메뉴 건너뛰기




Volumn 150, Issue 2, 2004, Pages 415-425

CtaG is required for formation of active cytochrome c oxidase in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COPPER ION; CYTOCHROME C OXIDASE; HEME; MEMBRANE PROTEIN; PROTEIN CTAG; PROTEIN YPMQ; UNCLASSIFIED DRUG;

EID: 1242273761     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26691-0     Document Type: Article
Times cited : (23)

References (50)
  • 2
    • 0037151096 scopus 로고    scopus 로고
    • Purification and characterization of yeast Sco1p, a mitochondrial copper protein
    • Beers, J., Glerum, D. M. & Tzagoloff, A. (2002). Purification and characterization of yeast Sco1p, a mitochondrial copper protein. J Biol Chem 277, 22185-22190.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22185-22190
    • Beers, J.1    Glerum, D.M.2    Tzagoloff, A.3
  • 4
    • 0032900982 scopus 로고    scopus 로고
    • Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein
    • Bengtsson, J., Tjalsma, H., Rivolta, C. & Hederstedt, L. (1999). Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein. J Bacteriol 181, 685-688.
    • (1999) J. Bacteriol. , vol.181 , pp. 685-688
    • Bengtsson, J.1    Tjalsma, H.2    Rivolta, C.3    Hederstedt, L.4
  • 5
    • 0034711013 scopus 로고    scopus 로고
    • Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides
    • Bratton, M. R., Hiser, L., Antholine, W. E., Hoganson, C. & Hosler, J. P. (2000). Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry 39, 12989-12995.
    • (2000) Biochemistry , vol.39 , pp. 12989-12995
    • Bratton, M.R.1    Hiser, L.2    Antholine, W.E.3    Hoganson, C.4    Hosler, J.P.5
  • 6
    • 0037163087 scopus 로고    scopus 로고
    • Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein
    • Carr, H. S., George, G. N. & Winge, D. R. (2002). Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein. J Biol Chem 277, 31237-31242.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 7
    • 0033930194 scopus 로고    scopus 로고
    • Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes
    • Chinenov, Y. V. (2000). Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. J Mol Med 78, 239-242.
    • (2000) J. Mol. Med. , vol.78 , pp. 239-242
    • Chinenov, Y.V.1
  • 8
    • 0034282737 scopus 로고    scopus 로고
    • A human SCO2 mutation helps define the role of Sco1p in the cytochrome oxidase assembly pathway
    • Dickinson, E. K., Adams, D. L., Schon, E. A. & Glerum, D. M. (2000). A human SCO2 mutation helps define the role of Sco1p in the cytochrome oxidase assembly pathway. J Biol Chem 275, 26780-26785.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26780-26785
    • Dickinson, E.K.1    Adams, D.L.2    Schon, E.A.3    Glerum, D.M.4
  • 9
    • 0014273491 scopus 로고
    • Analysis of sporulation mutants: II. Mutants blocked in the citric acid cycle
    • Fortnagel, P. & Freese, E. (1968). Analysis of sporulation mutants: II. Mutants blocked in the citric acid cycle. J Bacteriol 95, 1431-1438.
    • (1968) J. Bacteriol. , vol.95 , pp. 1431-1438
    • Fortnagel, P.1    Freese, E.2
  • 10
  • 11
    • 0022822105 scopus 로고
    • Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex
    • Hederstedt, L. (1986). Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. Methods Enzymol 126, 399-414.
    • (1986) Methods Enzymol. , vol.126 , pp. 399-414
    • Hederstedt, L.1
  • 13
    • 0025840353 scopus 로고
    • Genetic analysis in Bacillus subtilis
    • Hoch, J. A. (1991). Genetic analysis in Bacillus subtilis. Methods Enzymol 204, 305-320.
    • (1991) Methods Enzymol. , vol.204 , pp. 305-320
    • Hoch, J.A.1
  • 14
    • 0019877072 scopus 로고
    • Rapid and efficient cosmid cloning
    • Ish-Horowicz, D. & Burke, J. F. (1981). Rapid and efficient cosmid cloning. Nucleic Acids Res 9, 2989-2998.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2989-2998
    • Ish-Horowicz, D.1    Burke, J.F.2
  • 15
    • 0033025509 scopus 로고    scopus 로고
    • Organization of genes for tetrapyrrole biosynthesis in Gram-positive bacteria
    • Johansson, P. & Hederstedt, L. (1999). Organization of genes for tetrapyrrole biosynthesis in Gram-positive bacteria. Microbiology 145, 529-538.
    • (1999) Microbiology , vol.145 , pp. 529-538
    • Johansson, P.1    Hederstedt, L.2
  • 16
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • 148 other authors
    • Kunst, F., Ogasawara, N., Moszer, I. & 148 other authors (1997). The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 17
    • 0034058146 scopus 로고    scopus 로고
    • Genes required for cytochrome c synthesis in Bacillus subtilis
    • Le Brun, N. E., Bengtsson, J. & Hederstedt, L. (2000). Genes required for cytochrome c synthesis in Bacillus subtilis. Mol Microbiol 36, 638-650.
