메뉴 건너뛰기




Volumn 49, Issue 1, 2003, Pages 211-218

In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MALEIMIDE DERIVATIVE; OREGON GREEN 488 MALEIMIDE; PROTEIN TONB; UNCLASSIFIED DRUG;

EID: 0038385104     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03579.x     Document Type: Article
Times cited : (48)

References (34)
  • 1
    • 0024452245 scopus 로고
    • The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity
    • Braun, V. (1989) The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity. J Bacteriol 171: 6387-6390.
    • (1989) J Bacteriol , vol.171 , pp. 6387-6390
    • Braun, V.1
  • 2
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun, V., and Braun, M. (2002) Active transport of iron and siderophore antibiotics. Curr Opin Microbiol 5: 194-201.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 194-201
    • Braun, V.1    Braun, M.2
  • 3
    • 0027193060 scopus 로고
    • Evolutionary relationship of uptake systems for biopolymers in Escherichia coli cross-complementation between the TonB-ExbB- ExbD and the TolA-TolQ-TolR proteins
    • Braun, V., and Herrmann, C. (1993) Evolutionary relationship of uptake systems for biopolymers in Escherichia coli cross-complementation between the TonB-ExbB- ExbD and the TolA-TolQ-TolR proteins. Mol Microbiol 8: 261-268.
    • (1993) Mol Microbiol , vol.8 , pp. 261-268
    • Braun, V.1    Herrmann, C.2
  • 4
    • 0029913411 scopus 로고    scopus 로고
    • Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity
    • Braun, V., Gaisser, S., Herrman, C., Kampfenkel, K., Killman, H., and Traub, I. (1996) Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity. J Bacteriol 178: 2836-2845.
    • (1996) J Bacteriol , vol.178 , pp. 2836-2845
    • Braun, V.1    Gaisser, S.2    Herrman, C.3    Kampfenkel, K.4    Killman, H.5    Traub, I.6
  • 5
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold. J Biol Chem 276: 27535-27540.
    • (2001) J Biol Chem , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 6
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot, R., and Vanderleyden, J. (1994) The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol Microbiol 12: 333-334.
    • (1994) Mol Microbiol , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 7
    • 0024723058 scopus 로고
    • Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: Phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB
    • Fischer, E., Günter, K., and Braun, V. (1989) Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB. J Bacteriol 171: 5127-5134.
    • (1989) J Bacteriol , vol.171 , pp. 5127-5134
    • Fischer, E.1    Günter, K.2    Braun, V.3
  • 8
    • 0025599473 scopus 로고
    • TonB protein of Salmonella typhimurium. A model for signal transduction between membranes
    • Hannavy, K., Barr, G.C., Dorman, C.J., Adamson, J., Mazengera, L.R., Gallagher, M.P., et al. (1990) TonB protein of Salmonella typhimurium. A model for signal transduction between membranes. J Mol Biol 216: 897-910.
    • (1990) J Mol Biol , vol.216 , pp. 897-910
    • Hannavy, K.1    Barr, G.C.2    Dorman, C.J.3    Adamson, J.4    Mazengera, L.R.5    Gallagher, M.P.6
  • 9
    • 0036723874 scopus 로고    scopus 로고
    • ExbB and ExbD do not function independently in TonB-dependent energy transduction
    • Held, K.G., and Postle, K. (2002) ExbB and ExbD do not function independently in TonB-dependent energy transduction. J Bacteriol 184: 5170-5173.
    • (2002) J Bacteriol , vol.184 , pp. 5170-5173
    • Held, K.G.1    Postle, K.2
  • 10
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs, P.I., Myers, P.S., and Postle, K. (1998) Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers. J Bacteriol 180: 6031-6038.
    • (1998) J Bacteriol , vol.180 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 11
    • 0036188943 scopus 로고    scopus 로고
    • TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli
    • Higgs, P.I., Letain, T.E., Merriam, K.K., Burke, N.S., Park, H., Kang, C., and Postle, K. (2002) TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli. J Bacteriol 184: 1640-1648.
