protein structure and bioluminescent spectra for firefly bioluminescence
    • DOI 10.1002/bio.688
    • N. N. Ugarova L. Y. Brovko Protein structure and bioluminescent spectra for firefly bioluminescence Luminescence 2002 17 321 330 (Pubitemid 135694429)
    • (2002) Luminescence , vol.17 , Issue.5 , pp. 321-330
    • Ugarova, N.N.1    Brovko, L.Y.2
  • 29
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering experiments
    • DOI 10.1016/0959-440X(93)90205-Y
    • A. R. Fersht Principles of protein stability derived from protein engineering experiments Curr. Opin. Struct. Biol. 1993 3 75 83 (Pubitemid 23058386)
    • (1993) Current Opinion in Structural Biology , vol.3 , Issue.1 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 30
    • 31544468954 scopus 로고    scopus 로고
    • Bioluminescence spectra of native and mutant firefly luciferases as a function of pH
    • DOI 10.1007/s10541-005-0257-2
    • N. N. Ugarova L. G. Maloshenok I. V. Uporov M. I. Koksharov Bioluminescence Spectra of Native and Mutant Firefly Luciferases as a Function of pH Biochemistry (Moscow) 2005 70 1262 1267 (Pubitemid 41802123)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.11 , pp. 1262-1267
    • Ugarova, N.N.1    Maloshenok, L.G.2    Uporov, I.V.3    Koksharov, M.I.4
  • 31
    • 0035957085 scopus 로고    scopus 로고
    • The role of active site residue arginine 218 in firefly luciferase bioluminescence
    • DOI 10.1021/bi002246m
    • B. R. Branchini R. A. Magyar M. H. Murtiashaw N. C. Portier The role of active site residue arginine 218 in firefly luciferase bioluminescence Biochemistry 2001 40 2410 2418 (Pubitemid 32171713)
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2410-2418
    • Branchini, B.R.1    Magyar, R.A.2    Murtiashaw, M.H.3    Portier, N.C.4
  • 32
    • 0031784872 scopus 로고    scopus 로고
    • Structural basis for the inhibition of firefly luciferase by a general anesthetic
    • N. P. Franks A. Jenkins E. Conti W. R. Lieb P. Brick Structural Basis for the Inhibition of Firefly Luciferase by a General Anesthetic Biophys. J. 1998 75 2205 2211 (Pubitemid 28492103)
    • (1998) Biophysical Journal , vol.75 , Issue.5 , pp. 2205-2211
    • Franks, N.P.1    Jenkins, A.2    Conti, E.3    Lieb, W.R.4    Brick, P.5


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