메뉴 건너뛰기




Volumn 1861, Issue 11, 2017, Pages 2702-2709

Biophysical characterization of E. coli TolC interaction with the known blocker hexaamminecobalt

Author keywords

Electrophysiology; Hexaamminecobalt; Surface plasmon resonance; TolC

Indexed keywords

CATION; ERYTHROMYCIN; FUSIDIC ACID; HEXAAMMINECOBALT; TOLC PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; COBALT; ESCHERICHIA COLI PROTEIN; HEXAAMMINECOBALT(II); OUTER MEMBRANE PROTEIN; TOLC PROTEIN, E COLI;

EID: 85026390639     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2017.07.014     Document Type: Article
Times cited : (9)

References (36)
  • 3
    • 84926035587 scopus 로고    scopus 로고
    • The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria
    • Li, X.Z., Plésiat, P., Nikaido, H., The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria. Clin. Microbiol. Rev. 28 (2015), 337–418, 10.1128/CMR.00117-14.
    • (2015) Clin. Microbiol. Rev. , vol.28 , pp. 337-418
    • Li, X.Z.1    Plésiat, P.2    Nikaido, H.3
  • 4
    • 84908457716 scopus 로고    scopus 로고
    • Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations
    • Sun, J., Deng, Z., Yan, A., Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations. Biochem. Biophys. Res. Commun. 453 (2014), 254–267, 10.1016/j.bbrc.2014.05.090.
    • (2014) Biochem. Biophys. Res. Commun. , vol.453 , pp. 254-267
    • Sun, J.1    Deng, Z.2    Yan, A.3
  • 5
    • 84924150331 scopus 로고    scopus 로고
    • Homologs of the Acinetobacter baumannii AceI transporter represent a new family of bacterial multidrug efflux systems
    • Hassan, K.A., Liu, Q., Henderson, P.J.F., Paulsen, I.T., Homologs of the Acinetobacter baumannii AceI transporter represent a new family of bacterial multidrug efflux systems. MBio 6 (2015), e01982–14, 10.1128/mBio.01982-14.
    • (2015) MBio , vol.6 , pp. e01982-14
    • Hassan, K.A.1    Liu, Q.2    Henderson, P.J.F.3    Paulsen, I.T.4
  • 6
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng, T.T., Gratwick, K.S., Kollman, J., Park, D., Nies, D.H., Goffeau, A., Saier, M.H., The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1 (1999), 107–125.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 107-125
    • Tseng, T.T.1    Gratwick, K.S.2    Kollman, J.3    Park, D.4    Nies, D.H.5    Goffeau, A.6    Saier, M.H.7
  • 7
    • 58749106615 scopus 로고    scopus 로고
    • Gating at both ends and breathing in the middle: conformational dynamics of TolC
    • Vaccaro, L., Scott, K.A., Sansom, M.S.P., Gating at both ends and breathing in the middle: conformational dynamics of TolC. Biophys. J. 95 (2008), 5681–5691, 10.1529/biophysj.108.136028.
    • (2008) Biophys. J. , vol.95 , pp. 5681-5691
    • Vaccaro, L.1    Scott, K.A.2    Sansom, M.S.P.3
  • 8
    • 84938946273 scopus 로고    scopus 로고
    • The assembly and disassembly of the AcrAB-TolC three-component multidrug efflux pump
    • Muller, R.T., Pos, K.M., The assembly and disassembly of the AcrAB-TolC three-component multidrug efflux pump. Biol. Chem. 396 (2015), 1083–1089, 10.1515/hsz-2015-0150.
    • (2015) Biol. Chem. , vol.396 , pp. 1083-1089
    • Muller, R.T.1    Pos, K.M.2
  • 10
    • 84937637657 scopus 로고    scopus 로고
    • Assembly and operation of bacterial tripartite multidrug efflux pumps
    • Du, D., van Veen, H.W., Luisi, B.F., Assembly and operation of bacterial tripartite multidrug efflux pumps. Trends Microbiol., 2015, 1–9, 10.1016/j.tim.2015.01.010.
    • (2015) Trends Microbiol. , pp. 1-9
    • Du, D.1    van Veen, H.W.2    Luisi, B.F.3
  • 11
    • 67649415188 scopus 로고    scopus 로고
    • The C-terminal domain of AcrA is essential for the assembly and function of the multidrug efflux pump AcrAB-TolC
    • Ge, Q., Yamadah, Y., Zgurskaya, E., The C-terminal domain of AcrA is essential for the assembly and function of the multidrug efflux pump AcrAB-TolC. J. Bacteriol. 191 (2009), 4365–4371, 10.1128/JB.00204-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 4365-4371
    • Ge, Q.1    Yamadah, Y.2    Zgurskaya, E.3
  • 13
    • 0020679399 scopus 로고
    • Identification and characterization of the ToIC protein, an outer membrane protein from Escherichia coli
    • Morona, R., Manning, P.A., Reeves, P., Identification and characterization of the ToIC protein, an outer membrane protein from Escherichia coli. J. Bacteriol. 153 (1983), 693–699.
    • (1983) J. Bacteriol. , vol.153 , pp. 693-699
