메뉴 건너뛰기




Volumn 385, Issue 2, 2005, Pages 575-580

Random mutagenesis of bacterial luciferase: Critical role of Glu 175 in the control of luminescence decay

Author keywords

Bacterial luciferase; Bioluminescence; Decay rate; Error prone PCR; Fluorescence quenching; Random mutagenesis

Indexed keywords

ALDEHYDES; DECOMPOSITION; ENZYMES; LUMINESCENCE;

EID: 12844268096     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040863     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 0000125178 scopus 로고
    • Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide
    • Hastings, J. W. and Gibson, Q. H. (1963) Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide. J. Biol. Chem. 238, 2537-2554
    • (1963) J. Biol. Chem. , vol.238 , pp. 2537-2554
    • Hastings, J.W.1    Gibson, Q.H.2
  • 2
    • 0000445754 scopus 로고
    • The oxidation of reduced flavin mononucleotide by molecular oxygen
    • Gibson, Q. H. and Hastings, J. W. (1962) The oxidation of reduced flavin mononucleotide by molecular oxygen. Biochem. J. 83, 368-377
    • (1962) Biochem. J. , vol.83 , pp. 368-377
    • Gibson, Q.H.1    Hastings, J.W.2
  • 3
    • 0029664970 scopus 로고    scopus 로고
    • The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions
    • Fisher, A. J., Thompson, T. B., Thoden, J. B., Baldwin, T. O. and Rayment, I. (1996) The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271, 21956-21968
    • (1996) J. Biol. Chem. , vol.271 , pp. 21956-21968
    • Fisher, A.J.1    Thompson, T.B.2    Thoden, J.B.3    Baldwin, T.O.4    Rayment, I.5
  • 4
    • 0022381731 scopus 로고
    • Bacterial luciferase: Demonstration of a catalytically competent altered conformational state following a single turnover
    • AbouKhair, N. K., Ziegler, M. M. and Baldwin, T. O. (1985) Bacterial luciferase: demonstration of a catalytically competent altered conformational state following a single turnover. Biochemistry 24, 3942-3947
    • (1985) Biochemistry , vol.24 , pp. 3942-3947
    • Aboukhair, N.K.1    Ziegler, M.M.2    Baldwin, T.O.3
  • 5
    • 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
  • 6
    • 0018573528 scopus 로고
    • Bacterial bioluminescence: Its control and ecological significance
    • Nealson, K. H. and Hastings, J. W. (1979) Bacterial bioluminescence: its control and ecological significance. Microbiol. Rev. 43, 496-518
    • (1979) Microbiol. Rev. , vol.43 , pp. 496-518
    • Nealson, K.H.1    Hastings, J.W.2
  • 7
    • 0025064486 scopus 로고
    • Nucleotide sequence, expression, and properties of luciferase coded by lux genes from a terrestrial bacterium
    • Szittner, R. and Meighen, E. (1990) Nucleotide sequence, expression, and properties of luciferase coded by lux genes from a terrestrial bacterium. J. Biol. Chem. 265, 16581-16587
    • (1990) J. Biol. Chem. , vol.265 , pp. 16581-16587
    • Szittner, R.1    Meighen, E.2
  • 8
    • 0344564130 scopus 로고    scopus 로고
    • Control of luminescence decay and flavin binding by the LuxA carboxyl-terminal regions in chimeric bacterial luciferases
    • Valkova, N., Szittner, R. and Meighen, E. A. (1999) Control of luminescence decay and flavin binding by the LuxA carboxyl-terminal regions in chimeric bacterial luciferases. Biochemistry 38, 13820-13828
    • (1999) Biochemistry , vol.38 , pp. 13820-13828
    • Valkova, N.1    Szittner, R.2    Meighen, E.A.3
  • 9
    • 0015240515 scopus 로고
    • Binding site determination from kinetic data. Reduced flavin mononucleotide binding to bacterial luciferase
