메뉴 건너뛰기




Volumn 185, Issue 2, 2003, Pages 422-431

Features of Rhodobacter sphaeroides CcmFH

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; BETA GALACTOSIDASE; CYSTEINE; CYSTINE; CYTOCHROME C; MEMBRANE PROTEIN; PROTEIN CCMFH; PROTEIN PRECURSOR; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0037226495     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.2.422-431.2003     Document Type: Article
Times cited : (12)

References (58)
  • 1
    • 0032512416 scopus 로고    scopus 로고
    • Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation
    • Barber, R. D., and T. J. Donohue. 1998. Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation. Biochemistry 37:530-537.
    • (1998) Biochemistry , vol.37 , pp. 530-537
    • Barber, R.D.1    Donohue, T.J.2
  • 3
    • 0028031912 scopus 로고
    • 2 signal peptide is not necessary for export and heme attachment
    • 2 signal peptide is not necessary for export and heme attachment. J. Bacteriol. 176:602-609.
    • (1994) J. Bacteriol. , vol.176 , pp. 602-609
    • Brandner, J.P.1    Donohue, T.J.2
  • 5
    • 0034933212 scopus 로고    scopus 로고
    • Roles for the Rhodobacter sphaeroides CcmA and CcmG proteins
    • Cox, R. L., C. Patterson, and T. J. Donohue. 2001. Roles for the Rhodobacter sphaeroides CcmA and CcmG proteins. J. Bacteriol. 183:4643-4647.
    • (2001) J. Bacteriol. , vol.183 , pp. 4643-4647
    • Cox, R.L.1    Patterson, C.2    Donohue, T.J.3
  • 6
    • 0037162447 scopus 로고    scopus 로고
    • The CcmE protein of the c-type cytochrome biogenesis system: Unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome
    • Daltrop, O., J. M. Stevens, C. W. Higham, and S. J. Ferguson. 2002. The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome. Proc. Natl. Acad. Sci. USA 99:9703-9708.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9703-9708
    • Daltrop, O.1    Stevens, J.M.2    Higham, C.W.3    Ferguson, S.J.4
  • 7
    • 0029088169 scopus 로고
    • Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum
    • Delgado, M. J., K. H. Yeoman, G. Wu, C. Vargas, A. E. Davies, R. K. Poole, A. W. B. Johnston, and A. Downie. 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    Wu, G.3    Vargas, C.4    Davies, A.E.5    Poole, R.K.6    Johnston, A.W.B.7    Downie, A.8
  • 8
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, 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
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 9
    • 0025787993 scopus 로고
    • Genetic techniques in Rhodospirillaceae
    • Donohue, T. J., and S. Kaplan. 1991. Genetic techniques in Rhodospirillaceae. Methods Enzymol. 204:459-485.
    • (1991) Methods Enzymol. , vol.204 , pp. 459-485
    • Donohue, T.J.1    Kaplan, S.2
  • 11
    • 0025604834 scopus 로고
    • Localization and structural analysis of the ribosomal RNA operons of Rhodobacter sphaeroides
    • Dryden, S. C., and S. Kaplan. 1990. Localization and structural analysis of the ribosomal RNA operons of Rhodobacter sphaeroides. Nucleic Acids Res. 18:7267-7277.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7267-7277
    • Dryden, S.C.1    Kaplan, S.2
  • 12
    • 0029016713 scopus 로고
    • Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: A mutant histidine kinase
    • Eraso, J. M., and S. Kaplan. 1995. Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase. J. Bacteriol. 177:2695-2706.
    • (1995) J. Bacteriol. , vol.177 , pp. 2695-2706
    • Eraso, J.M.1    Kaplan, S.2
  • 13
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol: Disulfide oxidoreductase of Escherichia coli
    • Fabianek, R. A., H. Hennecke, and L. Thony-Meyer. 2000. Periplasmic protein thiol: disulfide oxidoreductase of Escherichia coli. FEMS Microbiol. Rev. 24:303-316.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 14
    • 0033032598 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation
    • Fabianek, R. A., T. Hofer, and L. Thony-Meyer. 1999. Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation. Arch. Microbiol. 171:92-100.
