메뉴 건너뛰기




Volumn 178, Issue 6, 1996, Pages 1742-1749

Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; CYTOCHROME B; OXIDOREDUCTASE;

EID: 0029867565     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.6.1742-1749.1996     Document Type: Article
Times cited : (65)

References (44)
  • 1
    • 0028106110 scopus 로고
    • Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase
    • Atlung, T., and L. Brondsted. 1994. Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase. J. Bacteriol. 176:5414-5422.
    • (1994) J. Bacteriol. , vol.176 , pp. 5414-5422
    • Atlung, T.1    Brondsted, L.2
  • 2
    • 0023196745 scopus 로고
    • Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli
    • Au, D. C. T., and R. B. Gennis. 1987. Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli. J. Bacteriol. 169:3237-3242.
    • (1987) J. Bacteriol. , vol.169 , pp. 3237-3242
    • Au, D.C.T.1    Gennis, R.B.2
  • 4
    • 0027014332 scopus 로고
    • Compilation of superlinker vectors
    • Brosius, J. 1992. Compilation of superlinker vectors. Methods Enzymol 216:469-483.
    • (1992) Methods Enzymol , vol.216 , pp. 469-483
    • Brosius, J.1
  • 5
    • 0026006133 scopus 로고
    • A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 25 acid phosphatase (appA)
    • Dassa, J., H. Fsihi, C. Marck, M. Dion, M. Kieffer-Bontemps, and P. L. Boquet. 1991. A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 25 acid phosphatase (appA). Mol Gen. Genet. 229:341-352.
    • (1991) Mol Gen. Genet. , vol.229 , pp. 341-352
    • Dassa, J.1    Fsihi, H.2    Marck, C.3    Dion, M.4    Kieffer-Bontemps, M.5    Boquet, P.L.6
  • 6
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereaux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereaux, J.1    Haeberli, P.2    Smithies, O.3
  • 7
    • 0026533385 scopus 로고
    • The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases
    • Dikshit, R. P., K. L. Dikshit, Y. Liu, and D. A. Webster. 1992. The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases. Arch. Biochem Biophys. 293:241-245.
    • (1992) Arch. Biochem Biophys. , vol.293 , pp. 241-245
    • Dikshit, R.P.1    Dikshit, K.L.2    Liu, Y.3    Webster, D.A.4
  • 8
    • 0028207238 scopus 로고
    • An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis
    • Fernandez, J., L. Andrews, and S. M. Mische. 1994. An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis. Anal. Biochem 218:112-117
    • (1994) Anal. Biochem , vol.218 , pp. 112-117
    • Fernandez, J.1    Andrews, L.2    Mische, S.M.3
  • 10
    • 0001559827 scopus 로고
    • The cytochromes of Escherichia coli
    • Gennis, R. B. 1987. The cytochromes of Escherichia coli. FEMS Microbiol. Lett 46:387-399.
    • (1987) FEMS Microbiol. Lett , vol.46 , pp. 387-399
    • Gennis, R.B.1
  • 11
    • 0023802457 scopus 로고
    • The nucleoticle sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • Green, G. N., H. Fang, R.-J. Lin, G. Newton, M. Mather, C. D. Georgieu, and R. B. Gennis. 1988. The nucleoticle sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli J. Biol. Chem. 263:13138-13143.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13138-13143
    • Green, G.N.1    Fang, H.2    Lin, R.-J.3    Newton, G.4    Mather, M.5    Georgieu, C.D.6    Gennis, R.B.7
  • 12
    • 0026539733 scopus 로고
    • Control of electron flow in Escherichia coli: Coordinated transcription of respiratory pathway genes
    • Gunsalus, R. P. 1992. Control of electron flow in Escherichia coli: coordinated transcription of respiratory pathway genes. J. Bacteriol. 174:7069-7074.
    • (1992) J. Bacteriol. , vol.174 , pp. 7069-7074
    • Gunsalus, R.P.1
  • 13
    • 0018158720 scopus 로고
    • Preparation and properties of succinate:ubiquinone oxidoreductase (complex II)
    • Hatefi, Y. 1978. Preparation and properties of succinate:ubiquinone oxidoreductase (complex II) Methods Enzymol. 53:21-27.
    • (1978) Methods Enzymol. , vol.53 , pp. 21-27
    • Hatefi, Y.1
  • 14
    • 0026343437 scopus 로고
    • Evidence for multiple terminal oxidases, including cytochrome d, in facultatively alkaliphilic Bacillus firmus OF4
    • Hicks, D. B., R. J. Plass, and P. G. Quirk. 1991. Evidence for multiple terminal oxidases, including cytochrome d, in facultatively alkaliphilic Bacillus firmus OF4. J. Bacteriol 173:5010-5016.
