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Volumn 68, Issue 12, 2000, Pages 7166-7171

fbpABC gene cluster in Neisseria meningitidis is transcribed as an operon

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BACTERIAL DNA; COMPLEMENTARY DNA; MESSENGER RNA; OLIGONUCLEOTIDE;

EID: 0034441291     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.12.7166-7171.2000     Document Type: Article
Times cited : (18)

References (29)
  • 1
    • 0029936842 scopus 로고    scopus 로고
    • The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron
    • Adhikari, P., S. A. Berish, A. J. Nowalk, K. L. Veraldi, S. A. Morse, and T. A. Mietzner. 1996. The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron. J. Bacteriol. 178:2145-2149.
    • (1996) J. Bacteriol. , vol.178 , pp. 2145-2149
    • Adhikari, P.1    Berish, S.A.2    Nowalk, A.J.3    Veraldi, K.L.4    Morse, S.A.5    Mietzner, T.A.6
  • 2
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: Structure, mechanism, and evolution
    • Ames, G. F.-L. 1986. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 55:397-425.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 397-425
    • Ames, G.F.-L.1
  • 3
    • 0026739111 scopus 로고
    • Expression of a functional neisserial fbp gene in Escherichia coli
    • Berish, S. A., C.-Y. Chen, T. A. Mietzner, and S. A. Morse. 1992. Expression of a functional neisserial fbp gene in Escherichia coli. Mol. Microhiol. 6:2607-2615.
    • (1992) Mol. Microhiol. , vol.6 , pp. 2607-2615
    • Berish, S.A.1    Chen, C.-Y.2    Mietzner, T.A.3    Morse, S.A.4
  • 4
    • 0025073960 scopus 로고
    • Nucleotide sequence of the Fbp gene from Neisseria meningitidis
    • Berish, S. A., D. Kapczunski, and S. A. Morse. 1990. Nucleotide sequence of the Fbp gene from Neisseria meningitidis. Nucleic Acids Res. 18:4596.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4596
    • Berish, S.A.1    Kapczunski, D.2    Morse, S.A.3
  • 5
    • 0027491241 scopus 로고
    • The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin
    • Chen, C.-Y., S. A. Berish, S. A. Morse, and T. A. Mietzner. 1993. The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol. Microbiol. 10:311-318.
    • (1993) Mol. Microbiol. , vol.10 , pp. 311-318
    • Chen, C.-Y.1    Berish, S.A.2    Morse, S.A.3    Mietzner, T.A.4
  • 6
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance
    • Doige, C. A., and G. F.-L. Ames. 1993. ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance. Annu. Rev. Microbiol. 47:291-319.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.-L.2
  • 9
    • 0031001581 scopus 로고    scopus 로고
    • Promoter mapping and transcriptional regulation of the iron-regulated Neisseria gonorrhoeae fbpA gene
    • Forng, R.-Y., C. R. Ekechukwu, S. Subbarao, S. A. Morse, and C. A. Genco. 1997. Promoter mapping and transcriptional regulation of the iron-regulated Neisseria gonorrhoeae fbpA gene. J. Bacteriol. 179:3047-3052.
    • (1997) J. Bacteriol. , vol.179 , pp. 3047-3052
    • Forng, R.-Y.1    Ekechukwu, C.R.2    Subbarao, S.3    Morse, S.A.4    Genco, C.A.5
  • 10
    • 0027248704 scopus 로고
    • Cloning and characterization of the Neisseria meningitidis asd gene
    • Hatten, L. A., H. P. Schweizer, N. Averill, L. Wang, and A. B. Schryvers. 1993. Cloning and characterization of the Neisseria meningitidis asd gene. Gene 129:123-128.
    • (1993) Gene , vol.129 , pp. 123-128
    • Hatten, L.A.1    Schweizer, H.P.2    Averill, N.3    Wang, L.4    Schryvers, A.B.5
  • 11
    • 0027360468 scopus 로고
    • Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli
    • Hekstra, D., and J. Tommassen. 1993. Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli. J. Bacteriol. 175:6546-6552.
    • (1993) J. Bacteriol. , vol.175 , pp. 6546-6552
    • Hekstra, D.1    Tommassen, J.2
  • 12
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 13
    • 0023644827 scopus 로고
    • Molecular characterization of the oligopeptide permease of Salmonella typhimurium
    • Hiles, I. D., M. P. Gallagher, D. J. Jamieson, and C. F. Higgins. 1987. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol. Biol. 195:125-142.
    • (1987) J. Mol. Biol. , vol.195 , pp. 125-142
    • Hiles, I.D.1    Gallagher, M.P.2    Jamieson, D.J.3    Higgins, C.F.4
  • 14
    • 0031948656 scopus 로고    scopus 로고
    • A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth
    • Khun, H. H., S. D. Kirby, and B. C. Lee. 1998. A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66:2330-2336.
    • (1998) Infect. Immun. , vol.66 , pp. 2330-2336
    • Khun, H.H.1    Kirby, S.D.2    Lee, B.C.3
  • 15
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton, K. J., and C. F. Higgins. 1998. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28:5-13.