    • (2000) Mol. Microbiol. , vol.36 , pp. 638-650
    • Le Brun, N.E.1    Bengtsson, J.2    Hederstedt, L.3
  • 18
    • 0027159639 scopus 로고
    • The menaquinol oxidase of Bacillus subtilis W23
    • Lemma, E., Schägger, H. & Kröger, A. (1993). The menaquinol oxidase of Bacillus subtilis W23. Arch Microbiol 159, 574-578.
    • (1993) Arch. Microbiol. , vol.159 , pp. 574-578
    • Lemma, E.1    Schägger, H.2    Kröger, A.3
  • 19
    • 0031726032 scopus 로고    scopus 로고
    • Catabolite regulation of the Bacillus subtilis ctaBCDEF gene cluster
    • Liu, X. & Taber, H. W. (1998). Catabolite regulation of the Bacillus subtilis ctaBCDEF gene cluster. J Bacteriol 180, 6154-6163.
    • (1998) J. Bacteriol. , vol.180 , pp. 6154-6163
    • Liu, X.1    Taber, H.W.2
  • 20
    • 0034680823 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Interaction between Sco1p and Cox2p
    • Lode, A., Kuschel, M., Paret, C. & Rödel, G. (2000). Mitochondrial copper metabolism in yeast: interaction between Sco1p and Cox2p. FEBS Lett 485, 19-24.
    • (2000) FEBS Lett. , vol.485 , pp. 19-24
    • Lode, A.1    Kuschel, M.2    Paret, C.3    Rödel, G.4
  • 21
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. (1961). A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol 3, 208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 22
    • 0034666433 scopus 로고    scopus 로고
    • Characterization of YmpQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis
    • Mattatall, N. R., Jazairi, J. & Hill, B. C. (2000). Characterization of YmpQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J Biol Chem 275, 28802-28809.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28802-28809
    • Mattatall, N.R.1    Jazairi, J.2    Hill, B.C.3
  • 23
    • 0037042213 scopus 로고    scopus 로고
    • PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity
    • McEwan, A. G., Lewin, A., Davy, S. L., Boetzel, R., Leech, A., Walker, D., Wood, T. & Moore, G. R. (2002). PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity. FEBS Lett 518, 10-16.
    • (2002) FEBS Lett. , vol.518 , pp. 10-16
    • McEwan, A.G.1    Lewin, A.2    Davy, S.L.3    Boetzel, R.4    Leech, A.5    Walker, D.6    Wood, T.7    Moore, G.R.8
  • 25
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function, is a Cu(I)-binding protein
    • Nittis, T., George, G. N. & Winge, D. R. (2001). Yeast Sco1, a protein essential for cytochrome c oxidase function, is a Cu(I)-binding protein. J Biol Chem 276, 42520-42526.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 27
    • 0043234457 scopus 로고    scopus 로고
    • Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase
    • Punter, F. A. & Glerum, D. M. (2003). Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase. J Biol Chem 278, 30875-30880.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30875-30880
    • Punter, F.A.1    Glerum, D.M.2
  • 28
    • 0033025125 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase
    • Rentzsch, A., Krummeck-Weiss, G., Hofer, A., Bartuschka, A., Ostermann, K. & Rödel, G. (1999). Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Curr Genet 35, 103-108.
    • (1999) Curr. Genet. , vol.35 , pp. 103-108
    • Rentzsch, A.1    Krummeck-Weiss, G.2    Hofer, A.3    Bartuschka, A.4    Ostermann, K.5    Rödel, G.6
  • 29
    • 0037090630 scopus 로고    scopus 로고
    • Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations
    • Salviati, L., Hernandez-Rosa, E., Walker, W. F., Sacconi, S., DiMauro, S., Schon, E. A. & Davidson, M. M. (2002). Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations. Biochem J 363, 321-327.
    • (2002) Biochem. J. , vol.363 , pp. 321-327
    • Salviati, L.1    Hernandez-Rosa, E.2    Walker, W.F.3    Sacconi, S.4    DiMauro, S.5    Schon, E.A.6    Davidson, M.M.7
  • 33
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (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
    • Schägger, H.1    von Jagow, G.2
  • 34
    • 0030897419 scopus 로고    scopus 로고
    • Identification and characterization of the ccdA gene required for cytochrome c synthesis in Bacillus subtilis
    • Schiött, T., von Wachenfeldt, C. & Hederstedt, L. (1997a). Identification and characterization of the ccdA gene required for cytochrome c synthesis in Bacillus subtilis. J Bacteriol 179, 1962-1973.
