메뉴 건너뛰기




Volumn 20, Issue 3-4, 2007, Pages 219-231

Energy-coupled outer membrane transport proteins and regulatory proteins

Author keywords

Bacterial iron and sugar transporters; ECF sigma factors; Signaling device

Indexed keywords

BACTERIAL DNA; BACTERIAL TOXIN; CARRIER PROTEIN; CYANOCOBALAMIN; FERRIC HYDROXAMATE UPTAKE PROTEIN COMPONENT A; FERRIC ION; FERRICHROME; IRON; MUTANT PROTEIN; PROTEIN BTUB; PROTEIN CIR; PROTEIN FECA; PROTEIN FEPA; PROTEIN TONB; REGULATOR PROTEIN; RNA POLYMERASE; SIDEROPHORE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 34248659388     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-006-9072-5     Document Type: Conference Paper
Times cited : (68)

References (43)
  • 1
    • 0034888050 scopus 로고    scopus 로고
    • Mutations in the Escherichia coli receptor FepA reveals residues involved in ligand binding and transport
    • Barnard TJ, Watson ME Jr, McIntosh MA (2001) Mutations in the Escherichia coli receptor FepA reveals residues involved in ligand binding and transport. Mol Microbiol 41:527-536
    • (2001) Mol Microbiol , vol.41 , pp. 527-536
    • Barnard, T.J.1    Watson Jr., M.E.2    McIntosh, M.A.3
  • 2
    • 0037221477 scopus 로고    scopus 로고
    • Siderophore-mediated cell signalling in Pseudomonas aeruginosa: Divergent pathways regulate virulence factor production and siderophore receptor synthesis
    • Beare PA, For RJ, Martin LW, Lamont IL (2003) Siderophore-mediated cell signalling in Pseudomonas aeruginosa: divergent pathways regulate virulence factor production and siderophore receptor synthesis. Mol Microbiol 47:195-207
    • (2003) Mol Microbiol , vol.47 , pp. 195-207
    • Beare, P.A.1    For, R.J.2    Martin, L.W.3    Lamont, I.L.4
  • 3
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell PE, Nau CD, Brown JT, Konisky J, Kadner RJ (1990) Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J Bacteriol 172:3826-3829
    • (1990) J Bacteriol , vol.172 , pp. 3826-3829
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, R.J.5
  • 4
    • 33846015876 scopus 로고    scopus 로고
    • Functional genomic and metabolic studies of the adaptations of a prominent adult human gut symbiont, Bacteroides thetaiotaomicron, to the suckling period.
    • Bjursell MK, Martens EC, Gordon JI (2006) Functional genomic and metabolic studies of the adaptations of a prominent adult human gut symbiont, Bacteroides thetaiotaomicron, to the suckling period. J Biol Chem 281:36269-36279
    • (2006) J Biol Chem , vol.281 , pp. 36269-36279
    • Bjursell, M.K.1    Martens, E.C.2    Gordon, J.I.3
  • 5
    • 0030925485 scopus 로고    scopus 로고
    • Surface signaling: Novel transcription initiation mechanism starting from the cell surface
    • Braun V (1997) Surface signaling: novel transcription initiation mechanism starting from the cell surface. Arch Microbiol 167:325-331
    • (1997) Arch Microbiol , vol.167 , pp. 325-331
    • Braun, V.1
  • 6
    • 0038352101 scopus 로고    scopus 로고
    • Regulation of the FecI-type ECF sigma factor by transmembrane signalling
    • Braun V, Mahren S, Ogierman M (2003) Regulation of the FecI-type ECF sigma factor by transmembrane signalling. Curr Opin Microbiol 6:173-180
    • (2003) Curr Opin Microbiol , vol.6 , pp. 173-180
    • Braun, V.1    Mahren, S.2    Ogierman, M.3
  • 7
    • 23744444687 scopus 로고    scopus 로고
    • Transmembrane transcriptional control (surface signalling) of the Escherichia coli Fec type
    • Braun V, Mahren S (2005) Transmembrane transcriptional control (surface signalling) of the Escherichia coli Fec type. FEMS Microbiol Rev 29:673-684
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 673-684
    • Braun, V.1    Mahren, S.2
  • 8
    • 33646914355 scopus 로고    scopus 로고
    • Gene regulation by transmembrane signaling
    • Braun V, Mahren S, Sauter A (2006) Gene regulation by transmembrane signaling. Biometals 19:103-113
