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Volumn 195, Issue 12, 2013, Pages 2898-2911

Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway

Author keywords

[No Author keywords available]

Indexed keywords

EXBB PROTEIN;

EID: 84880032567     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00017-13     Document Type: Article
Times cited : (20)

References (92)
  • 1
    • 78651364685 scopus 로고    scopus 로고
    • TonB or not TonB: is that the question?
    • Krewulak KD, Vogel HJ. 2011. TonB or not TonB: is that the question? Biochem. Cell Biol. 89:87-97.
    • (2011) Biochem.Cell Biol. , vol.89 , pp. 87-97
    • Krewulak, K.D.1    Vogel, H.J.2
  • 2
    • 77957562075 scopus 로고    scopus 로고
    • The TonB energy transduction systems in Vibrio species
    • Kuehl CJ, Crosa JH. 2010. The TonB energy transduction systems in Vibrio species. Future Microbiol. 5:1403-1412.
    • (2010) Future Microbiol. , vol.5 , pp. 1403-1412
    • Kuehl, C.J.1    Crosa, J.H.2
  • 5
    • 84857155819 scopus 로고    scopus 로고
    • TonB-dependent transporters expressed by Neisseria gonorrhoeae
    • doi:10.3389 /fmicb.2011.00117
    • Cornelissen CN, Hollander A. 2011. TonB-dependent transporters expressed by Neisseria gonorrhoeae. Front. Microbiol. 2:117. doi:10.3389 /fmicb.2011.00117.
    • (2011) Front. Microbiol. , vol.2 , pp. 117
    • Cornelissen, C.N.1    Hollander, A.2
  • 6
    • 33846627273 scopus 로고    scopus 로고
    • Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery
    • Schauer K, Gouget B, Carriere M, Labigne A, de Reuse H. 2007. Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery. Mol. Microbiol. 63:1054-1068.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1054-1068
    • Schauer, K.1    Gouget, B.2    Carriere, M.3    Labigne, A.4    de Reuse, H.5
  • 9
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through TonB-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria
    • doi:10.1371/journal.pone.0000224
    • Blanvillain S, Meyer D, Boulanger A, Lautier M, Guynet C, Denance N, Vasse J, Lauber E, Arlat M. 2007. Plant carbohydrate scavenging through TonB-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS One 2:e224. doi:10.1371/journal.pone.0000224.
    • (2007) PLoS One , vol.2
    • Blanvillain, S.1    Meyer, D.2    Boulanger, A.3    Lautier, M.4    Guynet, C.5    Denance, N.6    Vasse, J.7    Lauber, E.8    Arlat, M.9
  • 10
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • Roof SK, Allard JD, Bertrand KP, 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
  • 11
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • Kampfenkel K, Braun V. 1992. Membrane topology of the Escherichia coli ExbD protein. J. Bacteriol. 174:5485-5487.
    • (1992) J. Bacteriol. , vol.174 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 12
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel K, Braun V. 1993. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 268:6050-6057.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 13
    • 0027238302 scopus 로고
    • ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm
    • Karlsson M, Hannavy K, Higgins CF. 1993. ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm. Mol. Microbiol. 8:389-396.
    • (1993) Mol. Microbiol. , vol.8 , pp. 389-396
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 14
    • 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, 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
  • 15
    • 0029117190 scopus 로고
    • Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability
    • Ahmer BMM, Thomas MG, Larsen RA, Postle K. 1995. Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability. J. Bacteriol. 177:4742-4747.
    • (1995) J. Bacteriol. , vol.177 , pp. 4742-4747
    • Ahmer, B.M.M.1    Thomas, M.G.2    Larsen, R.A.3    Postle, K.4
  • 16
    • 77957662541 scopus 로고    scopus 로고
    • ExbB protein in the cytoplasmic membrane of Escherichia coli forms a stable oligomer
    • Pramanik A, Zhang F, Schwarz H, Schreiber F, Braun V. 2010. ExbB protein in the cytoplasmic membrane of Escherichia coli forms a stable oligomer. Biochemistry 49:8721-8728.