    • (1999) Arch. Microbiol. , vol.171 , pp. 92-100
    • Fabianek, R.A.1    Hofer, T.2    Thony-Meyer, L.3
  • 16
    • 0029149361 scopus 로고
    • Organization and expression of the Rhodobacter sphaeroides cycFG operon
    • Flory, J. E., and T. J. Donohue. 1995. Organization and expression of the Rhodobacter sphaeroides cycFG operon. J. Bacteriol. 177:4311-4320.
    • (1995) J. Bacteriol. , vol.177 , pp. 4311-4320
    • Flory, J.E.1    Donohue, T.J.2
  • 17
    • 0021328935 scopus 로고
    • Specific indication of hemoproteins in polyacrylamide gels using a double-staining process
    • Francis, R. T. J., and R. R. Becker. 1984. Specific indication of hemoproteins in polyacrylamide gels using a double-staining process. Anal. Biochem. 136: 509-514.
    • (1984) Anal. Biochem. , vol.136 , pp. 509-514
    • Francis, R.T.J.1    Becker, R.R.2
  • 18
    • 0029769308 scopus 로고    scopus 로고
    • A cytochrome c biogenesis gene involved in pyoverdine production in Pseudomonas fluorescens ATCC 17400
    • Gaballa, A., N. Koedam, and P. Cornelis. 1996. A cytochrome c biogenesis gene involved in pyoverdine production in Pseudomonas fluorescens ATCC 17400. Mol. Microbiol. 21:777-785.
    • (1996) Mol. Microbiol. , vol.21 , pp. 777-785
    • Gaballa, A.1    Koedam, N.2    Cornelis, P.3
  • 22
    • 0019880604 scopus 로고
    • The cytochromes in microsomes of germinating mung beans
    • Hendry, G. A. F., J. D. Houghton, and O. T. G. Jones. 1991. The cytochromes in microsomes of germinating mung beans. J. Biochem. 194:743-751.
    • (1991) J. Biochem. , vol.194 , pp. 743-751
    • Hendry, G.A.F.1    Houghton, J.D.2    Jones, O.T.G.3
  • 23
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 24
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanism of cytochrome c biogenesis: Three distinct systems
    • Kranz, R., R. Lill, B. Goldman, G. Bonnard, and S. Merchant. 1998. Molecular mechanism 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
  • 25
    • 0002054757 scopus 로고
    • Cytochrome biogenesis
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordecht, The Netherlands
    • Kranz, R. G., and D. L. Beckman. 1995. Cytochrome biogenesis, p. 709-723. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 709-723
    • Kranz, R.G.1    Beckman, D.L.2
  • 26
    • 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., F. E. Jenney, Jr., and F. Daldal. 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., Jr.2    Daldal, F.3
  • 31
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions: Sensors of subcellular location
    • Manoil, C., J. J. Mekalanos, and J. Beckwith. 1990. Alkaline phosphatase fusions: sensors of subcellular location. J. Bacteriol. 172:515-518.
    • (1990) J. Bacteriol. , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 32
    • 0026047004 scopus 로고
    • Analysis of membrane protein topology using alkaline phosphatase and β-galactosidase gene fusions
    • Manoil, C. 1991. Analysis of membrane protein topology using alkaline phosphatase and β-galactosidase gene fusions. Methods Cell. Biol. 34:61-75.
    • (1991) Methods Cell. Biol. , vol.34 , pp. 61-75
    • Manoil, C.1
  • 33
    • 0031554890 scopus 로고    scopus 로고
    • A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis: In vitro and in vivo studies
    • Monika, E. M., B. S. Goldman, D. L. Beckman, and R. G. Kranz. 1997. A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis: in vitro and in vivo studies. J. Mol. Biol. 271:679-692.