    • (2006) Biometals , vol.19 , pp. 103-113
    • Braun, V.1    Mahren, S.2    Sauter, A.3
  • 9
    • 33749009804 scopus 로고    scopus 로고
    • Residues involved in FecR binding are localized on one side of the FecA signaling domain in Escherichia coli
    • Breidenstein E, Mahren S, Braun V (2006) Residues involved in FecR binding are localized on one side of the FecA signaling domain in Escherichia coli. J Bacteriol 188:6440-6442
    • (2006) J Bacteriol , vol.188 , pp. 6440-6442
    • Breidenstein, E.1    Mahren, S.2    Braun, V.3
  • 10
    • 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, Kadner RJ (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
  • 11
    • 0033764762 scopus 로고    scopus 로고
    • Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein
    • Cadieux N, Bradbeer C, Kadner RJ (2000) Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein. J Bacteriol 182:5954-5961
    • (2000) J Bacteriol , vol.182 , pp. 5954-5961
    • Cadieux, N.1    Bradbeer, C.2    Kadner, R.J.3
  • 12
    • 0035205390 scopus 로고    scopus 로고
    • Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron
    • Cho KH, Salyers AA (2001) Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron. J Bacteriol 183:7224-7230
    • (2001) J Bacteriol , vol.183 , pp. 7224-7230
    • Cho, K.H.1    Salyers, A.A.2
  • 13
    • 0035923423 scopus 로고    scopus 로고
    • Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter
    • Coggshall KA, Cadieux N, Piedmont C, Kadner RJ, Cafiso DS (2001) Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter. Biochemistry 40:13964-13971
    • (2001) Biochemistry , vol.40 , pp. 13964-13971
    • Coggshall, K.A.1    Cadieux, N.2    Piedmont, C.3    Kadner, R.J.4    Cafiso, D.S.5
  • 14
    • 33646236127 scopus 로고    scopus 로고
    • Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade
    • Cwerman H, Wandersman C, Biville F (2006) Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade. J Bacteriol 188:3357-3364
    • (2006) J Bacteriol , vol.188 , pp. 3357-3364
    • Cwerman, H.1    Wandersman, C.2    Biville, F.3
  • 15
    • 24044525255 scopus 로고    scopus 로고
    • Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains
    • Eisenhauer HA, Shames S, Pawelek PD, Coulton JW (2005) Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains. J Biol Chem 280:30574-30580
    • (2005) J Biol Chem , vol.280 , pp. 30574-30580
    • Eisenhauer, H.A.1    Shames, S.2    Pawelek, P.D.3    Coulton, J.W.4
  • 16
    • 0043165150 scopus 로고    scopus 로고
    • Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity
    • Endriß F, Braun M, Killmann H, Braun V (2003) Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity. J Bacteriol 185:4683-4692
    • (2003) J Bacteriol , vol.185 , pp. 4683-4692
    • Endriß, F.1    Braun, M.2    Killmann, H.3    Braun, V.4
  • 18
    • 0002891822 scopus 로고    scopus 로고
    • The ferric hydroxamate uptake receptor FhuA and related TonB dependent transporters in the outer membrane of gram-negative bacteria
    • Chichester Ltd Wiley, New York
    • Ferguson AD, Coulton JW, Diederichs K, Welte W (2001) The ferric hydroxamate uptake receptor FhuA and related TonB dependent transporters in the outer membrane of gram-negative bacteria. In: Messerschmidt A, Huber R, Poulos T, Wiegenhardt K (eds) Handbook of Metalloproteins. Chichester Ltd., Wiley, New York, pp 834-849
    • (2001) Handbook of Metalloproteins , pp. 834-849
    • Ferguson, A.D.1    Coulton, J.W.2    Diederichs, K.3    Welte, W.4    Messerschmidt, A.5    Huber, R.6    Poulos, T.7    Wiegenhardt, K.8
  • 19
    • 0842329749 scopus 로고    scopus 로고
    • Metal import through microbial membranes
    • Ferguson AD, Deisenhofer J (2004) Metal import through microbial membranes. Cell 116:15-24
    • (2004) Cell , vol.116 , pp. 15-24
    • Ferguson, A.D.1    Deisenhofer, J.2
  • 20