    • (2010) Biochemistry , vol.49 , pp. 8721-8728
    • Pramanik, A.1    Zhang, F.2    Schwarz, H.3    Schreiber, F.4    Braun, V.5
  • 18
    • 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. U. S. A. 96:10673-10678.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 19
    • 0037337264 scopus 로고    scopus 로고
    • Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box
    • Ogierman M, Braun V. 2003. Interactions between 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
  • 20
    • 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 JT, Ahmer BMM, Seachord CL, Darveau RP, 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
  • 21
    • 0041704803 scopus 로고    scopus 로고
    • Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB
    • Zhai YF, Heijne W, Saier MH, Jr. 2003. Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB. Biochim. Biophys. Acta 1614: 201-210.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 201-210
    • Zhai, Y.F.1    Heijne, W.2    Saier, M.H.3
  • 22
    • 33947424588 scopus 로고    scopus 로고
    • His20 provides the sole functionally significant side chain in the essential TonB transmembrane domain
    • Larsen RA, Deckert GE, Kastead KA, Devanathan S, Keller KL, Postle K. 2007. His20 provides the sole functionally significant side chain in the essential TonB transmembrane domain. J. Bacteriol. 189:2825-2833.
    • (2007) J. Bacteriol. , vol.189 , pp. 2825-2833
    • Larsen, R.A.1    Deckert, G.E.2    Kastead, K.A.3    Devanathan, S.4    Keller, K.L.5    Postle, K.6
  • 23
    • 79960411531 scopus 로고    scopus 로고
    • Taking the Escherichia coli TonB transmembrane domain "offline"? Nonprotonatable Asn substitutes fully for TonB His20
    • Swayne C, Postle K. 2011. Taking the Escherichia coli TonB transmembrane domain "offline"? Nonprotonatable Asn substitutes fully for TonB His20. J. Bacteriol. 193:3693-3701.
    • (2011) J. Bacteriol. , vol.193 , pp. 3693-3701
    • Swayne, C.1    Postle, K.2
  • 24
    • 0036723874 scopus 로고    scopus 로고
    • ExbB and ExbD do not function independently in TonB-dependent energy transduction
    • Held KG, 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
  • 25
    • 67651233947 scopus 로고    scopus 로고
    • Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB
    • Ollis AA, Manning M, Held KG, Postle K. 2009. Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB. Mol. Microbiol. 73:466-481.
    • (2009) Mol. Microbiol. , vol.73 , pp. 466-481
    • Ollis, A.A.1    Manning, M.2    Held, K.G.3    Postle, K.4
  • 26
    • 84855811875 scopus 로고    scopus 로고
    • ExbD mutants define initial stages in TonB energization
    • Ollis AA, Postle K. 2012. ExbD mutants define initial stages in TonB energization. J. Mol. Biol. 415:237-247.
    • (2012) J. Mol. Biol. , vol.415 , pp. 237-247
    • Ollis, A.A.1    Postle, K.2
  • 27
    • 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, Herrmann C, Kampfenkel K, Killman H, 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    Herrmann, C.3    Kampfenkel, K.4    Killman, H.5    Traub, I.6
  • 28
    • 3042615583 scopus 로고    scopus 로고
    • Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12
    • Braun V, Herrmann C. 2004. Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12. J. Bacteriol. 186:4402-4406.
    • (2004) J. Bacteriol. , vol.186 , pp. 4402-4406
    • Braun, V.1    Herrmann, C.2
  • 31
    • 0003785155 scopus 로고
    • Experiments in molecular genetics
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Miller JH. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972)
    • Miller, J.H.1
  • 32
    • 78651132012 scopus 로고
    • A chemical basis for the host-induced modification of T-even bacteriophages
    • Shedlovsky A, Brenner S. 1963. A chemical basis for the host-induced modification of T-even bacteriophages. Proc. Natl. Acad. Sci. U. S. A. 50:300-305
    • (1963) Proc. Natl. Acad. Sci. U. S. A. , vol.50 , pp. 300-305
    • Shedlovsky, A.1    Brenner, S.2
  • 33
    • 34347369410 scopus 로고    scopus 로고
    • TonB system, in vivo assays and characterization
    • Postle K. 2007. TonB system, in vivo assays and characterization. Methods Enzymol. 422:245-269.
