메뉴 건너뛰기




Volumn 40, Issue 2, 2005, Pages 299-318

A homologous expression system for obtaining engineered cytochrome ba 3 from Thermus thermophilus HB8

Author keywords

Cytochrome ba3; Homologous expression; Mutant forms; Thermus thermophilus

Indexed keywords


EID: 14844336371     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.11.014     Document Type: Article
Times cited : (33)

References (69)
  • 1
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa
    • T. Oshima, and K. Imahora Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa Int. J. Syst. Bacteriol. 24 1974 102 112
    • (1974) Int. J. Syst. Bacteriol. , vol.24 , pp. 102-112
    • Oshima, T.1    Imahora, K.2
  • 3
    • 0019322916 scopus 로고
    • Cytochrome oxidase from an extreme thermophile, Thermus thermophilus HB8
    • K. Hon-nami, and T. Oshima Cytochrome oxidase from an extreme thermophile, Thermus thermophilus HB8 Biochem. Biophys. Res. Commun. 92 1980 1023 1029
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 1023-1029
    • Hon-Nami, K.1    Oshima, T.2
  • 6
    • 0024061597 scopus 로고
    • Properties of a copper-containing cytochrome ba3: A second terminal oxidase from the extreme thermophile Thermus thermophilus
    • B.H. Zimmermann, C.I. Nitsche, J.A. Fee, F. Rusnak, and E. Munck Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus Proc. Natl. Acad. Sci. USA 85 1988 5779 5783
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5779-5783
    • Zimmermann, B.H.1    Nitsche, C.I.2    Fee, J.A.3    Rusnak, F.4    Munck, E.5
  • 9
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • J. Castresana, M. Lubben, M. Saraste, and D.G. Higgins Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen EMBO J. 13 1994 2516 2525
    • (1994) EMBO J. , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lubben, M.2    Saraste, M.3    Higgins, D.G.4
  • 10
    • 0032461198 scopus 로고    scopus 로고
    • 3 from strain HB8 is a sulphide resistant cytochrome c oxidase
    • 3 from strain HB8 is a sulphide resistant cytochrome c oxidase Cah. Biol. Mar. 39 1998 351 354
    • (1998) Cah. Biol. Mar. , vol.39 , pp. 351-354
    • Fee, J.A.1    Todaro, T.R.2    Sanders, D.3
  • 11
    • 0031282998 scopus 로고    scopus 로고
    • Cytochrome ba3 from Natronobacterium pharaonis-an archaeal four-subunit cytochrome-c-type oxidase
    • S. Mattar, and M. Engelhard Cytochrome ba3 from Natronobacterium pharaonis-an archaeal four-subunit cytochrome-c-type oxidase E. J. Biochem. 250 1997 332 341
    • (1997) E. J. Biochem. , vol.250 , pp. 332-341
    • Mattar, S.1    Engelhard, M.2
  • 14
    • 0028955899 scopus 로고
    • Fast reactions of cytochrome oxidase
    • O. Einarsdottir Fast reactions of cytochrome oxidase Biochim. Biophys. Acta 1229 1995 129 147
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 129-147
    • Einarsdottir, O.1
  • 16
    • 0032828960 scopus 로고    scopus 로고
    • Respiratory chains in the last common ancestor of living organisms
    • J. Castresana, and D. Moreira Respiratory chains in the last common ancestor of living organisms J. Mol. Evol. 49 1999 453 460
    • (1999) J. Mol. Evol. , vol.49 , pp. 453-460
    • Castresana, J.1    Moreira, D.2
  • 18
    • 0042307434 scopus 로고    scopus 로고
    • Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase
    • R.M. Nyquist, D. Heitbrink, C. Bolwien, R.B. Gennis, and J. Heberle Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase Proc. Natl. Acad. Sci. USA 100 2003 8715 8720
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8715-8720
    • Nyquist, R.M.1    Heitbrink, D.2    Bolwien, C.3    Gennis, R.B.4    Heberle, J.5
  • 28
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and other Thermus spp.