    • 28244476414 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli
    • Garcia-Herrero A, Vogel HJ (2005) Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Mol Microbiol 58:1226-1237
    • (2005) Mol Microbiol , vol.58 , pp. 1226-1237
    • Garcia-Herrero, A.1    Vogel, H.J.2
  • 21
    • 12344263219 scopus 로고    scopus 로고
    • Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein
    • Ghosh J, Postle K (2005) Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein. Mol Microbiol 55:276-288
    • (2005) Mol Microbiol , vol.55 , pp. 276-288
    • Ghosh, J.1    Postle, K.2
  • 23
    • 0025001648 scopus 로고
    • In vivo evidence for FhuA outer membrane receptor interaction with TonB inner membrane protein of Escherichia coli
    • Günter K, Braun V (1990) In vivo evidence for FhuA outer membrane receptor interaction with TonB inner membrane protein of Escherichia coli. FEBS 274:85-88
    • (1990) FEBS , vol.274 , pp. 85-88
    • Günter, K.1    Braun, V.2
  • 25
    • 0017258036 scopus 로고
    • Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli
    • Hancock RW, Braun V (1976) Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli. J Bacteriol 125:409-415
    • (1976) J Bacteriol , vol.125 , pp. 409-415
    • Hancock, R.W.1    Braun, V.2
  • 26
    • 0023886391 scopus 로고
    • Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli
    • Heller KJ, Kadner RJ, Gunther K (1988) Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli. Gene 64:147-153
    • (1988) Gene , vol.64 , pp. 147-153
    • Heller, K.J.1    Kadner, R.J.2    Gunther, K.3
  • 27
    • 0029805603 scopus 로고    scopus 로고
    • Properties of the FhuA channel in the Escherichia coli outer membrane after deletion of FhuA portions within and outside the predicted gating loop
    • Killmann H, Benz R, Braun V (1996) Properties of the FhuA channel in the Escherichia coli outer membrane after deletion of FhuA portions within and outside the predicted gating loop. J Bacteriol 178:6913-6920
    • (1996) J Bacteriol , vol.178 , pp. 6913-6920
    • Killmann, H.1    Benz, R.2    Braun, V.3
  • 28
    • 0842347939 scopus 로고    scopus 로고
    • RhuR, an extracytoplasmic function sigma factor activator, is essential for heme-dependent expression of the outer membrane heme and hemoprotein receptor of Bordetella avium
    • Kirby AE, King ND, Connell TD (2004) RhuR, an extracytoplasmic function sigma factor activator, is essential for heme-dependent expression of the outer membrane heme and hemoprotein receptor of Bordetella avium. Infect Immun 72:896-907
    • (2004) Infect Immun , vol.72 , pp. 896-907
    • Kirby, A.E.1    King, N.D.2    Connell, T.D.3
  • 29
    • 0028224918 scopus 로고
    • Role for the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope
    • Koster M, van Klompenburg W, Bitter W, Leong J, Weisbeek P (1994) Role for the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope. EMBO J 13:2805-2813
    • (1994) EMBO J , vol.13 , pp. 2805-2813
    • Koster, M.1    Van Klompenburg, W.2    Bitter, W.3    Leong, J.4    Weisbeek, P.5
  • 31
    • 1942438093 scopus 로고    scopus 로고
    • FhuA mutant of Escherichia coli is infected by phage T1-independent of TonB
    • Langenscheid J, Killmann H, Braun V (2004) FhuA mutant of Escherichia coli is infected by phage T1-independent of TonB. FEMS Microbiol Lett 234:133-137
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 133-137
    • Langenscheid, J.1    Killmann, H.2    Braun, V.3
  • 32
    • 0034819659 scopus 로고    scopus 로고
    • Ferric dicitrate transport system (Fec) of Shigella flexneri 2a YSH6000 is encoded on a novel pathogenicity island carrying multiple antibiotic resistance genes
    • Luck SN, Turner SA, Rajakumar K, Sakellaris H, Adler B (2001) Ferric dicitrate transport system (Fec) of Shigella flexneri 2a YSH6000 is encoded on a novel pathogenicity island carrying multiple antibiotic resistance genes. Infect Immun 69:6012-6021