    • (2007) Methods Enzymol. , vol.422 , pp. 245-269
    • Postle, K.1
  • 34
    • 0041402639 scopus 로고    scopus 로고
    • Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB
    • Larsen RA, Chen GJ, Postle K. 2003. Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB. J. Bacteriol. 185:4699-4706.
    • (2003) J. Bacteriol. , vol.185 , pp. 4699-4706
    • Larsen, R.A.1    Chen, G.J.2    Postle, K.3
  • 35
    • 0036231227 scopus 로고    scopus 로고
    • Quantitation of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA
    • Higgs PI, Larsen RA, Postle K. 2002. Quantitation of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA. Mol. Microbiol. 44:271-281.
    • (2002) Mol. Microbiol. , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 36
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs PI, Myers PS, 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
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0029958770 scopus 로고    scopus 로고
    • Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes
    • Larsen RA, Myers PS, Skare JT, Seachord CL, Darveau RP, 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
  • 39
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen RA, Thomas MG, Postle K. 1999. Protonmotive 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
  • 40
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (V17) by a missense mutation in ExbB
    • Larsen RA, Thomas MT, Wood GE, Postle K. 1994. Partial suppression of an Escherichia coli TonB transmembrane domain mutation (V17) 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
  • 41
    • 0024730355 scopus 로고
    • Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively
    • Eick-Helmerich K, Braun V. 1989. Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively. J. Bacteriol. 171: 5117-5126.
    • (1989) J. Bacteriol. , vol.171 , pp. 5117-5126
    • Eick-Helmerich, K.1    Braun, V.2
  • 42
    • 0034079112 scopus 로고    scopus 로고
    • Selective constraints, amino acid composition, and the rate of protein evolution
    • Tourasse NJ, Li WH. 2000. Selective constraints, amino acid composition, and the rate of protein evolution. Mol. Biol. Evol. 17:656-664.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 656-664
    • Tourasse, N.J.1    Li, W.H.2
  • 43
    • 80053614487 scopus 로고    scopus 로고
    • Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains
    • Jana B, Manning M, Postle K. 2011. Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains. J. Bacteriol. 193:5649-5657.
    • (2011) J. Bacteriol. , vol.193 , pp. 5649-5657
    • Jana, B.1    Manning, M.2    Postle, K.3
  • 44
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey TE. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 45
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: derivation of an implicit membrane potential
    • Ulmschneider MB, Sansom MS, Di Nola A. 2005. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins 59:252-265.
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.2    Di Nola, A.3
  • 46
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
    • Senes A, Engel DE, DeGrado WF. 2004. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14:465-479.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 48
    • 33846839298 scopus 로고    scopus 로고
    • Mutational analyses define helix organization and key residues of a bacterial membrane energytransducing complex
    • Goemaere EL, Cascales E, Lloubes R. 2007. Mutational analyses define helix organization and key residues of a bacterial membrane energytransducing complex. J. Mol. Biol. 366:1424-1436.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1424-1436
    • Goemaere, E.L.1    Cascales, E.2    Lloubes, R.3
  • 49
    • 37549041678 scopus 로고    scopus 로고
    • Interactions of the energy transducer TonB with noncognate energy-harvesting complexes
    • Brinkman KK, Larsen RA. 2008. Interactions of the energy transducer TonB with noncognate energy-harvesting complexes. J. Bacteriol. 190: 421-427.
    • (2008) J. Bacteriol. , vol.190 , pp. 421-427
    • Brinkman, K.K.1    Larsen, R.A.2
  • 50
    • 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, 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
  • 51
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices
    • Sansom MS, Weinstein H. 2000. Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21:445-451.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 52
    • 0025782832 scopus 로고
    • Proline kinks in transmembrane alpha-helices
    • von Heijne G. 1991. Proline kinks in transmembrane alpha-helices. J. Mol. Biol. 218:499-503.
