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Volumn 35, Issue 1, 2000, Pages 123-138

Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHAPERONE; COPROPORPHYRIN; CYSTEINE; CYTOCHROME C; HISTIDINE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); PROTOPORPHYRIN;

EID: 0033982955     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01683.x     Document Type: Article
Times cited : (85)

References (76)
  • 1
    • 0024585335 scopus 로고
    • Structural and functional analysis of transcriptional control of the Rhodobacter capsulatus puf operon
    • Adams, C.W., Forrest, M.E., Cohen, S.N., and Beatty, J.T. (1989) Structural and functional analysis of transcriptional control of the Rhodobacter capsulatus puf operon. J Bacteriol 171: 473-482.
    • (1989) J Bacteriol , vol.171 , pp. 473-482
    • Adams, C.W.1    Forrest, M.E.2    Cohen, S.N.3    Beatty, J.T.4
  • 2
    • 0030571513 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the Rhizobium etli ccmA and ccmB genes involved in c-type cytochrome biogenesis
    • Aguilar, G.R., and Soberón, M. (1996) Cloning and sequence analysis of the Rhizobium etli ccmA and ccmB genes involved in c-type cytochrome biogenesis. Gene 182: 129-135.
    • (1996) Gene , vol.182 , pp. 129-135
    • Aguilar, G.R.1    Soberón, M.2
  • 4
    • 0027502357 scopus 로고
    • Cytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein
    • Beckman, D.L., and Kranz, R.G. (1993) Cytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein. Proc Natl Acad Sci USA 90: 2179-2183.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2179-2183
    • Beckman, D.L.1    Kranz, R.G.2
  • 5
    • 0026540658 scopus 로고
    • Bacterial cytochromes c biogenesis
    • Beckman, D.L., Trawick, D.R., and Kranz, R.G. (1992) Bacterial cytochromes c biogenesis. Genes Dev 6: 268-283.
    • (1992) Genes Dev , vol.6 , pp. 268-283
    • Beckman, D.L.1    Trawick, D.R.2    Kranz, R.G.3
  • 6
    • 0025219623 scopus 로고
    • Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins
    • Biel, S.W., and Biel, A.J. (1990) Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins. J Bacteriol 172: 1321-1326.
    • (1990) J Bacteriol , vol.172 , pp. 1321-1326
    • Biel, S.W.1    Biel, A.J.2
  • 7
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphate synthesis using deletions and φ80 transducing phages
    • Brickman, E., and Beckwith, J. (1975) Analysis of the regulation of Escherichia coli alkaline phosphate synthesis using deletions and φ80 transducing phages. J Mol Biol 96: 307-316.
    • (1975) J Mol Biol , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 8
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D. et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 9
    • 0028930524 scopus 로고
    • The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain
    • Crooke, H., and Cole, J. (1995) The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol Microbiol 15: 1139-1150.
    • (1995) Mol Microbiol , vol.15 , pp. 1139-1150
    • Crooke, H.1    Cole, J.2
  • 11
    • 0029088169 scopus 로고
    • Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum
    • Delgado, M.J., Yeoman, K.H., Guanghui, W., Vargas, C., Davies, A.E., Poole, R.K., et al. (1995) Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum. J Bacteriol 177: 4927-4934.
    • (1995) J Bacteriol , vol.177 , pp. 4927-4934
    • Delgado, M.J.1    Yeoman, K.H.2    Guanghui, W.3    Vargas, C.4    Davies, A.E.5    Poole, R.K.6
  • 12
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression
    • Ditta, G., Schmidhauser, T., Yacobson, E., Lu, P., Liang, X., Finlay, D.R., et al. (1985) Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression. Plasmid 13: 149-153.
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditta, G.1    Schmidhauser, T.2    Yacobson, E.3    Lu, P.4    Liang, X.5    Finlay, D.R.6
  • 13
    • 0024978590 scopus 로고
    • Cloning and analysis of the Neurospora crassa gene for cytochrome c heme lyase
    • Drygas, M., Lambowitz, A.M., and Nargang, F.E. (1989) Cloning and analysis of the Neurospora crassa gene for cytochrome c heme lyase. J Biol Chem 264: 17897-17906.
