메뉴 건너뛰기




Volumn 187, Issue 13, 2005, Pages 4637-4645

Activities of the Serratia marcescens heme receptor HasR and isolated plug and β-barrel domains: The β-barrel forms a heme-specific channel

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; HEME; MEMBRANE PROTEIN; MEMBRANE RECEPTOR;

EID: 21144458518     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.13.4637-4645.2005     Document Type: Article
Times cited : (24)

References (38)
  • 2
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell, P. E., C. D. Nau, J. T. Brown, J. Konisky, and R. J. Kadner. 1990. Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J. Bacteriol. 172:6387-6390.
    • (1990) J. Bacteriol. , vol.172 , pp. 6387-6390
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, R.J.5
  • 3
    • 4344690894 scopus 로고    scopus 로고
    • Hemophore-mediated signaling in Serratia marcescens: A new mode of regulation for an extra cytoplasmic function (ECF) sigma factor involved in heme-acquisition
    • Biville, F., H. Cwerman, S. Létoffé, S. Rossi, V. Drouet, J. M. Ghigo, and C. Wandersman. 2004. Hemophore-mediated signaling in Serratia marcescens: a new mode of regulation for an extra cytoplasmic function (ECF) sigma factor involved in heme-acquisition. Mol. Microbiol. 53:1267-1277.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1267-1277
    • Biville, F.1    Cwerman, H.2    Létoffé, S.3    Rossi, S.4    Drouet, V.5    Ghigo, J.M.6    Wandersman, C.7
  • 4
    • 0032862457 scopus 로고    scopus 로고
    • Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: Histidine residues are essential for receptor function
    • Bracken, C. S., M. T. Baer, A. Abdur-Rashid, W. Helms, and I. Stojiljkovic. 1999. Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function. J. Bacteriol. 181:6063-6072.
    • (1999) J. Bacteriol. , vol.181 , pp. 6063-6072
    • Bracken, C.S.1    Baer, M.T.2    Abdur-Rashid, A.3    Helms, W.4    Stojiljkovic, I.5
  • 5
    • 0042838110 scopus 로고    scopus 로고
    • In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12
    • Braun, M., F. Endriss, H. Killmann, and V. Braun. 2003. In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12. J. Bacteriol. 185:5508-5518.
    • (2003) J. Bacteriol. , vol.185 , pp. 5508-5518
    • Braun, M.1    Endriss, F.2    Killmann, H.3    Braun, V.4
  • 6
    • 0036411842 scopus 로고    scopus 로고
    • Diffusion through channel derivatives of the Escherichia coli FhuA transport protein
    • Braun, M., H. Killmann, E. Maier, R. Benz, and V. Braun. 2002. Diffusion through channel derivatives of the Escherichia coli FhuA transport protein. Eur. J. Biochem. 269:4948-4959.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4948-4959
    • Braun, M.1    Killmann, H.2    Maier, E.3    Benz, R.4    Braun, V.5
  • 8
    • 0032849375 scopus 로고    scopus 로고
    • Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
    • Cadieux, N., and R. J. Kadner. 1999. Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter. Proc. Natl. Acad. Sci. USA 96: 10673-10678.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 9
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu, A., A. Shelenkov, and R. J. Dunbrack. 2003. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12:2001-2014.
    • (2003) Protein Sci. , vol.12 , pp. 2001-2014
    • Canutescu, A.1    Shelenkov, A.2    Dunbrack, R.J.3
  • 10
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento, D. P., A. K. Mohanty, R. J. Kadner, and M. C. Wiener. 2003. Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat. Struct. Biol. 10:394-401.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 11
    • 14144255323 scopus 로고    scopus 로고
    • The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6A resolution
    • Cobessi, D., H. Celia, N. Folschweiller, I. J. Schalk, M. A. Abdallah, and F. Pattus. 2005. The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6A resolution. J. Mol. Biol. 347:121-134.
    • (2005) J. Mol. Biol. , vol.347 , pp. 121-134
    • Cobessi, D.1    Celia, H.2    Folschweiller, N.3    Schalk, I.J.4    Abdallah, M.A.5    Pattus, F.6
  • 12
    • 16644398584 scopus 로고    scopus 로고
    • Crystallization and X-ray diffraction analyses of the outer membrane pyochelin receptor FptA from Pseudomonas aeruginosa