    • (1991) J. Mol. Biol. , vol.218 , pp. 499-503
    • von Heijne, G.1
  • 53
    • 0033000388 scopus 로고    scopus 로고
    • Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli
    • Braun TF, Poulson S, Gully JB, Empey JC, Van Way S, Putnam A, Blair DF. 1999. Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli. J. Bacteriol. 181:3542-3551.
    • (1999) J. Bacteriol. , vol.181 , pp. 3542-3551
    • Braun, T.F.1    Poulson, S.2    Gully, J.B.3    Empey, J.C.4    Van Way, S.5    Putnam, A.6    Blair, D.F.7
  • 54
    • 70349431086 scopus 로고    scopus 로고
    • Role of a conserved prolyl residue (Pro173) of MotA in the mechanochemical reaction cycle of the proton-driven flagellar motor of Salmonella
    • Nakamura S, Morimoto YV, Kami-ike N, Minamino T, Namba K. 2009. Role of a conserved prolyl residue (Pro173) of MotA in the mechanochemical reaction cycle of the proton-driven flagellar motor of Salmonella. J. Mol. Biol. 393:300-307.
    • (2009) J. Mol. Biol. , vol.393 , pp. 300-307
    • Nakamura, S.1    Morimoto, Y.V.2    Kami-ike, N.3    Minamino, T.4    Namba, K.5
  • 55
    • 0030776508 scopus 로고    scopus 로고
    • Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor
    • Zhou J, Blair DF. 1997. Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor. J. Mol. Biol. 273:428-439.
    • (1997) J. Mol. Biol. , vol.273 , pp. 428-439
    • Zhou, J.1    Blair, D.F.2
  • 56
    • 0033609498 scopus 로고    scopus 로고
    • The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane
    • Braun P, von Heijne G. 1999. The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 38:9778-9782.
    • (1999) Biochemistry , vol.38 , pp. 9778-9782
    • Braun, P.1    von Heijne, G.2
  • 57
    • 34648828239 scopus 로고    scopus 로고
    • The role of tryptophan residues in the function and stability of the mechanosensitive channel MscS from Escherichia coli
    • Rasmussen A, Rasmussen T, Edwards MD, Schauer D, Schumann U, Miller S, Booth IR. 2007. The role of tryptophan residues in the function and stability of the mechanosensitive channel MscS from Escherichia coli. Biochemistry 46:10899-10908.
    • (2007) Biochemistry , vol.46 , pp. 10899-10908
    • Rasmussen, A.1    Rasmussen, T.2    Edwards, M.D.3    Schauer, D.4    Schumann, U.5    Miller, S.6    Booth, I.R.7
  • 59
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotAMotB
    • Cascales E, Lloubes R, Sturgis JN. 2001. The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotAMotB. Mol. Microbiol. 42:795-807.
    • (2001) Mol. Microbiol. , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 60
    • 0031944413 scopus 로고    scopus 로고
    • Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB
    • Zhou J, Sharp LL, Tang HL, Lloyd SA, Billings S, Braun TF, Blair DF. 1998. Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB. J. Bacteriol. 180:2729-2735.
    • (1998) J. Bacteriol. , vol.180 , pp. 2729-2735
    • Zhou, J.1    Sharp, L.L.2    Tang, H.L.3    Lloyd, S.A.4    Billings, S.5    Braun, T.F.6    Blair, D.F.7
  • 61
    • 66249145702 scopus 로고    scopus 로고
    • Geometric characteristics of hydrogen bonds involving sulfur atoms in proteins
    • Zhou P, Tian F, Lv F, Shang Z. 2009. Geometric characteristics of hydrogen bonds involving sulfur atoms in proteins. Proteins 76:151-163.