    • (1991) J. Bacteriol , vol.173 , pp. 5010-5016
    • Hicks, D.B.1    Plass, R.J.2    Quirk, P.G.3
  • 15
    • 0025832166 scopus 로고
    • Adaptation of Escherichia coli to respiratory conditions: Regulation of gene expression
    • Iuchi, S., and E. C. C. Lin. 1991. Adaptation of Escherichia coli to respiratory conditions: regulation of gene expression. Cell 66:5-7.
    • (1991) Cell , vol.66 , pp. 5-7
    • Iuchi, S.1    Lin, E.C.C.2
  • 17
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii
    • Junemann, S., and J. M. Wrigglesworth. 1995. Cytochrome bd oxidase from Azotobacter vinelandii. J. Biol. Chem. 270:16213-16220.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16213-16220
    • Junemann, S.1    Wrigglesworth, J.M.2
  • 18
    • 0022821977 scopus 로고
    • Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain
    • Kita, K., K. Konishi, and Y. Anraku. 1986 Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain. Methods Enzymol. 126:94-113
    • (1986) Methods Enzymol. , vol.126 , pp. 94-113
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 19
    • 0028332212 scopus 로고
    • Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: Comparison to the complex from Escherichia coli
    • Kolonay, J. F., Jr., F. Moshiri, R. B. Gennis, T. M. Kaysser, and R. J. Maier. 1994. Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli. J. Bacteriol. 176:4177-4181.
    • (1994) J. Bacteriol. , vol.176 , pp. 4177-4181
    • Kolonay Jr., J.F.1    Moshiri, F.2    Gennis, R.B.3    Kaysser, T.M.4    Maier, R.J.5
  • 20
    • 0026475733 scopus 로고
    • Four genes in Streptomyces aureofaciens containing a domain characteristic of principal sigma factors
    • Kormanec, J., M. Farkasovsky, and L. Potuckova. 1992 Four genes in Streptomyces aureofaciens containing a domain characteristic of principal sigma factors. Gene 122:63-70.
    • (1992) Gene , vol.122 , pp. 63-70
    • Kormanec, J.1    Farkasovsky, M.2    Potuckova, L.3
  • 21
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange, R., and R. Hengge-Aronis. 1991. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol Microbiol 5:49-59.
    • (1991) Mol Microbiol , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 22
    • 0027159639 scopus 로고
    • The menaquinol oxidase of Bacillus subtilis W23
    • Lemma, E., H. Schagger, and A. Kroger. 1993. The menaquinol oxidase of Bacillus subtilis W23. Arch. Microbiol. 159:574-578.
    • (1993) Arch. Microbiol. , vol.159 , pp. 574-578
    • Lemma, E.1    Schagger, H.2    Kroger, A.3
  • 25
    • 0024976978 scopus 로고
    • EPR studies of the cytochrome-d complex of Escherichia coli
    • Meinhardt, S. VV., R. B. Gennis, and T. Ohnishi. 1989. EPR studies of the cytochrome-d complex of Escherichia coli. Biochim. Biophys Acta 975:175-184.
    • (1989) Biochim. Biophys Acta , vol.975 , pp. 175-184
    • Meinhardt, S.V.V.1    Gennis, R.B.2    Ohnishi, T.3
  • 26
    • 0021099774 scopus 로고
    • The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • Miller, M. J., and R. B. Gennis. 1983. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol. Chem 258:9159-9165.
    • (1983) J Biol. Chem , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 27
    • 0022383731 scopus 로고
    • The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli
    • Miller, M. J., and R. B. Gennis. 1985. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J. Biol. Chem. 260:14003-14008.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14003-14008
    • Miller, M.J.1    Gennis, R.B.2
  • 28
    • 0025945337 scopus 로고
    • Cloning, characterization, and expression in Escherichia coli of genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii
    • Moshiri, F., A. Chawla, and R. J. Maier. 1991. Cloning, characterization, and expression in Escherichia coli of genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii. J. Bacteriol. 173:6230-6241.
    • (1991) J. Bacteriol. , vol.173 , pp. 6230-6241
    • Moshiri, F.1    Chawla, A.2    Maier, R.J.3
  • 29
    • 0024729626 scopus 로고
    • 3 biosynthesis and sporulation in Bacillus subtilis
    • 3 biosynthesis and sporulation in Bacillus subtilis. J Bacteriol 171:4967-4978.