    • Y. Koyama, T. Hoshino, N. Tomizuka, and K. Furakawa Genetic transformation of the extreme thermophile Thermus thermophilus and other Thermus spp. J. Bacteriol. 166 1986 338 340
    • (1986) J. Bacteriol. , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furakawa, K.4
  • 29
    • 0022538679 scopus 로고
    • Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein
    • M. Matsumura, S. Yasumura, and S. Aiba Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein Nature 323 1986 356 358
    • (1986) Nature , vol.323 , pp. 356-358
    • Matsumura, M.1    Yasumura, S.2    Aiba, S.3
  • 30
    • 0026500944 scopus 로고
    • Development of plasmid cloning vectors for Thermus thermophilus HB8: Expression of a heterologous, plasmid-borne kanamycin nucleotydyltransferase gene
    • M.W. Mather, and J.A. Fee Development of plasmid cloning vectors for Thermus thermophilus HB8: expression of a heterologous, plasmid-borne kanamycin nucleotydyltransferase gene Appl. Environ. Microbiol. 58 1992 421 425
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 421-425
    • Mather, M.W.1    Fee, J.A.2
  • 31
    • 0032146328 scopus 로고    scopus 로고
    • Characterization of a plasmid replicative origin from an extreme thermophile
    • M. de Grado, I. Lasa, and J. Berenguer Characterization of a plasmid replicative origin from an extreme thermophile FEMS Microbiol. 165 1998 51 57
    • (1998) FEMS Microbiol. , vol.165 , pp. 51-57
    • De Grado, M.1    Lasa, I.2    Berenguer, J.3
  • 32
    • 0032750230 scopus 로고    scopus 로고
    • A high-transformation-efficiency cloning vector for Thermus thermophilus
    • M. de Grado, P. Castan, and J. Berenguer A high-transformation-efficiency cloning vector for Thermus thermophilus Plasmid 42 1999 241 245
    • (1999) Plasmid , vol.42 , pp. 241-245
    • De Grado, M.1    Castan, P.2    Berenguer, J.3
  • 33
    • 0030814243 scopus 로고    scopus 로고
    • Identification of a thermophilic plasmid origin and its cloning within a new Thermus-E. coli shuttle-vector
    • J. Wayne, and S.-Y. Xu Identification of a thermophilic plasmid origin and its cloning within a new Thermus-E. coli shuttle-vector Gene 195 1997 321 328
    • (1997) Gene , vol.195 , pp. 321-328
    • Wayne, J.1    Xu, S.-Y.2
  • 35
    • 0033047665 scopus 로고    scopus 로고
    • An efficient gene replacement and deletion system for an extreme thermophile, Thermus thermophilus
    • M. Tamakoshi, T. Yaoi, T. Oshima, and A. Yamagushi An efficient gene replacement and deletion system for an extreme thermophile, Thermus thermophilus FEMS Microbiol. Lett. 173 1999 431 437
    • (1999) FEMS Microbiol. Lett. , vol.173 , pp. 431-437
    • Tamakoshi, M.1    Yaoi, T.2    Oshima, T.3    Yamagushi, A.4
  • 36
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • E. Alani, L. Cao, and N. Kleckner A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains Genetics 116 1987 541 545
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 38
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • W.J. Dower, J.F. Miller, and C.W. Ragsdale High efficiency transformation of E. coli by high voltage electroporation Nucleic Acids Res. 16 1988 6127 6144
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6144
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 39
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction
    • R.M. Horton, Z. Cai, S.N. Ho, and L.R. Pease Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction BioTechniques 8 1990 528 535
    • (1990) BioTechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.2    Ho, S.N.3    Pease, L.R.4
  • 40
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes A, B, and C from pyridine hemochrome spectra