    • (1997) J. Bacteriol. , vol.179 , pp. 1962-1973
    • Schiött, T.1    von Wachenfeldt, C.2    Hederstedt, L.3
  • 35
    • 0038228616 scopus 로고    scopus 로고
    • Bacillus subtilis CcdA defective mutants are blocked in a late step of cytochrome c biogenesis
    • Schiött, T., Trone-Holst, M. & Hederstedt, L. (1997b). Bacillus subtilis CcdA defective mutants are blocked in a late step of cytochrome c biogenesis. J Bacteriol 179, 4523-4529.
    • (1997) J. Bacteriol. , vol.179 , pp. 4523-4529
    • Schiött, T.1    Trone-Holst, M.2    Hederstedt, L.3
  • 37
    • 0037494813 scopus 로고    scopus 로고
    • A Sco homologue plays a role in defence against oxidative stress in pathogenic Neisseria
    • Seib, K. L., Jennings, M. P. & McEwan, A. G. (2003). A Sco homologue plays a role in defence against oxidative stress in pathogenic Neisseria. FEBS Lett 546, 411-415.
    • (2003) FEBS Lett. , vol.546 , pp. 411-415
    • Seib, K.L.1    Jennings, M.P.2    McEwan, A.G.3
  • 38
    • 0023853759 scopus 로고
    • Processing of a sporulation sigma factor in Bacillus subtilis. How morphological structure could control gene expression
    • Stragier, P., Bonamy, C. & Karmazyn-Campelli, C. (1988). Processing of a sporulation sigma factor in Bacillus subtilis. How morphological structure could control gene expression. Cell 532, 697-704.
    • (1988) Cell , vol.532 , pp. 697-704
    • Stragier, P.1    Bonamy, C.2    Karmazyn-Campelli, C.3
  • 39
    • 0027527547 scopus 로고
    • Bacillus subtilis CtaA and CtaB function in haem A biosynthesis
    • Svensson, B., Lübben, M. & Hederstedt, L. (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    Lübben, M.2    Hederstedt, L.3
  • 40
    • 0035162592 scopus 로고    scopus 로고
    • The COG database: New developments in phylogenetic classification of proteins from complete genomes
    • 7 other authors
    • Tatusov, R. L., Natale, D. A., Garkavtsev, I. V. & 7 other authors (2001). The COG database: new developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res 29, 22-28.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 22-28
    • Tatusov, R.L.1    Natale, D.A.2    Garkavtsev, I.V.3
  • 41
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. (1997). Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61, 337-376.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 42
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • Tzagoloff, A. & Dieckman, C. C. (1990). PET genes of Saccharomyces cerevisiae. Microbiol Rev 54, 211-225.
    • (1990) Microbiol. Rev. , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckman, C.C.2
  • 44
    • 0027121323 scopus 로고
    • Molecular biology of Bacillus subtilis cytochromes
    • von Wachenfeldt, C. & Hederstedt, L. (1992). Molecular biology of Bacillus subtilis cytochromes. FEMS Microbiol Lett 100, 91-100.
    • (1992) FEMS Microbiol. Lett. , vol.100 , pp. 91-100
    • von Wachenfeldt, C.1    Hederstedt, L.2
  • 45
    • 0027403011 scopus 로고
    • Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550
    • von Wachenfeldt, C. & Hederstedt, L. (1993). Physico-chemical characterisation of membrane-bound and water-soluble forms of Bacillus subtilis cytochrome c-550. Eur J Biochem 212, 499-509.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 499-509
    • von Wachenfeldt, C.1    Hederstedt, L.2
  • 46
    • 0013132577 scopus 로고    scopus 로고
    • Respiratory cytochromes, other heme proteins, and heme biosynthesis
    • Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology
    • von Wachenfeldt, C. & Hederstedt, L. (2002). Respiratory cytochromes, other heme proteins, and heme biosynthesis. In Bacillus subtilis and its Closest Relatives: from Genes to Cells, pp. 163-179. Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells , pp. 163-179
    • von Wachenfeldt, C.1    Hederstedt, L.2
  • 49
    • 0032415869 scopus 로고    scopus 로고
    • Cytochrome bd biosynthesis in Bacillus subtilis: Characterization of the cydABCD operon
    • Winstedt, L., Youshida, K., Fujita, Y. & von Wachenfeldt, C. (1998). Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon. J Bacteriol 180, 6571-6580.
    • (1998) J. Bacteriol. , vol.180 , pp. 6571-6580
    • Winstedt, L.1    Youshida, K.2    Fujita, Y.3    von Wachenfeldt, C.4
  • 50
    • 0028840368 scopus 로고
    • The cytochrome bc complex (menaquinol:Cytochrome c reductase) in Bacillus subtilis has a non-traditional subunit organization
    • Yu, J., Hederstedt, L. & Piggot, P. (1995). The cytochrome bc complex (menaquinol:cytochrome c reductase) in Bacillus subtilis has a non-traditional subunit organization. J Bacteriol 177, 6751-6760.
    • (1995) J. Bacteriol. , vol.177 , pp. 6751-6760
    • Yu, J.1    Hederstedt, L.2    Piggot, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.