    • (1997) J. Mol. Biol. , vol.271 , pp. 679-692
    • Monika, E.M.1    Goldman, B.S.2    Beckman, D.L.3    Kranz, R.G.4
  • 34
    • 0024720192 scopus 로고
    • Construction of TnphoA gene fusions in Rhodobacter sphaeroides: Isolation and characterization of a respiratory mutant unable to utilize dimethyl sulfoxide as a terminal electron acceptor during anaerobic growth in the dark on glucose
    • Moore, M. D., and S. Kaplan. 1989. Construction of TnphoA gene fusions in Rhodobacter sphaeroides: isolation and characterization of a respiratory mutant unable to utilize dimethyl sulfoxide as a terminal electron acceptor during anaerobic growth in the dark on glucose. J. Bacteriol. 171:4385-4394.
    • (1989) J. Bacteriol. , vol.171 , pp. 4385-4394
    • Moore, M.D.1    Kaplan, S.2
  • 35
    • 0030835030 scopus 로고    scopus 로고
    • T: An essential metabolic gene function encoded on chromosome II
    • T: an essential metabolic gene function encoded on chromosome II. J. Bacteriol. 179:7617-7624.
    • (1997) J. Bacteriol. , vol.179 , pp. 7617-7624
    • Mouncey, N.J.1    Choudhary, M.2    Kaplan, S.3
  • 36
    • 0034664042 scopus 로고    scopus 로고
    • Redox signaling: Globalization of gene expression
    • Oh, J.-I., and S. Kaplan. 2000. Redox signaling: globalization of gene expression. EMBO J. 19:4237-4247.
    • (2000) EMBO J. , vol.19 , pp. 4237-4247
    • Oh, J.-I.1    Kaplan, S.2
  • 37
    • 0033514508 scopus 로고    scopus 로고
    • 3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: Structural and functional implications for the regulation of spectral complex formation
    • 3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation. Biochemistry 38:2688-2696.
    • (1999) Biochemistry , vol.38 , pp. 2688-2696
    • Oh, J.I.1    Kaplan, S.2
  • 39
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 40
    • 0037040888 scopus 로고    scopus 로고
    • A bacterial cytochrome c heme lyase: CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c
    • Ren, Q., U. Ahuja, and L. Thony-Meyer. 2002. A bacterial cytochrome c heme lyase: CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c. J. Biol. Chem. 277:7657-7663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7657-7663
    • Ren, Q.1    Ahuja, U.2    Thony-Meyer, L.3
  • 41
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • Rietsch, A., and J. Beckwith. 1998. The genetics of disulfide bond metabolism. Annu. Rev. Genet. 32:163-184.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 43
    • 0027181123 scopus 로고
    • Formation of several bacterial c-type cytochromes requires a novel membrane-anchored protein that faces the periplasm
    • Ritz, D., M. Bott, and H. Hennecke. 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
  • 44
    • 0028964914 scopus 로고
    • The cycHJKL gene cluster plays an essential role in the biogenesis of c-type cytochromes in Bradyrhizobium japonicum
    • Ritz, D., L. Thony-Meyer, and H. Hennecke. 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    Thony-Meyer, L.2    Hennecke, H.3
  • 45
  • 46
    • 0030566826 scopus 로고    scopus 로고
    • Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesize monoheam c-type cytochromes except in the presence of disulphide compounds
    • Sambogni, Y., and S. J. Ferguson. 1996. Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesize monoheam c-type cytochromes except in the presence of disulphide compounds. FEBS Lett. 398:265-268.
    • (1996) FEBS Lett. , vol.398 , pp. 265-268
    • Sambogni, Y.1    Ferguson, S.J.2
  • 47
    • 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
    • Sambogni, Y., and S. J. Ferguson. 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. 353:235-258.
    • (1994) FEBS Lett. , vol.353 , pp. 235-258
    • Sambogni, Y.1    Ferguson, S.J.2
  • 48
    • 0026611626 scopus 로고
    • δ-aminolevulinate couples cycA transcription to changes in heme availability in Rhodobacter sphaeroides
    • Schilke, B. A., and T. J. Donohue. 1992. δ-Aminolevulinate couples cycA transcription to changes in heme availability in Rhodobacter sphaeroides. J. Mol. Biol. 226:101-115.