    • (2002) J Bacteriol , vol.184 , pp. 1640-1648
    • Higgs, P.I.1    Letain, T.E.2    Merriam, K.K.3    Burke, N.S.4    Park, H.5    Kang, C.6    Postle, K.7
  • 12
    • 0028280919 scopus 로고
    • Role of the TonB amino terminus in energy transduction between membranes
    • Jaskula, J.C., Letain, T.E., Roof, S.K., Skare, J.T., and Postle, K. (1994) Role of the TonB amino terminus in energy transduction between membranes. J Bacteriol 176: 2326-2338.
    • (1994) J Bacteriol , vol.176 , pp. 2326-2338
    • Jaskula, J.C.1    Letain, T.E.2    Roof, S.K.3    Skare, J.T.4    Postle, K.5
  • 13
    • 0027154838 scopus 로고
    • A sequence-specific function for the N-terminal signal-like sequence of the TonB protein
    • Karlsson, M., Hannavy, K., and Higgins, C.F. (1993) A sequence-specific function for the N-terminal signal-like sequence of the TonB protein. Mol Microbiol 8: 379-388.
    • (1993) Mol Microbiol , vol.8 , pp. 379-388
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 14
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope
    • Klebba, P.E., Rutz, J.M., Liu, J., and Murphy, C.K. (1993) Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J Bioenerg Biomembr 25: 603-611.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 15
    • 0027165444 scopus 로고
    • The molecular interaction between components of the TonB-ExbBD-dependent and of the TolQRA-dependent bacterial uptake systems
    • Koebnik, R. (1993) The molecular interaction between components of the TonB-ExbBD-dependent and of the TolQRA-dependent bacterial uptake systems. Mol Microbiol 9: 219.
    • (1993) Mol Microbiol , vol.9 , pp. 219
    • Koebnik, R.1
  • 16
    • 0035896546 scopus 로고    scopus 로고
    • Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force
    • Larsen, R.A., and Postle, K. (2001) Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force. J Biol Chem 276: 8111-8117.
    • (2001) J Biol Chem , vol.276 , pp. 8111-8117
    • Larsen, R.A.1    Postle, K.2
  • 17
    • 0027730652 scopus 로고
    • The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein
    • Larsen, R.A., Wood, G.E., and Postle, K. (1993) The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol Microbiol 10: 943-953.
    • (1993) Mol Microbiol , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, G.E.2    Postle, K.3
  • 18
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (ΔV17) by a missense mutation in ExbB
    • Larsen, R.A., Thomas, M.T., Wood, G.E., and Postle, K. (1994) Partial suppression of an Escherichia coli TonB transmembrane domain mutation (ΔV17) by a missense mutation in ExbB. Mol Microbiol 13: 627-640.
    • (1994) Mol Microbiol , vol.13 , pp. 627-640
    • Larsen, R.A.1    Thomas, M.T.2    Wood, G.E.3    Postle, K.4
  • 19
    • 0029958770 scopus 로고    scopus 로고
    • Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes
    • Larsen, R.A., Myers, P.S., Skare, J.T., Seachord, C.L., Darveau, R.P., and Postle, K. (1996) Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes. J Bacteriol 178: 1363-1373.
    • (1996) J Bacteriol , vol.178 , pp. 1363-1373
    • Larsen, R.A.1    Myers, P.S.2    Skare, J.T.3    Seachord, C.L.4    Darveau, R.P.5    Postle, K.6
  • 20
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • Larsen, R.A., Foster-Hartnett, D., McIntosh, M.A., and Postle, K. (1997) Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions. J Bacteriol 179: 3213-3221.
    • (1997) J Bacteriol , vol.179 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 21
    • 0032991467 scopus 로고    scopus 로고
    • Proton-motive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen, R.A., Thomas, M.G., and Postle, K. (1999) Proton-motive force, ExbB and ligand-bound FepA drive conformational changes in TonB. Mol Microbiol 31: 1809-1824.
    • (1999) Mol Microbiol , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 22
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Gram-negative bacteria
    • Letain, T.E., and Postle, K. (1997) TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Gram-negative bacteria. Mol Microbiol 24: 271-283.
    • (1997) Mol Microbiol , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 23
    • 0028051476 scopus 로고
    • Site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA
    • Liu, J., Rutz, J.M., Klebba, P.E., and Feix, J.B. (1994) Site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA. Biochemistry 33: 13274-13283.