    • Cobessi, D., H. Celia, and F. Pattus. 2004. Crystallization and X-ray diffraction analyses of the outer membrane pyochelin receptor FptA from Pseudomonas aeruginosa. Acta Crystallogr. D Biol. Crystallogr. 60:1919-1921.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1919-1921
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 13
    • 0036947253 scopus 로고    scopus 로고
    • Signal sequence mutations as tools for the characterization of LamB folding intermediates
    • Duguay, A. R., and T. J. Silhavy. 2002. Signal sequence mutations as tools for the characterization of LamB folding intermediates. J. Bacteriol. 184:6918-6928.
    • (2002) J. Bacteriol. , vol.184 , pp. 6918-6928
    • Duguay, A.R.1    Silhavy, T.J.2
  • 14
    • 0033954445 scopus 로고    scopus 로고
    • Surface signaling in ferric citrate transport gene induction: Interaction of the FecA, FecR, and Feel regulatory proteins
    • Enz, S., S. Mahren, U. H. Stroeher, and V. Braun. 2000. Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR, and Feel regulatory proteins. J. Bacteriol. 182:637-646.
    • (2000) J. Bacteriol. , vol.182 , pp. 637-646
    • Enz, S.1    Mahren, S.2    Stroeher, U.H.3    Braun, V.4
  • 15
    • 0030756034 scopus 로고    scopus 로고
    • Folding of a bacterial outer membrane protein during passage through the periplasm
    • Eppens, E. F., N. Nouwen, and J. Tommassen. 1997. Folding of a bacterial outer membrane protein during passage through the periplasm. EMBO J. 16:4295-4301.
    • (1997) EMBO J. , vol.16 , pp. 4295-4301
    • Eppens, E.F.1    Nouwen, N.2    Tommassen, J.3
  • 17
    • 0842329749 scopus 로고    scopus 로고
    • Metal import through microbial membranes
    • Ferguson, A. D., and J. Deisenhofer. 2004. Metal import through microbial membranes. Cell 116:15-24.
    • (2004) Cell , vol.116 , pp. 15-24
    • Ferguson, A.D.1    Deisenhofer, J.2
  • 18
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., E. Hofmann, J. W. Coulton, K. Diederichs, and W. Welte. 1998. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282:2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 19
    • 1842326840 scopus 로고    scopus 로고
    • A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
    • Ghigo, J. M., S. Létoffé, and C. Wandersman. 1997. A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J. Bacteriol. 179:3572-3579.
    • (1997) J. Bacteriol. , vol.179 , pp. 3572-3579
    • Ghigo, J.M.1    Létoffé, S.2    Wandersman, C.3
  • 20
    • 0035222012 scopus 로고    scopus 로고
    • A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization
    • Guda, C., E. D. Scheeff, P. E. Bourne, and I. N. Shyndyalov. 2001. A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization. Pacific Symp. Biocomput. 6:275-286.
    • (2001) Pacific Symp. Biocomput. , vol.6 , pp. 275-286
    • Guda, C.1    Scheeff, E.D.2    Bourne, P.E.3    Shyndyalov, I.N.4
  • 21
    • 0141707666 scopus 로고    scopus 로고
    • Ligand delivery by heme carrier proteins: The binding of Serralia marcescens hemophore to its outer membrane receptor is mediated by two distinct peptide regions
    • Létoffé, S., L. Debarbieux, N. Izadi, N. Delepelaire, and C. Wandersman. 2003. Ligand delivery by heme carrier proteins: the binding of Serralia marcescens hemophore to its outer membrane receptor is mediated by two distinct peptide regions. Mol. Microbiol. 50:77-88.
    • (2003) Mol. Microbiol. , vol.50 , pp. 77-88
    • Létoffé, S.1    Debarbieux, L.2    Izadi, N.3    Delepelaire, N.4    Wandersman, C.5
  • 22
    • 3042521155 scopus 로고    scopus 로고
    • Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex
    • Létoffé, S., P. Delepelaire, and C. Wandersman. 2004. Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex. J. Bacteriol. 186: 4067-4074.
    • (2004) J. Bacteriol. , vol.186 , pp. 4067-4074
    • Létoffé, S.1    Delepelaire, P.2    Wandersman, C.3
  • 23
    • 0028023120 scopus 로고
    • Secretion of the Serratia marcescens HasA protein by an ABC transporter
    • Létoffé, S., J. M. Ghigo, and C. Wandersman. 1994. Secretion of the Serratia marcescens HasA protein by an ABC transporter. J. Bacteriol. 176:5372-5377.
    • (1994) J. Bacteriol. , vol.176 , pp. 5372-5377
    • Létoffé, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 24
    • 0042990231 scopus 로고    scopus 로고
    • Interactions of HasA, a bacterial haemophore, with haemoglobin and with its outer membrane receptor HasR