    • Meighen, E. A. and Hastings, J. W. (1971) Binding site determination from kinetic data. Reduced flavin mononucleotide binding to bacterial luciferase. J. Biol. Chem. 246, 7666-7674
    • (1971) J. Biol. Chem. , vol.246 , pp. 7666-7674
    • Meighen, E.A.1    Hastings, J.W.2
  • 10
    • 0016188369 scopus 로고
    • Mutated luciferases with altered bioluminescence emission spectra
    • Cline, T. W. and Hastings, J. W. (1974) Mutated luciferases with altered bioluminescence emission spectra. J. Biol. Chem. 249, 4668-4669
    • (1974) J. Biol. Chem. , vol.249 , pp. 4668-4669
    • Cline, T.W.1    Hastings, J.W.2
  • 11
    • 0027309148 scopus 로고
    • Efficient random mutagenesis method with adjustable mutation frequency by use of PCR and dITP
    • Spee, J. H., Vos, W. M. D. and Kuipers, O. P. (1993) Efficient random mutagenesis method with adjustable mutation frequency by use of PCR and dITP. Nucleic Acids Res. 21, 777-778
    • (1993) Nucleic Acids Res. , vol.21 , pp. 777-778
    • Spee, J.H.1    Vos, W.M.D.2    Kuipers, O.P.3
  • 12
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D. W., Chen, E. and Geoddel, D. V. (1989) A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1, 11-15
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Geoddel, D.V.3
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantization 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
  • 15
    • 0015919524 scopus 로고
    • Flavin specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction
    • Meighen, E. A. and Mackenzie, R. E. (1973) Flavin specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction. Biochemistry 12, 1482-1491
    • (1973) Biochemistry , vol.12 , pp. 1482-1491
    • Meighen, E.A.1    Mackenzie, R.E.2
  • 16
    • 0037413360 scopus 로고    scopus 로고
    • Adsorptive immobilization of bacterial luciferase on alkyl-substituted Sepharose 4B
    • Hosseinkhani, S., Szittner, R., Nemat-Gorgani, M. and Meighen, E. (2003) Adsorptive immobilization of bacterial luciferase on alkyl-substituted Sepharose 4B. Enzyme Microb. Technol. 32, 186-193
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 186-193
    • Hosseinkhani, S.1    Szittner, R.2    Nemat-Gorgani, M.3    Meighen, E.4
  • 17
    • 0014987250 scopus 로고
    • Stable, inexpensive, solid-state photo multiplier photometer
    • Mitchell, G. W. and Hastings, J. W. (1971) Stable, inexpensive, solid-state photo multiplier photometer. Anal. Biochem. 39, 243-250
    • (1971) Anal. Biochem. , vol.39 , pp. 243-250
    • Mitchell, G.W.1    Hastings, J.W.2
  • 18
    • 0027379161 scopus 로고
    • Subunit interactions and the role of the luxA polypeptide in controlling thermal stability and catalytic properties in recombinant luciferase hybrids
    • Li, Z., Szittner, R. and Meighen, E. A. (1993) Subunit interactions and the role of the luxA polypeptide in controlling thermal stability and catalytic properties in recombinant luciferase hybrids. Biochim. Biophys. Acta 1158, 137-145
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 137-145
    • Li, Z.1    Szittner, R.2    Meighen, E.A.3
  • 19
    • 0034918673 scopus 로고    scopus 로고
    • Modeling of bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data
    • Lin, L. Y., Sulea, T., Szittner, R., Vassilyev, V., Purisima, E. O. and Meighen, A. (2001) Modeling of bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data. Protein Sci. 10, 1563-1571
    • (2001) Protein Sci. , vol.10 , pp. 1563-1571
    • Lin, L.Y.1    Sulea, T.2    Szittner, R.3    Vassilyev, V.4    Purisima, E.O.5    Meighen, A.6
  • 20
    • 0024498481 scopus 로고