    • (1992) J. Mol. Biol. , vol.226 , pp. 101-115
    • Schilke, B.A.1    Donohue, T.J.2
  • 49
    • 0034702814 scopus 로고    scopus 로고
    • Oxidation-reduction properties of disulfide containing properties of the Rhodobacter capsulatus cytochrome c biogenesis system
    • Setterdahl, A. T., B. S. Goldman, M. Hirasawa, P. Jacquot, A. J. Smith, R. G. Kranz, and D. B. Knaff. 2000. Oxidation-reduction properties of disulfide containing properties of the Rhodobacter capsulatus cytochrome c biogenesis system. Biochemistry 39:10172-10176.
    • (2000) Biochemistry , vol.39 , pp. 10172-10176
    • Setterdahl, A.T.1    Goldman, B.S.2    Hirasawa, M.3    Jacquot, P.4    Smith, A.J.5    Kranz, R.G.6    Knaff, D.B.7
  • 50
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vitro genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vitro genetic engineering: transposon mutagenesis in gram negative bacteria. Bio/Technology 1:748-791.
    • (1983) Bio/Technology , vol.1 , pp. 748-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 51
    • 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. Gen. Microbiol. 22:778-785.
    • (1960) Gen. Microbiol. , vol.22 , pp. 778-785
    • Sistrom, W.R.1
  • 52
    • 0024443488 scopus 로고
    • Physical and genetic mapping of the Rhodobacter sphaeroides 2.4.1 genome: Presence of two unique circular chromosomes
    • Suwanto, A., and S. Kaplan. 1989. Physical and genetic mapping of the Rhodobacter sphaeroides 2.4.1 genome: presence of two unique circular chromosomes. J. Bacteriol. 171:5850-5859.
    • (1989) J. Bacteriol. , vol.171 , pp. 5850-5859
    • Suwanto, A.1    Kaplan, S.2
  • 53
    • 0022350092 scopus 로고
    • Intracellular localization of phospholipid transfer activity in Rhodopseudomonas sphaeroides and a possible role in membrane biogenesis
    • Tai, S. P., and S. Kaplan. 1985. Intracellular localization of phospholipid transfer activity in Rhodopseudomonas sphaeroides and a possible role in membrane biogenesis. J. Bacteriol. 164:181-186.
    • (1985) J. Bacteriol. , vol.164 , pp. 181-186
    • Tai, S.P.1    Kaplan, S.2
  • 54
    • 0024010832 scopus 로고
    • A broad-host-range vector system for cloning and translational lacZ fusion analysis
    • Tai, T. N., W. A. Havelka, and S. Kaplan. 1988. A broad-host-range vector system for cloning and translational lacZ fusion analysis. Plasmid 19:175-188.
    • (1988) Plasmid , vol.19 , pp. 175-188
    • Tai, T.N.1    Havelka, W.A.2    Kaplan, S.3
  • 55
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thony-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
    • Thony-Meyer, L.1
  • 56
    • 0024462262 scopus 로고
    • Construction, expression, and localization of a CycA::PhoA fusion protein in Rhodobacter sphaeroides and Escherichia coli
    • Varga, A. R., and S. Kaplan. 1989. Construction, expression, and localization of a CycA::PhoA fusion protein in Rhodobacter sphaeroides and Escherichia coli. J. Bacteriol. 171:5830-5839.
    • (1989) J. Bacteriol. , vol.171 , pp. 5830-5839
    • Varga, A.R.1    Kaplan, S.2
  • 57
    • 0032311168 scopus 로고    scopus 로고
    • A novel pathway for cytochromes c biogenesis in chloroplasts
    • Xie, Z., and S. Merchant. 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
  • 58
    • 0029987670 scopus 로고    scopus 로고
    • A chromosomal locus required for copper resistance, competitive fitness, and cytochrome c biogenesis in Pseudomonas fluorescens
    • Yang, C. H., H. R. Azad, and D. A. Cooksey. 1996. A chromosomal locus required for copper resistance, competitive fitness, and cytochrome c biogenesis in Pseudomonas fluorescens. Proc. Natl. Acad. Sci. USA 93:7315-7320.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7315-7320
    • Yang, C.H.1    Azad, H.R.2    Cooksey, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.