    • Létoffé, S., F. Nato, M. E. Goldberg, and C. Wandersman. 1999. Interactions of HasA, a bacterial haemophore, with haemoglobin and with its outer membrane receptor HasR. Mol. Microbiol. 33:546-555.
    • (1999) Mol. Microbiol. , vol.33 , pp. 546-555
    • Létoffé, S.1    Nato, F.2    Goldberg, M.E.3    Wandersman, C.4
  • 27
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 28
    • 1942532328 scopus 로고    scopus 로고
    • The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel
    • Oke, M., R. Sarra, R. Ghirlando, S. Farnaud, A. Gorringe, R. Evans, and S. Buchanan. 2004. The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel. FEBS Lett. 564:294-300.
    • (2004) FEBS Lett. , vol.564 , pp. 294-300
    • Oke, M.1    Sarra, R.2    Ghirlando, R.3    Farnaud, S.4    Gorringe, A.5    Evans, R.6    Buchanan, S.7
  • 29
    • 0016339106 scopus 로고
    • Separation of the inner (cytoplasmic) and outer membranes of Gram-negative bacteria
    • Osborn, M. J., and R. Munson. 1974. Separation of the inner (cytoplasmic) and outer membranes of Gram-negative bacteria. Methods Enzymol. 31: 642-653.
    • (1974) Methods Enzymol. , vol.31 , pp. 642-653
    • Osborn, M.J.1    Munson, R.2
  • 30
    • 0035174049 scopus 로고    scopus 로고
    • Characterization of HasB, a Serratia marcescens TonB-like protein specifically involved in the haemophore-dependent haem acquisition system
    • Paquelin, A., J. M. Ghigo, S. Bertin, and C. Wandersman. 2001. Characterization of HasB, a Serratia marcescens TonB-like protein specifically involved in the haemophore-dependent haem acquisition system. Mol. Microbiol. 42: 995-1005.
    • (2001) Mol. Microbiol. , vol.42 , pp. 995-1005
    • Paquelin, A.1    Ghigo, J.M.2    Bertin, S.3    Wandersman, C.4
  • 31
    • 0033587572 scopus 로고    scopus 로고
    • Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: Implications for siderophore-mediated iron transport
    • Schalk, I. J., P. Kyslik, D. Prome, A. van Dorsselaer, K. Poole, M. A. Abdallah, and F. Pattus. 1999. Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: implications for siderophore-mediated iron transport. Biochemistry 38:9357-9365.
    • (1999) Biochemistry , vol.38 , pp. 9357-9365
    • Schalk, I.J.1    Kyslik, P.2    Prome, D.3    Van Dorsselaer, A.4    Poole, K.5    Abdallah, M.A.6    Pattus, F.7
  • 32
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., F. Milpetz, P. Bork, and C. P. Ponting. 1998. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0035845572 scopus 로고    scopus 로고
    • The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain. Proc
    • Usher, K. C., E. Ozkan, K. H. Gardner, and J. Deisenhofer. 2001. The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain. Proc. Natl. Acad. Sci. USA 98:10676-10681.
    • (2001) Natl. Acad. Sci. USA , vol.98 , pp. 10676-10681
    • Usher, K.C.1    Ozkan, E.2    Gardner, K.H.3    Deisenhofer, J.4
  • 35
    • 0036778139 scopus 로고    scopus 로고
    • FepA with globular domain deletions lacks activity
    • Vakharia, H., and K. Postle. 2002. FepA with globular domain deletions lacks activity. J. Bacteriol. 184:5508-5512.
    • (2002) J. Bacteriol. , vol.184 , pp. 5508-5512
    • Vakharia, H.1    Postle, K.2
  • 36
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: From siderophores to hemophores
    • Wandersman, C., and P. Delepelaire. 2004. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58:611-647.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 37
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: Role of hemophores and receptors
    • Wandersman, C., and I. Stojiljkovic. 2000. Bacterial heme sources: role of hemophores and receptors. Curr. Opin. Microbiol. 3:215-220.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2
  • 38
    • 0037369939 scopus 로고    scopus 로고
    • Hemin binding, functional expression, and complementation analysis of Pap 31 from Bartonella henselae
    • Zimmermann, R., V. Kempf, E. Schiltz, K. Oberle, and A. Sander. 2003. Hemin binding, functional expression, and complementation analysis of Pap 31 from Bartonella henselae. J. Bacteriol. 185:1739-1744.
    • (2003) J. Bacteriol. , vol.185 , pp. 1739-1744
    • Zimmermann, R.1    Kempf, V.2    Schiltz, E.3    Oberle, K.4    Sander, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.