    • (1989) J Biol Chem , vol.264 , pp. 17897-17906
    • Drygas, M.1    Lambowitz, A.M.2    Nargang, F.E.3
  • 14
    • 0023067403 scopus 로고
    • Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae
    • Dumont, M., Ernst, J., Hampsey, D., and Sherman, F. (1987) Identification and sequence of the gene encoding cytochrome c heme lyase in the yeast Saccharomyces cerevisiae. EMBO J 6: 235-241.
    • (1987) EMBO J , vol.6 , pp. 235-241
    • Dumont, M.1    Ernst, J.2    Hampsey, D.3    Sherman, F.4
  • 15
    • 0031048260 scopus 로고    scopus 로고
    • Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes
    • Fabianek, R.A., Huber-Wunderich, M., Glockshuber, R., Kunzler, P., Henneke, H., and Thöny-Meyer, L. (1997) Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes. J Biol Chem 272: 4467-4473.
    • (1997) J Biol Chem , vol.272 , pp. 4467-4473
    • Fabianek, R.A.1    Huber-Wunderich, M.2    Glockshuber, R.3    Kunzler, P.4    Henneke, H.5    Thöny-Meyer, L.6
  • 17
    • 0031574912 scopus 로고    scopus 로고
    • Molecular and immunological analysis of an ABC transporter complex required for cytochrome c biogenesis
    • Goldman, B.S., Beckman, D.L., Bali, A., Monika, E.M., Gabbert, K.K., and Kranz, R.G. (1997) Molecular and immunological analysis of an ABC transporter complex required for cytochrome c biogenesis. J Mol Biol 268: 724-738.
    • (1997) J Mol Biol , vol.268 , pp. 724-738
    • Goldman, B.S.1    Beckman, D.L.2    Bali, A.3    Monika, E.M.4    Gabbert, K.K.5    Kranz, R.G.6
  • 18
    • 0028268026 scopus 로고
    • Rhodobacter capsulatus contains a novel cb-type cytochrome c oxidase without a CuA center
    • Gray, K.A., Grooms, M., Myllykallio, H., Moomaw, C., Slaughter, C., and Daldal, F. (1994) Rhodobacter capsulatus contains a novel cb-type cytochrome c oxidase without a CuA center. Biochemistry 33: 3120-3127.
    • (1994) Biochemistry , vol.33 , pp. 3120-3127
    • Gray, K.A.1    Grooms, M.2    Myllykallio, H.3    Moomaw, C.4    Slaughter, C.5    Daldal, F.6
  • 19
    • 0030033752 scopus 로고    scopus 로고
    • Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
    • Grove, J., Tanapongpipat, S., Thomas, G., Griffiths, L., Croole, H., and Cole, J. (1996) Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm. Mol Microbiol 19: 467-481.
    • (1996) Mol Microbiol , vol.19 , pp. 467-481
    • Grove, J.1    Tanapongpipat, S.2    Thomas, G.3    Griffiths, L.4    Croole, H.5    Cole, J.6
  • 20
    • 0026716643 scopus 로고
    • Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992) Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule. J Mol Biol 225: 487-494.
    • (1992) J Mol Biol , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 21
    • 0030926229 scopus 로고    scopus 로고
    • Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity
    • Helde, R., Hengelage, T., Hoffschulte, H., Muller, M., Neubuser, A., Schimz, K., et al. (1997) Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity. J Bacteriol 179: 4003-4012.
    • (1997) J Bacteriol , vol.179 , pp. 4003-4012
    • Helde, R.1    Hengelage, T.2    Hoffschulte, H.3    Muller, M.4    Neubuser, A.5    Schimz, K.6
  • 22
    • 0000207681 scopus 로고
    • TMBASE - A database of membrane spanning protein segments
    • Hofmann, K., and Stoffel, W. (1993) TMBASE - a database of membrane spanning protein segments. Biol Chem Hoppe Seyler 347: 166.
    • (1993) Biol Chem Hoppe Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 23
    • 0027947186 scopus 로고
    • The biosynthesis of bacterial and plastidic c-type cytochromes
    • Howe, G., and Merchant, S. (1994) The biosynthesis of bacterial and plastidic c-type cytochromes. Photosynth Res 40: 147-165.
    • (1994) Photosynth Res , vol.40 , pp. 147-165
    • Howe, G.1    Merchant, S.2
  • 24
    • 0027503597 scopus 로고
    • y, can mediate the photosynthetic growth of Rhodobacter capsulatus and Rhodobacter sphaeroides
    • y, can mediate the photosynthetic growth of Rhodobacter capsulatus and Rhodobacter sphaeroides. EMBO J 12: 2496-2502.