    • Random and site-directed mutagenesis of bacterial luciferase: Investigation of the aldehyde binding site
    • Chen, L. H. and Baldwin, T. O. (1989) Random and site-directed mutagenesis of bacterial luciferase: investigation of the aldehyde binding site. Biochemistry 28, 2684-2689
    • (1989) Biochemistry , vol.28 , pp. 2684-2689
    • Chen, L.H.1    Baldwin, T.O.2
  • 21
    • 0015528746 scopus 로고
    • Mutationally altered bacterial luciferase. Implications for subunit functions
    • Cline, T. W. and Hastings, J. W. (1972) Mutationally altered bacterial luciferase. Implications for subunit functions. Biochemistry 11, 3359-3370
    • (1972) Biochemistry , vol.11 , pp. 3359-3370
    • Cline, T.W.1    Hastings, J.W.2
  • 22
    • 0142248496 scopus 로고    scopus 로고
    • Directed evolution of enzymes for applied biocatalysis
    • Nicholas, J. T. (2003) Directed evolution of enzymes for applied biocatalysis. Trends Biotechnol. 21, 474-478
    • (2003) Trends Biotechnol. , vol.21 , pp. 474-478
    • Nicholas, J.T.1
  • 23
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: An update
    • Cherry, J. R. and Fidantsef, A. L. (2003) Directed evolution of industrial enzymes: an update. Curr. Opin. Biotechnol. 14, 438-443
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 25
    • 0029027663 scopus 로고
    • Three dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
    • Fisher, A. J., Raushel, F. M., Baldwin, T. O. and Rayment, I. (1995) Three dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution. Biochemistry 34, 6581-6586
    • (1995) Biochemistry , vol.34 , pp. 6581-6586
    • Fisher, A.J.1    Raushel, F.M.2    Baldwin, T.O.3    Rayment, I.4
  • 26
    • 0037031250 scopus 로고    scopus 로고
    • Implications of the reactive thiol and the proximal non-proline cis-peptide bond in the structure and function of Vibrio harveyi luciferase
    • Lin, L. Y., Sulea, T., Szittner, R., Vassilyev, V., Kor, C., Purisima, E. O. and Meighen, E. A. (2002) Implications of the reactive thiol and the proximal non-proline cis-peptide bond in the structure and function of Vibrio harveyi luciferase. Biochemistry 41, 9938-9945
    • (2002) Biochemistry , vol.41 , pp. 9938-9945
    • Lin, L.Y.1    Sulea, T.2    Szittner, R.3    Vassilyev, V.4    Kor, C.5    Purisima, E.O.6    Meighen, E.A.7
  • 27
    • 0032858233 scopus 로고    scopus 로고
    • Site-directed mutagenesis of firefly luciferase active site amino acids: A proposed model for bioluminescence color
    • Branchini, B. R., Magyer, R. A., Murtiashaw, M. H., Anderson, S. M., Helgrson, L. C. and Zimmer, M. (1999) Site-directed mutagenesis of firefly luciferase active site amino acids: a proposed model for bioluminescence color. Biochemistry 38, 13223-13230
    • (1999) Biochemistry , vol.38 , pp. 13223-13230
    • Branchini, B.R.1    Magyer, R.A.2    Murtiashaw, M.H.3    Anderson, S.M.4    Helgrson, L.C.5    Zimmer, M.6
  • 28
    • 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., Murtiashaw, 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    Murtiashaw, M.H.3    Anderson, S.M.4    Zimmer, M.5
  • 29
    • 0030000625 scopus 로고    scopus 로고
    • DNA shuffling brightens prospects for GFP
    • Matsumura, I. and Ellington, A. D. (1996) DNA shuffling brightens prospects for GFP. Nat. Biotechnol. 14, 366
    • (1996) Nat. Biotechnol. , vol.14 , pp. 366
    • Matsumura, I.1    Ellington, A.D.2
  • 30
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E. A., Tate, E. and Stemmer, W. P. (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315-319
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.