    • E.A. Berry, and B.L. Trumpower Simultaneous determination of hemes A, B, and C from pyridine hemochrome spectra Anal. Biochem. 161 1987 1 15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 42
    • 0017908773 scopus 로고
    • Transition metal electron paramagnetic resonance related to proteins
    • C.H.W. Hirs S.N. Timasheff Academic Press New York
    • J.A. Fee Transition metal electron paramagnetic resonance related to proteins C.H.W. Hirs S.N. Timasheff Enzyme Structure, Part G 1978 Academic Press New York 512 528
    • (1978) Enzyme Structure, Part G , pp. 512-528
    • Fee, J.A.1
  • 43
    • 0032524917 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the cytochrome c552 gene from Thermus thermophilus HB8. Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products
    • J.A. Keightley, D. Sanders, T.R. Todaro, A. Pastuszyn, and J.A. Fee Cloning and expression in Escherichia coli of the cytochrome c552 gene from Thermus thermophilus HB8. Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products J. Biol. Chem. 273 1998 12006 12016
    • (1998) J. Biol. Chem. , vol.273 , pp. 12006-12016
    • Keightley, J.A.1    Sanders, D.2    Todaro, T.R.3    Pastuszyn, A.4    Fee, J.A.5
  • 44
    • 0034489319 scopus 로고    scopus 로고
    • Integrity of Thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral and structural characterization of the recombinant protein
    • J.A. Fee, Y. Chen, T.R. Todaro, K.L. Bren, K.M. Patel, M.G. Hill, E. Gomez-Moran, T.M. Loehr, J. Ai, L. Thöny-Meyer, P.A. Williams, E. Stura, V. Sridhar, and D.E. McRee Integrity of Thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral and structural characterization of the recombinant protein Protein Sci. 9 2000 2074 2084
    • (2000) Protein Sci. , vol.9 , pp. 2074-2084
    • Fee, J.A.1    Chen, Y.2    Todaro, T.R.3    Bren, K.L.4    Patel, K.M.5    Hill, M.G.6    Gomez-Moran, E.7    Loehr, T.M.8    Ai, J.9    Thöny-Meyer, L.10    Williams, P.A.11    Stura, E.12    Sridhar, V.13    McRee, D.E.14
  • 46
    • 0025134659 scopus 로고
    • Plasmid associated aggregation in Thermus thermophilus HB8
    • M.W. Mather, and J.A. Fee Plasmid associated aggregation in Thermus thermophilus HB8 Plasmid 24 1990 45 56
    • (1990) Plasmid , vol.24 , pp. 45-56
    • Mather, M.W.1    Fee, J.A.2
  • 47
    • 0006485526 scopus 로고
    • A chemically defined medium for the large scale culture of Thermus thermophilus
    • K.L. Findling, T. Yoshida, and J.A. Fee A chemically defined medium for the large scale culture of Thermus thermophilus J. Biol. Chem. 259 1984 123
    • (1984) J. Biol. Chem. , vol.259 , pp. 123
    • Findling, K.L.1    Yoshida, T.2    Fee, J.A.3
  • 48
    • 1942473305 scopus 로고    scopus 로고
    • 3-type cytochrome c oxidase from Thermus thermophilus: Purification, crystallization, and crystal transformation
    • C. Hunte G. von Jagow H. Schägger Academic Press Amsterdam
    • 3-type cytochrome c oxidase from Thermus thermophilus: purification, crystallization, and crystal transformation C. Hunte G. von Jagow H. Schägger Membrane Protein Purification and Characterization: A Practical Guide 2003 Academic Press Amsterdam 229 251
    • (2003) Membrane Protein Purification and Characterization: A Practical Guide , pp. 229-251
    • Soulimane, T.1    Kiefersauer, R.2    Than, M.E.3
  • 49
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coli
    • D.M. Glover IRL Press Oxford
    • D. Hanahan Techniques for transformation of E. coli D.M. Glover DNA Cloning 1985 IRL Press Oxford 109 135
    • (1985) DNA Cloning , pp. 109-135
    • Hanahan, D.1
  • 50
    • 0027248272 scopus 로고
    • Recovery and cloning of genomic DNA fragments from dried agarose gels
    • R. Wu Academic Press New York