    • (2009) Proteins , vol.76 , pp. 151-163
    • Zhou, P.1    Tian, F.2    Lv, F.3    Shang, Z.4
  • 62
    • 0028009448 scopus 로고
    • Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity
    • Vianney A, Lewin TM, Beyer WF, Lazzaroni JC, Portalier R, Webster RE. 1994. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J. Bacteriol. 176:822-829.
    • (1994) J. Bacteriol. , vol.176 , pp. 822-829
    • Vianney, A.1    Lewin, T.M.2    Beyer, W.F.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 63
    • 0027181940 scopus 로고
    • Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segment
    • Kampfenkel K, Braun V. 1993. Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segment. J. Bacteriol. 175: 4485-4491.
    • (1993) J. Bacteriol. , vol.175 , pp. 4485-4491
    • Kampfenkel, K.1    Braun, V.2
  • 64
    • 0021611311 scopus 로고
    • Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli
    • Dean GE, Macnab RM, Stader J, Matsumura P, Burks C. 1984. Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli. J. Bacteriol. 159:991-999.
    • (1984) J. Bacteriol. , vol.159 , pp. 991-999
    • Dean, G.E.1    Macnab, R.M.2    Stader, J.3    Matsumura, P.4    Burks, C.5
  • 65
    • 0029165325 scopus 로고
    • Membrane topology of the MotA protein of Escherichia coli
    • Zhou JD, Fazzio RT, Blair DF. 1995. Membrane topology of the MotA protein of Escherichia coli. J. Mol. Biol. 251:237-242.
    • (1995) J. Mol. Biol. , vol.251 , pp. 237-242
    • Zhou, J.D.1    Fazzio, R.T.2    Blair, D.F.3
  • 66
    • 0026068420 scopus 로고
    • Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
    • Blair DF, Berg HC. 1991. Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction. J. Mol. Biol. 221:1433-1442.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1433-1442
    • Blair, D.F.1    Berg, H.C.2
  • 67
    • 80053131520 scopus 로고    scopus 로고
    • Sodium-driven motor of the polar flagellum in marine bacteria Vibrio
    • Li N, Kojima S, Homma M. 2011. Sodium-driven motor of the polar flagellum in marine bacteria Vibrio. Genes Cells 16:985-999.
    • (2011) Genes Cells , vol.16 , pp. 985-999
    • Li, N.1    Kojima, S.2    Homma, M.3
  • 68
    • 54849421748 scopus 로고    scopus 로고
    • Membrane segment organization in the stator complex of the flagellar motor: implications for proton flow and proton-induced conformational change
    • Kim EA, Price-Carter M, Carlquist WC, Blair DF. 2008. Membrane segment organization in the stator complex of the flagellar motor: implications for proton flow and proton-induced conformational change. Biochemistry 47:11332-11339.
    • (2008) Biochemistry , vol.47 , pp. 11332-11339
    • Kim, E.A.1    Price-Carter, M.2    Carlquist, W.C.3    Blair, D.F.4
  • 69
    • 0032780519 scopus 로고    scopus 로고
    • Random mutagenesis of the pomA gene encoding a putative channel component of the Na(ω)-driven polar flagellar motor of Vibrio alginolyticus
    • Kojima S, Kuroda M, Kawagishi I, Homma M. 1999. Random mutagenesis of the pomA gene encoding a putative channel component of the Na(ω)-driven polar flagellar motor of Vibrio alginolyticus. Microbiology (Reading, Engl.) 145:1759-1767.
    • (1999) Microbiology (Reading, Engl.) , vol.145 , pp. 1759-1767
    • Kojima, S.1    Kuroda, M.2    Kawagishi, I.3    Homma, M.4
  • 70
    • 0032417321 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli K-12 TolA N-terminal region and characterization of its TolQ-interacting domain by genetic suppression
    • Germon P, Clavel T, Vianney A, Portalier R, Lazzaroni JC. 1998. Mutational analysis of the Escherichia coli K-12 TolA N-terminal region and characterization of its TolQ-interacting domain by genetic suppression. J. Bacteriol. 180:6433-6439.