    • (1993) EMBO J , vol.12 , pp. 2496-2502
    • Jenney, F.E.1    Daldal, F.2
  • 25
    • 0028231734 scopus 로고
    • y of Rhodobacter capsulatus in photosynthetic electron transfer
    • y of Rhodobacter capsulatus in photosynthetic electron transfer. Biochemistry 33: 2496-2502.
    • (1994) Biochemistry , vol.33 , pp. 2496-2502
    • Jenney, F.E.J.1    Prince, R.C.2    Daldal, F.3
  • 27
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A. et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 28
    • 0030988928 scopus 로고    scopus 로고
    • Identification, sequence analysis, and expression of the lepB gene for a leader peptidase in Rhodobacter capsulatus
    • Klug, G., Jager, A., Heck, C., and Rauhut, R. (1997) Identification, sequence analysis, and expression of the lepB gene for a leader peptidase in Rhodobacter capsulatus. Mol Gen Genet 253: 666-673.
    • (1997) Mol Gen Genet , vol.253 , pp. 666-673
    • Klug, G.1    Jager, A.2    Heck, C.3    Rauhut, R.4
  • 30
    • 85008530456 scopus 로고
    • Cloning and characterization of a pair of genes that stimulate the production and secretion of Zymomonas mobilis extracellular levansucrase and invertase
    • Kondo, Y., Toyoda, A., Fukushi, H., Yananase, H., Tonomura, K., Kawasaki, H., and Sakai, T. (1994) Cloning and characterization of a pair of genes that stimulate the production and secretion of Zymomonas mobilis extracellular levansucrase and invertase. Biosci Biotechnol Biochem 58: 526-530.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 526-530
    • Kondo, Y.1    Toyoda, A.2    Fukushi, H.3    Yananase, H.4    Tonomura, K.5    Kawasaki, H.6    Sakai, T.7
  • 31
    • 0024534632 scopus 로고
    • Isolation of mutants and genes involved in cytochromes c biosynthesis in Rhodobacter capsulatus
    • Kranz, R.G. (1989) Isolation of mutants and genes involved in cytochromes c biosynthesis in Rhodobacter capsulatus. J Bacteriol 171: 456-464.
    • (1989) J Bacteriol , vol.171 , pp. 456-464
    • Kranz, R.G.1
  • 32
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz, R., Lill, R., Goldman, B., Bonnard, G., and Merchant, S. (1998) Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol Microbiol 29: 383-396.
    • (1998) Mol Microbiol , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 33
    • 0030905547 scopus 로고    scopus 로고
    • Membrane localization, topology and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH-oxidoreductases
    • Kumagai, H., Fujiwara, T., Matsubara, H., and Saeki, K. (1997) Membrane localization, topology and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH-oxidoreductases. Biochemistry 36: 5509-5521.
    • (1997) Biochemistry , vol.36 , pp. 5509-5521
    • Kumagai, H.1    Fujiwara, T.2    Matsubara, H.3    Saeki, K.4
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0029835189 scopus 로고    scopus 로고
    • Rhodobacter capsulatus CycH: A bipartite gene product with pleiotropic effects on the biogenesis of structurally different c-type cytochromes
    • Lang, S.E., Jenney, F.E., and Daldal, F. (1996) Rhodobacter capsulatus CycH: a bipartite gene product with pleiotropic effects on the biogenesis of structurally different c-type cytochromes. J Bacteriol 178: 5279-5290.
    • (1996) J Bacteriol , vol.178 , pp. 5279-5290
    • Lang, S.E.1    Jenney, F.E.2    Daldal, F.3
  • 36
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • Lowry, O., Rosebrough, N., Farr, A., and Randall, R. (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193: 265-275.
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.1    Rosebrough, N.2    Farr, A.3    Randall, R.4
  • 37
    • 0028850245 scopus 로고
    • An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12
    • Metheringham, R., Griffiths, L., Crooke, H., Forsythe, S., and Cole, J. (1995) An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12. Arch Microbiol 164: 301-307.