    • M.W. Mather, J.A. Keightley, and J.A. Fee Recovery and cloning of genomic DNA fragments from dried agarose gels R. Wu Methods in Enzymology, Recombinant DNA, Part I 1993 Academic Press New York 695 704
    • (1993) Methods in Enzymology, Recombinant DNA, Part I , pp. 695-704
    • Mather, M.W.1    Keightley, J.A.2    Fee, J.A.3
  • 51
    • 0024002905 scopus 로고
    • Base composition-independent hybridization in dried agarose gels: Screening and recovery for cloning of genomic DNA fragments
    • M.W. Mather Base composition-independent hybridization in dried agarose gels: screening and recovery for cloning of genomic DNA fragments BioTechniques 6 1988 444 447
    • (1988) BioTechniques , vol.6 , pp. 444-447
    • Mather, M.W.1
  • 53
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • D. Hanahan, J. Jessee, and F.R. Bloom Plasmid transformation of Escherichia coli and other bacteria Methods Enzymol. 101 1991 63 113
    • (1991) Methods Enzymol. , vol.101 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 55
    • 0030001222 scopus 로고    scopus 로고
    • Pyrimidine biosynthesis genes (pyrE and pyrF) of an extreme thermophile, Thermus thermophilus
    • A. Yamagishi, T. Tanimoto, T. Suzuki, and T. Oshima Pyrimidine biosynthesis genes (pyrE and pyrF) of an extreme thermophile, Thermus thermophilus Appl. Environ. Microbiol. 62 1996 2191 2194
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2191-2194
    • Yamagishi, A.1    Tanimoto, T.2    Suzuki, T.3    Oshima, T.4
  • 56
    • 0023976653 scopus 로고
    • Homologous recombination in procaryotes
    • G. Smith Homologous recombination in procaryotes Microbiol. Rev. 52 1988 1 28
    • (1988) Microbiol. Rev. , vol.52 , pp. 1-28
    • Smith, G.1
  • 57
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • K.A. Datsenko, and B.L. Wanner One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc. Natl. Acad. Sci. USA 97 2000 6640 6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 63
    • 0342378077 scopus 로고    scopus 로고
    • One-step purification of histidine-tagged cytochrome bo from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase
    • J.N. Rumbley, E.F. Nickels, and R.B. Gennis One-step purification of histidine-tagged cytochrome bo from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase Biochim. Biophys. Acta 1340 1997 131 142
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 131-142
    • Rumbley, J.N.1    Nickels, E.F.2    Gennis, R.B.3
  • 64
    • 0023096955 scopus 로고
    • Cytochrome c oxidase in prokaryotes
    • B. Ludwig Cytochrome c oxidase in prokaryotes FEMS Microbiol. Rev. 46 1987 41 56
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 41-56
    • Ludwig, B.1
  • 66
    • 0001354839 scopus 로고
    • Reductive alteration of heme a hemochromes
    • G. Vanderkooi, and E. Stotz Reductive alteration of heme A hemochromes J. Biol. Chem. 240 1965 3418 3424
    • (1965) J. Biol. Chem. , vol.240 , pp. 3418-3424
    • Vanderkooi, G.1    Stotz, E.2
  • 68
    • 0021361424 scopus 로고
    • Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase
    • J.C. Salerno Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase J. Biol. Chem. 259 1984 2331 2336
    • (1984) J. Biol. Chem. , vol.259 , pp. 2331-2336
    • Salerno, J.C.1
  • 69
    • 0026556951 scopus 로고
    • Characterization of a novel g′ = 2.95 EPR signal from the binuclear center of mitochondrial cytochrome c oxidase
    • C.E. Cooper, and J.C. Salerno Characterization of a novel g′ = 2.95 EPR signal from the binuclear center of mitochondrial cytochrome c oxidase J. Biol. Chem. 267 1992 280 285
    • (1992) J. Biol. Chem. , vol.267 , pp. 280-285
    • Cooper, C.E.1    Salerno, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.