    • (1998) J. Bacteriol. , vol.180 , pp. 6433-6439
    • Germon, P.1    Clavel, T.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 72
    • 0346334403 scopus 로고    scopus 로고
    • Evidence for dynamic clustering of carboxyterminal aromatic amino acids in TonB-dependent energy transduction
    • Ghosh J, Postle K. 2004. Evidence for dynamic clustering of carboxyterminal aromatic amino acids in TonB-dependent energy transduction. Mol. Microbiol. 51:203-213.
    • (2004) Mol. Microbiol. , vol.51 , pp. 203-213
    • Ghosh, J.1    Postle, K.2
  • 73
    • 79952158450 scopus 로고    scopus 로고
    • The TonB dimeric crystal structures do not exist in vivo
    • doi:10.1128/mBio.00307-10
    • Postle K, Kastead KA, Gresock MG, Ghosh J, Swayne CD. 2010. The TonB dimeric crystal structures do not exist in vivo. mBio 1(5):e00307-10. doi:10.1128/mBio.00307-10.
    • (2010) mBio , vol.1 , Issue.5
    • Postle, K.1    Kastead, K.A.2    Gresock, M.G.3    Ghosh, J.4    Swayne, C.D.5
  • 74
    • 33646775316 scopus 로고    scopus 로고
    • Escherichia coli TolA tolerates multiple amino-acid substitutions as revealed by screening randomized variants for membrane integrity and phage receptor function
    • Karlsson F, Malmborg-Hager AC, Borrebaeck CA. 2006. Escherichia coli TolA tolerates multiple amino-acid substitutions as revealed by screening randomized variants for membrane integrity and phage receptor function. FEMS Microbiol. Lett. 259:81-88.
    • (2006) FEMS Microbiol. Lett. , vol.259 , pp. 81-88
    • Karlsson, F.1    Malmborg-Hager, A.C.2    Borrebaeck, C.A.3
  • 75
    • 0024592528 scopus 로고
    • Localization and assembly into the Escherichia coli envelope of a protein required for entry of colicin A
    • Bourdineaud J-P, Howard SP, Lazdunski C. 1989. Localization and assembly into the Escherichia coli envelope of a protein required for entry of colicin A. J. Bacteriol. 171:2458-2465.
    • (1989) J. Bacteriol. , vol.171 , pp. 2458-2465
    • Bourdineaud, J.-P.1    Howard, S.P.2    Lazdunski, C.3
  • 76
    • 0027280517 scopus 로고
    • The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
    • Bradbeer C. 1993. The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli. J. Bacteriol. 175:3146-3150.
    • (1993) J. Bacteriol. , vol.175 , pp. 3146-3150
    • Bradbeer, C.1
  • 77
    • 3142688448 scopus 로고    scopus 로고
    • Three paradoxes of ferric enterobactin uptake
    • Klebba PE. 2003. Three paradoxes of ferric enterobactin uptake. Front. Biosci. 8:s1422-s1436.
    • (2003) Front. Biosci. , vol.8
    • Klebba, P.E.1
  • 78
    • 34347374753 scopus 로고    scopus 로고
    • Energy transfer between biological membranes
    • Braun V. 2006. Energy transfer between biological membranes. ACS Chem. Biol. 1:352-354.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 352-354
    • Braun, V.1
  • 79
    • 0028280919 scopus 로고
    • Role of the TonB amino terminus in energy transduction between membranes
    • Jaskula JC, Letain TE, Roof SK, Skare JT, 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
  • 80
    • 84855824413 scopus 로고    scopus 로고
    • The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers
    • Ollis AA, Postle K. 2011. The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers. J. Bacteriol. 193:6852-6863.
    • (2011) J. Bacteriol. , vol.193 , pp. 6852-6863
    • Ollis, A.A.1    Postle, K.2
  • 81
    • 84864021815 scopus 로고    scopus 로고
    • Identification of functionally important TonBExbD periplasmic domain interactions in vivo
    • Ollis AA, Postle K. 2012. Identification of functionally important TonBExbD periplasmic domain interactions in vivo. J. Bacteriol. 194:3078-3087.