    • (1995) Arch Microbiol , vol.164 , pp. 301-307
    • Metheringham, R.1    Griffiths, L.2    Crooke, H.3    Forsythe, S.4    Cole, J.5
  • 38
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. (1995) Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J 14: 3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 39
    • 0026558482 scopus 로고
    • Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome
    • Oda, K., Yamato, K., Ohta, E., Nakamura, Y., Takemura, M., Nozato, N. et al. (1992) Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome. J Mol Biol 223: 1-7.
    • (1992) J Mol Biol , vol.223 , pp. 1-7
    • Oda, K.1    Yamato, K.2    Ohta, E.3    Nakamura, Y.4    Takemura, M.5    Nozato, N.6
  • 40
    • 0030749493 scopus 로고    scopus 로고
    • 3-type cytochrome biogenesis; evidence for a reductase role in vivo
    • 3-type cytochrome biogenesis; evidence for a reductase role in vivo. Mol Microbiol 24: 977-990.
    • (1997) Mol Microbiol , vol.24 , pp. 977-990
    • Page, M.D.1
  • 42
    • 0031050448 scopus 로고    scopus 로고
    • The Paracoccus denitrificans ccmA, B and C genes: Cloning and sequencing, and analysis of the potential of their products to form haem or apo-c-type cytochrome transporter
    • Page, M.D., Pearce, D.A., Norris, H.A.C., and Ferguson, S.J. (1997a) The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing, and analysis of the potential of their products to form haem or apo-c-type cytochrome transporter. Microbiology 143: 563-576.
    • (1997) Microbiology , vol.143 , pp. 563-576
    • Page, M.D.1    Pearce, D.A.2    Norris, H.A.C.3    Ferguson, S.J.4
  • 43
    • 0030780084 scopus 로고    scopus 로고
    • Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis
    • Page, M.D., Saunders, N.F.W., and Ferguson, S.J. (1997b) Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis. Microbiology 143: 3111-3122.
    • (1997) Microbiology , vol.143 , pp. 3111-3122
    • Page, M.D.1    Saunders, N.F.W.2    Ferguson, S.J.3
  • 44
    • 0031937605 scopus 로고    scopus 로고
    • Identification of the contiguous Paracoccus denitrificans ccmF and ccmH genes: Disruption of ccmF, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production
    • Pearce, D.A., Page, M.D., Norris, H.A.C., Tomlinson, E.J., and Ferguson, S.J. (1998) Identification of the contiguous Paracoccus denitrificans ccmF and ccmH genes: disruption of ccmF, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production. Microbiology 144: 467-477.
    • (1998) Microbiology , vol.144 , pp. 467-477
    • Pearce, D.A.1    Page, M.D.2    Norris, H.A.C.3    Tomlinson, E.J.4    Ferguson, S.J.5
  • 46
    • 0021592032 scopus 로고
    • In vitro insertional mutagnesis with a selectable DNA fragment
    • Prentki, P., and Krisch, H.M. (1984) In vitro insertional mutagnesis with a selectable DNA fragment. Gene 29: 293-303.
    • (1984) Gene , vol.29 , pp. 293-303
    • Prentki, P.1    Krisch, H.M.2
  • 47
    • 0025823215 scopus 로고
    • Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes
    • Ramseier, T.M., Winteler, H.V., and Hennecke, H. (1991) Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J Biol Chem 266: 7793-7803.
    • (1991) J Biol Chem , vol.266 , pp. 7793-7803
    • Ramseier, T.M.1    Winteler, H.V.2    Hennecke, H.3
  • 48
    • 0032529951 scopus 로고    scopus 로고
    • The CcmE protein from Escherichia coli is a haem-binding protein
    • Reid, E., Eaves, D.J., and Cole, J.A. (1998) The CcmE protein from Escherichia coli is a haem-binding protein. FEMS Microbiol Lett 166: 369-375.
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 369-375
    • Reid, E.1    Eaves, D.J.2    Cole, J.A.3
  • 49
    • 51649139576 scopus 로고
    • Complete nucleotide sequence of the Porphyra purpurea chloroplast genome
    • Reith, M., and Munholland, J. (1995) Complete nucleotide sequence of the Porphyra purpurea chloroplast genome. Plant Mol Biol Rep 13: 333-335.
    • (1995) Plant Mol Biol Rep , vol.13 , pp. 333-335
    • Reith, M.1    Munholland, J.2
  • 50
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., Bessette, P., Georgiou, G., and Beckwith, J. (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179: 6602-6608.