    • (1994) Biochemistry , vol.33 , pp. 13274-13283
    • Liu, J.1    Rutz, J.M.2    Klebba, P.E.3    Feix, J.B.4
  • 24
    • 0034944420 scopus 로고    scopus 로고
    • The Tol-Pal proteins of the Escherichia coli cell envelope: An energized system required for outer membrane integrity?
    • Lloubes, R., Cascales, E., Walberger, A., Bouveret, E., Lazdunski, C., Bernadac, A., and Journet, L. (2001) The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity? Res Microbiol 152: 523-529.
    • (2001) Res Microbiol , vol.152 , pp. 523-529
    • Lloubes, R.1    Cascales, E.2    Walberger, A.3    Bouveret, E.4    Lazdunski, C.5    Bernadac, A.6    Journet, L.7
  • 25
    • 0028177644 scopus 로고
    • Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification
    • Michael, S.F. (1994) Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification. Biotechniques 16: 410-412.
    • (1994) Biotechniques , vol.16 , pp. 410-412
    • Michael, S.F.1
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 27
    • 0030680156 scopus 로고    scopus 로고
    • Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor FhuA promotes interaction with the energy-transducing protein TonB
    • Moeck, G.S., Coulton, J.W., and Postle, K. (1997) Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor FhuA promotes interaction with the energy-transducing protein TonB. J Biol Chem 272: 28391-28397.
    • (1997) J Biol Chem , vol.272 , pp. 28391-28397
    • Moeck, G.S.1    Coulton, J.W.2    Postle, K.3
  • 28
    • 0019230249 scopus 로고
    • Transport of vitamin B12 in Escherichia coli. Some observations on the roles of the gene products of btuC and tonB
    • Reynolds, P.R., Mottur, G.P., and Bradbeer, C. (1980) Transport of vitamin B12 in Escherichia coli. Some observations on the roles of the gene products of btuC and tonB. J Biol Chem 255: 4313-4319.
    • (1980) J Biol Chem , vol.255 , pp. 4313-4319
    • Reynolds, P.R.1    Mottur, G.P.2    Bradbeer, C.3
  • 29
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • Roof, S.K., Allard, J.D., Bertrand, K.P., and Postle, K. (1991) Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. J Bacteriol 173: 5554-5557.
    • (1991) J Bacteriol , vol.173 , pp. 5554-5557
    • Roof, S.K.1    Allard, J.D.2    Bertrand, K.P.3    Postle, K.4
  • 30
    • 0028084846 scopus 로고
    • Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12
    • Silber, K.R., and Sauer, R.T. (1994) Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12. Mol Gen Genet 242: 237-240.
    • (1994) Mol Gen Genet , vol.242 , pp. 237-240
    • Silber, K.R.1    Sauer, R.T.2
  • 31
    • 0024506353 scopus 로고
    • A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli
    • Singer, M., Baker, T.A., Schnitzler, G., Deischel, S.M., Goel, M., Dove, W., et al. (1989) A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol Rev 53: 1-24.
    • (1989) Microbiol Rev , vol.53 , pp. 1-24
    • Singer, M.1    Baker, T.A.2    Schnitzler, G.3    Deischel, S.M.4    Goel, M.5    Dove, W.6
  • 32
    • 0027282061 scopus 로고
    • Energy transduction between membranes - TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
    • Skare, J.T., Ahmer, B.M.M., Seachord, C.L., Darveau, R.P., and Postle, K. (1993) Energy transduction between membranes - TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA. J Biol Chem 268: 16302-16308.
    • (1993) J Biol Chem , vol.268 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 33
    • 0020028246 scopus 로고
    • The tonB gene of E. coli: Energy-coupling or molecular processing of permeases?
    • Wookey, P. (1982) The tonB gene of E. coli: Energy-coupling or molecular processing of permeases? FEBS Lett 139: 145-154.
    • (1982) FEBS Lett , vol.139 , pp. 145-154
    • Wookey, P.1
  • 34
    • 0027484363 scopus 로고
    • Identification of a residue in the translocation pathway of a membrane carrier
    • Yan, R.T., and Maloney, P.C. (1993) Identification of a residue in the translocation pathway of a membrane carrier. Cell 75: 37-44.
    • (1993) Cell , vol.75 , pp. 37-44
    • Yan, R.T.1    Maloney, P.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.