    • (2012) J. Bacteriol. , vol.194 , pp. 3078-3087
    • Ollis, A.A.1    Postle, K.2
  • 82
    • 0025666854 scopus 로고
    • TonB and the gram-negative dilemma
    • Postle K. 1990. TonB and the gram-negative dilemma. Mol. Microbiol. 4:2019-2025. 83. Skare JT, Postl e K. 1991. Evidence for a TonB-dependent energy transduction complex in Escherichia coli. Mol. Microbiol. 5:2883-2890.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 83
    • 0026344184 scopus 로고
    • Evidence for a TonB-dependent energy transduction complex in Escherichia coli
    • Skare JT, Postle K. 1991. Evidence for a TonB-dependent energy transduction complex in Escherichia coli. Mol. Microbiol. 5:2883-2890.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2883-2890
    • Skare, J.T.1    Postle, K.2
  • 84
    • 0022577734 scopus 로고
    • Reduced activity of TonB-dependent functions in strains of Escherichia coli
    • Mann BJ, Holroyd CD, Bradbeer C, Kadner RJ. 1986. Reduced activity of TonB-dependent functions in strains of Escherichia coli. FEMS Lett. 33:255-260.
    • (1986) FEMS Lett. , vol.33 , pp. 255-260
    • Mann, B.J.1    Holroyd, C.D.2    Bradbeer, C.3    Kadner, R.J.4
  • 85
    • 0024413265 scopus 로고
    • A mutation in the amino terminus of a hybrid TrpC-TonB protein relieves overproduction lethality and results in cytoplasmic accumulation
    • Skare JT, Roof SK, Postle K. 1989. A mutation in the amino terminus of a hybrid TrpC-TonB protein relieves overproduction lethality and results in cytoplasmic accumulation. J. Bacteriol. 171:4442-4447.
    • (1989) J. Bacteriol. , vol.171 , pp. 4442-4447
    • Skare, J.T.1    Roof, S.K.2    Postle, K.3
  • 86
    • 84867374260 scopus 로고    scopus 로고
    • Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance
    • Hobbs EC, Yin X, Paul BJ, Astarita JL, Storz G. 2012. Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance. Proc. Natl. Acad. Sci. U. S. A. 109:16696-16701.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16696-16701
    • Hobbs, E.C.1    Yin, X.2    Paul, B.J.3    Astarita, J.L.4    Storz, G.5
  • 87
    • 63249134496 scopus 로고    scopus 로고
    • Mapping the interactions between Escherichia coli Tol subunits: rotation of the TolR transmembrane helix
    • Zhang XY, Goemaere EL, Thome R, Gavioli M, Cascales E, Lloubes R. 2009. Mapping the interactions between Escherichia coli Tol subunits: rotation of the TolR transmembrane helix. J. Biol. Chem. 284:4275-4282.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4275-4282
    • Zhang, X.Y.1    Goemaere, E.L.2    Thome, R.3    Gavioli, M.4    Cascales, E.5    Lloubes, R.6
  • 89
    • 0019639160 scopus 로고
    • Inversions between ribosomal RNA genes of Escherichia coli
    • Hill CW, Harnish BW. 1981. Inversions between ribosomal RNA genes of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 78:7069-7072.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 7069-7072
    • Hill, C.W.1    Harnish, B.W.2
  • 90
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 91
    • 84864020106 scopus 로고    scopus 로고
    • The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization
    • Ollis AA, Kumar A, Postle K. 2012. The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization. J. Bacteriol. 194:3069-3077.
    • (2012) J. Bacteriol. , vol.194 , pp. 3069-3077
    • Ollis, A.A.1    Kumar, A.2    Postle, K.3
  • 92
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima S, Blair DF. 2001. Conformational change in the stator of the bacterial flagellar motor. Biochemistry 40:13041-13050.
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2


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