    • (1989) J Bacteriol , vol.171 , pp. 4967-4978
    • Mueller, J.P.1    Taber, H.W.2
  • 30
    • 0025643358 scopus 로고
    • Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA
    • Oden, K. L., L. C. DeVeaux, C. R. T. Vibat, J. E. Cronan, Jr., and R. B. Gennis. 1990 Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA. Gene 96:29-36.
    • (1990) Gene , vol.96 , pp. 29-36
    • Oden, K.L.1    Deveaux, L.C.2    Vibat, C.R.T.3    Cronan Jr., J.E.4    Gennis, R.B.5
  • 31
    • 0024469545 scopus 로고
    • Spectinomycin operon of Micrococcus luteus: Evolutionary implications of organization and novel codon usage
    • Ohama, T., A. Muto, and S. Osawa. 1989. Spectinomycin operon of Micrococcus luteus: evolutionary implications of organization and novel codon usage. J. Mol. Evol. 29:331-395
    • (1989) J. Mol. Evol. , vol.29 , pp. 331-395
    • Ohama, T.1    Muto, A.2    Osawa, S.3
  • 32
    • 0027212676 scopus 로고
    • Cloning, nucleotide sequence and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4 and an apparent amino acid racemase
    • Popham, D. L., and P. Setlow. 1993. Cloning, nucleotide sequence and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4 and an apparent amino acid racemase. J Bacteriol. 175: 2917-2925.
    • (1993) J Bacteriol. , vol.175 , pp. 2917-2925
    • Popham, D.L.1    Setlow, P.2
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 38
    • 0028046467 scopus 로고
    • Bacillus subtilis CtaA is a heme-containing membrane protein involved in heme a biosynthesis
    • Svensson, B., and L. Hederstedt. 1994. Bacillus subtilis CtaA is a heme-containing membrane protein involved in heme A biosynthesis J. Bacteriol. 176:6663-6671.
    • (1994) J. Bacteriol. , vol.176 , pp. 6663-6671
    • Svensson, B.1    Hederstedt, L.2
  • 39
    • 0027527547 scopus 로고
    • Bacillus subtilis CtaA and CtaB function in haem a biosynthesis
    • Svensson, B., M. Lubben, and L. Hederstedt. 1993. Bacillus subtilis CtaA and CtaB function in haem A biosynthesis. Mol. Microbiol. 10:193-201.
    • (1993) Mol. Microbiol. , vol.10 , pp. 193-201
    • Svensson, B.1    Lubben, M.2    Hederstedt, L.3
  • 40
    • 0028386509 scopus 로고
    • Directed disruption of the Chlamydomonas chloroplast psbK. gene destabilizes the photobystem II reaction center complex
    • Takahashi, Y., H. Matsumoto, M. Goldschmidt-Clermont, and J. D. Rochaix. 1994. Directed disruption of the Chlamydomonas chloroplast psbK. gene destabilizes the photobystem II reaction center complex Plant Mol Biol. 5:779-788.
    • (1994) Plant Mol Biol. , vol.5 , pp. 779-788
    • Takahashi, Y.1    Matsumoto, H.2    Goldschmidt-Clermont, M.3    Rochaix, J.D.4
  • 41
    • 0024457461 scopus 로고
    • Sigma H-directed transcription of citG in Bacillus subtilis
    • Tatti, K. M., H. L. Carter III, A. Moir, and C. P. Moran, Jr. 1984. Sigma H-directed transcription of citG in Bacillus subtilis. J. Bacteriol 171:5928-5932.
    • (1984) J. Bacteriol , vol.171 , pp. 5928-5932
    • Tatti, K.M.1    Carter III, H.L.2    Moir, A.3    Moran Jr., C.P.4
  • 42
    • 0025830312 scopus 로고
    • Are appR and katF the same Escherichia coli gene encoding a new sigma transcription initiation factor?
    • Touati, E., E. Dassa, J. Dassa, and P. L. Boquet. 1991. Are appR and katF the same Escherichia coli gene encoding a new sigma transcription initiation factor? Res Microbiol. 142:29-36.
    • (1991) Res Microbiol. , vol.142 , pp. 29-36
    • Touati, E.1    Dassa, E.2    Dassa, J.3    Boquet, P.L.4
  • 43
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L., and R, B. Gennis. 1994. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation Annu. Rev. Biochem. 63:675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 44
    • 0022982361 scopus 로고
    • Identification and nuelcotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonella typhimurium
    • Yu, G., and J, Hong. 1986. Identification and nuelcotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonella typhimurium Gene 45:51-57.
    • (1986) Gene , vol.45 , pp. 51-57
    • Yu, G.1    Hong, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.