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 51
    • 0027181123 scopus 로고
    • Formation of several bacterial c-type cytochromes requires a novel membrane-anchored protein that faces the periplasm
    • Ritz, D., Bott, M., and Hennecke, H. (1993) Formation of several bacterial c-type cytochromes requires a novel membrane-anchored protein that faces the periplasm. Mol Microbiol 9: 729-740.
    • (1993) Mol Microbiol , vol.9 , pp. 729-740
    • Ritz, D.1    Bott, M.2    Hennecke, H.3
  • 52
    • 0028964914 scopus 로고
    • The cycHJKL gene cluster plays an essential role in the biogenesis of c-type cytochromes in Bradyrhizobium japonicum
    • Ritz, D., Thöny-Meyer, L., and Hennecke, H. (1995) The cycHJKL gene cluster plays an essential role in the biogenesis of c-type cytochromes in Bradyrhizobium japonicum. Mol Gen Genet 247: 27-38.
    • (1995) Mol Gen Genet , vol.247 , pp. 27-38
    • Ritz, D.1    Thöny-Meyer, L.2    Hennecke, H.3
  • 53
    • 0029890249 scopus 로고    scopus 로고
    • Genetic and physical mapping in Brassica diploid species of a gene cluster defined in Arabidopsis thaliana
    • Sadowski, J., Gaubier, P., Delseny, M., and Quiros, C.F. (1996) Genetic and physical mapping in Brassica diploid species of a gene cluster defined in Arabidopsis thaliana. Mol Gen Genet 251: 298-306.
    • (1996) Mol Gen Genet , vol.251 , pp. 298-306
    • Sadowski, J.1    Gaubier, P.2    Delseny, M.3    Quiros, C.F.4
  • 54
    • 0028116313 scopus 로고
    • Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein
    • Sambongi, Y., and Ferguson, S. (1994) Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein. FEBS Lett 353: 235-238.
    • (1994) FEBS Lett , vol.353 , pp. 235-238
    • Sambongi, Y.1    Ferguson, S.2
  • 55
    • 0030566826 scopus 로고    scopus 로고
    • Mutants of Escherichia coli lacking disulphide oxidoreductase DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
    • Sambongi, Y., and Ferguson, S. (1996) Mutants of Escherichia coli lacking disulphide oxidoreductase DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds. FEBS Lett 398: 265-268.
    • (1996) FEBS Lett , vol.398 , pp. 265-268
    • Sambongi, Y.1    Ferguson, S.2
  • 57
    • 0028857635 scopus 로고
    • Membrane topology analysis of Escherichia coli K-12 Mtr permease by alkaline phosphatase and β-galactosidase fusions
    • Sarsero, J.P., and Pittard, A.J. (1995) Membrane topology analysis of Escherichia coli K-12 Mtr permease by alkaline phosphatase and β-galactosidase fusions. J Bacteriol 177: 297-306.
    • (1995) J Bacteriol , vol.177 , pp. 297-306
    • Sarsero, J.P.1    Pittard, A.J.2
  • 58
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range 1-100 kDa
    • Schägger, H., and Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range 1-100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 59
    • 0038228616 scopus 로고    scopus 로고
    • Bacillus subtilis CcdA-defective mutants are blocked in a late step of cytochrome c biogenesis
    • Schiött, T., Throne-Holst, M., and Hederstedt, L. (1997a) 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    Throne-Holst, M.2    Hederstedt, L.3
  • 60
    • 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., and Hederstedt, L. (1997b) 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
  • 61
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz, H., Hennecke, H., and Thöny-Meyer, L. (1998) Prototype of a heme chaperone essential for cytochrome c maturation. Science 281: 1197-1200.
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thöny-Meyer, L.3
  • 62
    • 0033033305 scopus 로고    scopus 로고
    • Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB
    • Schulz, H., Fabianek, R.A., Pelliciolli, E.C., Hennecke, H., and Thöny-Meyer, L. (1999) Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB. Proc Natl Acad Sci USA 96: 6462-6467.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6462-6467
    • Schulz, H.1    Fabianek, R.A.2    Pelliciolli, E.C.3    Hennecke, H.4    Thöny-Meyer, L.5
  • 63
    • 0018963751 scopus 로고
    • Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata
    • Scolnik, P.A., Walker, M.A., and Marrs, B.L. (1980) Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata. J Biol Chem 255: 2427-2432.