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 16
    • 0031923708 scopus 로고    scopus 로고
    • Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake
    • Mademidis, A., and W. Koster. 1998. Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake. Mol. Gen. Genet. 258:156-165.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 156-165
    • Mademidis, A.1    Koster, W.2
  • 17
    • 0022630125 scopus 로고
    • Distribution of an antigenically related iron-regulated protein among the Neisseria spp.
    • Mietzner, T. A., R. C. Barnes, Y. A. Jeanlouis, W. M. Shafer, and S. A. Morse. 1986. Distribution of an antigenically related iron-regulated protein among the Neisseria spp. Infect. Immun. 51:60-68.
    • (1986) Infect. Immun. , vol.51 , pp. 60-68
    • Mietzner, T.A.1    Barnes, R.C.2    Jeanlouis, Y.A.3    Shafer, W.M.4    Morse, S.A.5
  • 18
    • 0023663908 scopus 로고
    • Differential mRNA stability controls relative gene expression within a polycistronic operon
    • Newbury, S. F., N. H. Smith, and C. F. Higgins. 1987. Differential mRNA stability controls relative gene expression within a polycistronic operon. Cell 51:1131-1143.
    • (1987) Cell , vol.51 , pp. 1131-1143
    • Newbury, S.F.1    Smith, N.H.2    Higgins, C.F.3
  • 19
    • 0023667782 scopus 로고
    • Stabilization of translationally active mRNA by prokaryotic REP sequences
    • Newbury, S. F., N. H. Smith, E. C. Robinson, I. D. Hiles, and C. F. Higgins. 1987. Stabilization of translationally active mRNA by prokaryotic REP sequences. Cell 48:297-310.
    • (1987) Cell , vol.48 , pp. 297-310
    • Newbury, S.F.1    Smith, N.H.2    Robinson, E.C.3    Hiles, I.D.4    Higgins, C.F.5
  • 20
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of a common theme
    • Quiocho, F. A., and P. S. Ledvina. 1996. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of a common theme. Mol. Microbiol. 20:17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 23
    • 0029806390 scopus 로고    scopus 로고
    • In search of Mycoplasma genitalium lost substrate-binding proteins: Sequence divergence could be the result of a broader substrate specificity
    • Saurin, W., and E. Dassa. 1996. In search of Mycoplasma genitalium lost substrate-binding proteins: sequence divergence could be the result of a broader substrate specificity. Mol. Microbiol. 22:389-390.
    • (1996) Mol. Microbiol. , vol.22 , pp. 389-390
    • Saurin, W.1    Dassa, E.2
  • 24
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/ domains
    • Schneider, E., and S. Hunke. 1998. ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/ domains. FEMS Microbiol. Rev. 22:1-20.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 25
    • 0033052477 scopus 로고    scopus 로고
    • FbpC is not essential for iron acquisition in Neisseria gonorrhoeae
    • Sebastian, S., and C. A. Genco. 1999. FbpC is not essential for iron acquisition in Neisseria gonorrhoeae. Infect. Immun. 67:3141-3145.
    • (1999) Infect. Immun. , vol.67 , pp. 3141-3145
    • Sebastian, S.1    Genco, C.A.2
  • 26
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and M. H. Saier, Jr. 1993. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57:320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier M.H., Jr.2
  • 27
    • 0031033423 scopus 로고    scopus 로고
    • Haem iron-transport system in enterohaemorrhagic Escherichia coli O157:H7
    • Torres, A. G., and S. M. Payne. 1997. Haem iron-transport system in enterohaemorrhagic Escherichia coli O157:H7. Mol. Microbiol. 23:825-833.
    • (1997) Mol. Microbiol. , vol.23 , pp. 825-833
    • Torres, A.G.1    Payne, S.M.2
  • 28
    • 0029830549 scopus 로고    scopus 로고
    • A putative helical domain in the Malk subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for the interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool
    • Wilken, S., G. Schmees, and E. Schneider. 1996. A putative helical domain in the Malk subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for the interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool. Mol. Microbiol. 22:655-666.
    • (1996) Mol. Microbiol. , vol.22 , pp. 655-666
    • Wilken, S.1    Schmees, G.2    Schneider, E.3
  • 29
    • 0030614426 scopus 로고    scopus 로고
    • The LightCycler: A microvolume multisample fluorimeter with rapid temperature control
    • Wittwer, C. T., K. M. Ririe, R. V. Andrew, D. A. David, R. A. Gundry, and U. J. Balis. 1997. The LightCycler: a microvolume multisample fluorimeter with rapid temperature control. BioTechniques 22:176-181.
    • (1997) BioTechniques , vol.22 , pp. 176-181
    • Wittwer, C.T.1    Ririe, K.M.2    Andrew, R.V.3    David, D.A.4    Gundry, R.A.5    Balis, U.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.