    • (2001) Infect Immun , vol.69 , pp. 6012-6021
    • Luck, S.N.1    Turner, S.A.2    Rajakumar, K.3    Sakellaris, H.4    Adler, B.5
  • 33
    • 27744564073 scopus 로고    scopus 로고
    • Occurrence and regulation of the ferric citrate transport system in Escherichia coli B, Klebsiella pneumoniae, Enterobacter aerogenes, and Photorhabdus luminescens
    • Mahren S, Schnell H, Braun V (2005) Occurrence and regulation of the ferric citrate transport system in Escherichia coli B, Klebsiella pneumoniae, Enterobacter aerogenes, and Photorhabdus luminescens. Arch Microbiol 184:175-186
    • (2005) Arch Microbiol , vol.184 , pp. 175-186
    • Mahren, S.1    Schnell, H.2    Braun, V.3
  • 34
    • 28844503096 scopus 로고    scopus 로고
    • ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus
    • Neugebauer H, Herrmann C, Kammer W, Schwarz G, Nordheim A, Braun V (2005) ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus. J Bacteriol 187:8300-8311
    • (2005) J Bacteriol , vol.187 , pp. 8300-8311
    • Neugebauer, H.1    Herrmann, C.2    Kammer, W.3    Schwarz, G.4    Nordheim, A.5    Braun, V.6
  • 35
    • 0037337264 scopus 로고    scopus 로고
    • In vivo cross-linking of the outer membrane ferric citrate transporter FecA and TonB, studies of the FecA TonB box
    • Ogierman M, Braun V (2003) In vivo cross-linking of the outer membrane ferric citrate transporter FecA and TonB, studies of the FecA TonB box. J Bacteriol 185:1870-1885
    • (2003) J Bacteriol , vol.185 , pp. 1870-1885
    • Ogierman, M.1    Braun, V.2
  • 37
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • Schöffler H, Braun V (1989) Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol Gen Genet 217:378-383
    • (1989) Mol Gen Genet , vol.217 , pp. 378-383
    • Schöffler, H.1    Braun, V.2
  • 38
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: Structure of the BtuB:TonB complex
    • Shultis DD, Purdy MD, Banchs CN, Wiener MC (2006) Outer membrane active transport: structure of the BtuB:TonB complex. Science 312:1396-1399
    • (2006) Science , vol.312 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 39
    • 0037309146 scopus 로고    scopus 로고
    • Heme-responsive transcriptional activation of Bordetella bhu genes
    • Vanderpool CK, Armstrong SK (2003) Heme-responsive transcriptional activation of Bordetella bhu genes. J Bacteriol 185:909-917
    • (2003) J Bacteriol , vol.185 , pp. 909-917
    • Vanderpool, C.K.1    Armstrong, S.K.2
  • 40
    • 0036094870 scopus 로고    scopus 로고
    • Sugar transport through maltoporin of Escherichia coli: Role of the greasy slide
    • Van Gelder P, Dumas F, Bartoldus I et al (2002) Sugar transport through maltoporin of Escherichia coli: role of the greasy slide. J Bacteriol 184:2994-2999
    • (2002) J Bacteriol , vol.184 , pp. 2994-2999
    • Van Gelder, P.1    Dumas, F.2    Bartoldus, I.3
  • 41
    • 33644797502 scopus 로고    scopus 로고
    • Import of precursor proteins into isolated yeast mitochondria
    • Wiedemann N, Pfanner N, Rehling P (2006) Import of precursor proteins into isolated yeast mitochondria. Methods Mol Biol 313:373-383
    • (2006) Methods Mol Biol , vol.313 , pp. 373-383
    • Wiedemann, N.1    Pfanner, N.2    Rehling, P.3
  • 42
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: Going for Baroque?
    • Wiener MC (2005) TonB-dependent outer membrane transport: going for Baroque? Curr Opin Struct Biol 15:394-400
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 394-400
    • Wiener, M.C.1
  • 43
    • 0042508859 scopus 로고    scopus 로고
    • Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
    • Yue WW, Grizot S, Buchanan SK (2003) Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J Mol Biol 332:353-368
    • (2003) J Mol Biol , vol.332 , pp. 353-368
    • Yue, W.W.1    Grizot, S.2    Buchanan, S.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.