    • (1980) J Biol Chem , vol.255 , pp. 2427-2432
    • Scolnik, P.A.1    Walker, M.A.2    Marrs, B.L.3
  • 64
    • 72849182812 scopus 로고
    • A requirement for sodium in the growth of Rhodopseudomonas sphaeroides
    • Sistrom, W.R. (1960) A requirement for sodium in the growth of Rhodopseudomonas sphaeroides. J Gen Microbiol 22: 778-785.
    • (1960) J Gen Microbiol , vol.22 , pp. 778-785
    • Sistrom, W.R.1
  • 65
    • 0032570834 scopus 로고    scopus 로고
    • Rhizobium etli cycHJKL gene locus involved in c-type cytochrome biogenesis: Sequence analysis and characterization of two cycH mutants
    • Tabche, M.L., Garcia, E.G., Miranda, J., Escamilla, J.E., and Soberón, M. (1998) Rhizobium etli cycHJKL gene locus involved in c-type cytochrome biogenesis: sequence analysis and characterization of two cycH mutants. Gene 208: 215-219.
    • (1998) Gene , vol.208 , pp. 215-219
    • Tabche, M.L.1    Garcia, E.G.2    Miranda, J.3    Escamilla, J.E.4    Soberón, M.5
  • 66
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P.E., Ryan, D., and Levin, W. (1976) An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal Biochem 75: 168-176.
    • (1976) Anal Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 67
    • 0027968068 scopus 로고
    • CLUSTAL w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specific gap penalties and weight matrix choice
    • Thompson, J., Higgins, D., and Gibson, T. (1994) CLUSTAL w: improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 68
    • 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
  • 69
    • 0030953231 scopus 로고    scopus 로고
    • Translocation to the periplasm and signal sequence cleavage of preapocytochrome c depend on sec and lep, but not on the ccm gene products
    • Thöny-Meyer, L., and Kunzler, P. (1997) Translocation to the periplasm and signal sequence cleavage of preapocytochrome c depend on sec and lep, but not on the ccm gene products. Eur J Biochem 246: 794-799.
    • (1997) Eur J Biochem , vol.246 , pp. 794-799
    • Thöny-Meyer, L.1    Kunzler, P.2
  • 71
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • Unseld, M., Marienfeld, J.R., Brandt, P., and Brennicke, A. (1997) The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides. Nature Genet 15: 57-61.
    • (1997) Nature Genet , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brandt, P.3    Brennicke, A.4
  • 72
    • 0026584950 scopus 로고
    • Identification and solubilization of a signal peptidase from the phototrophic bacterium Rhodobacter capsulatus
    • Wieseler, B., Schiltz, E., and Muller, M. (1992) Identification and solubilization of a signal peptidase from the phototrophic bacterium Rhodobacter capsulatus. FEBS Lett 298: 273-276.
    • (1992) FEBS Lett , vol.298 , pp. 273-276
    • Wieseler, B.1    Schiltz, E.2    Muller, M.3
  • 73
    • 0032311168 scopus 로고    scopus 로고
    • A novel pathway for cytochromes c biogenesis in chloroplasts
    • Xie, Z., and Merchant, S. (1998) A novel pathway for cytochromes c biogenesis in chloroplasts. Biochim Biophys Acta 1365: 309-318.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 309-318
    • Xie, Z.1    Merchant, S.2
  • 74
    • 0018391101 scopus 로고
    • Characterization of the gene transfer agent made by an overproducer mutant of Rhodopseudomonas capsulata
    • Yen, H.C., Hu, N.T., and Marrs, B.L. (1979) Characterization of the gene transfer agent made by an overproducer mutant of Rhodopseudomonas capsulata. J Mol Biol 131: 157-168.
    • (1979) J Mol Biol , vol.131 , pp. 157-168
    • Yen, H.C.1    Hu, N.T.2    Marrs, B.L.3
  • 75
    • 0027448646 scopus 로고
    • The role of c-type cytochromes in catalyzing oxidative and photosynthetic electron transport in the dual functional plasma membrane of facultative phototrophs
    • Zannoni, D., and Daldal, F. (1993) The role of c-type cytochromes in catalyzing oxidative and photosynthetic electron transport in the dual functional plasma membrane of facultative phototrophs. Arch Microbiol 160: 413-423.
    • (1993) Arch Microbiol , vol.160 , pp. 413-423
    • Zannoni, D.1    Daldal, F.2


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