    • Morona, R.1    Manning, P.A.2    Reeves, P.3
  • 14
    • 0031278034 scopus 로고    scopus 로고
    • A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria
    • Paulsen, I.T., Park, J.H., Choi, P.S., Saier, M.H., A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria. FEMS Microbiol. Lett. 156 (2006), 1–8, 10.1111/j.1574-6968.1997.tb12697.x.
    • (2006) FEMS Microbiol. Lett. , vol.156 , pp. 1-8
    • Paulsen, I.T.1    Park, J.H.2    Choi, P.S.3    Saier, M.H.4
  • 15
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals
    • Koronakis, V., Li, J., Koronakis, E., Stauffer, K., Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals. Mol. Microbiol. 23 (1997), 617–626, 10.1046/j.1365-2958.1997.d01-1880.x.
    • (1997) Mol. Microbiol. , vol.23 , pp. 617-626
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 16
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., Hughes, C., Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 (2000), 914–919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 18
    • 84954305043 scopus 로고    scopus 로고
    • Pseudoatomic structure of the tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and TolC
    • Jeong, H., Kim, J.S., Song, S., Shigematsu, H., Yokoyama, T., Hyun, J., Ha, N.C., Pseudoatomic structure of the tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and TolC. Structure 24 (2016), 272–276, 10.1016/j.str.2015.12.007.
    • (2016) Structure , vol.24 , pp. 272-276
    • Jeong, H.1    Kim, J.S.2    Song, S.3    Shigematsu, H.4    Yokoyama, T.5    Hyun, J.6    Ha, N.C.7
  • 21
    • 0036147130 scopus 로고    scopus 로고
    • Electrophysiological behavior of the TolC channel-tunnel in planar lipid bilayers
    • Andersen, C., Hughes, C., Koronakis, V., Electrophysiological behavior of the TolC channel-tunnel in planar lipid bilayers. J. Membr. Biol. 185 (2002), 83–92, 10.1007/s00232-001-0113-2.
    • (2002) J. Membr. Biol. , vol.185 , pp. 83-92
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 22
    • 0036015627 scopus 로고    scopus 로고
    • An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations
    • Andersen, C., Koronakis, E., Hughes, C., Koronakis, V., An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations. Mol. Microbiol. 44 (2002), 1131–1139, 10.1046/j.1365-2958.2002.02898.x.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1131-1139
    • Andersen, C.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 24
    • 4444252811 scopus 로고    scopus 로고
    • Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC
    • Higgins, M.K., Eswaran, J., Edwards, P., Schertler, G.F.X., Hughes, C., Koronakis, V., Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC. J. Mol. Biol. 342 (2004), 697–702, 10.1016/j.jmb.2004.07.088.
    • (2004) J. Mol. Biol. , vol.342 , pp. 697-702
    • Higgins, M.K.1    Eswaran, J.2    Edwards, P.3    Schertler, G.F.X.4    Hughes, C.5    Koronakis, V.6
  • 25
    • 0036794301 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein
    • Pos, K.M., Diederichs, K., Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein. Acta Crystallogr. Sect. D Biol. Crystallogr. 58 (2002), 1865–1867, 10.1107/S0907444902013963.
    • (2002) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.58 , pp. 1865-1867
    • Pos, K.M.1    Diederichs, K.2
  • 26
    • 0000559465 scopus 로고
    • Reconstitution of cell membrane structure in vitro and its transformation into an excitable system
    • Mueller, P., Rudin, D.O., Ti Tien, H., Wescott, W.C., Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature 194 (1962), 979–980, 10.1038/194979a0.
    • (1962) Nature , vol.194 , pp. 979-980
    • Mueller, P.1    Rudin, D.O.2    Ti Tien, H.3    Wescott, W.C.4
  • 27
    • 84944089183 scopus 로고    scopus 로고
    • VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore
    • Okazaki, M., Kurabayashi, K., Asanuma, M., Saito, Y., Dodo, K., Sodeoka, M., VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore. Biochim. Biophys. Acta Biomembr. 1848 (2015), 3188–3196, 10.1016/j.bbamem.2015.09.017.
    • (2015) Biochim. Biophys. Acta Biomembr. , vol.1848 , pp. 3188-3196
    • Okazaki, M.1    Kurabayashi, K.2    Asanuma, M.3    Saito, Y.4    Dodo, K.5    Sodeoka, M.6
  • 28
    • 0038637764 scopus 로고    scopus 로고
    • On translocation through a membrane channel via an internal binding site: kinetics and voltage dependence
    • Schwarz, G., Danelon, C., Winterhalter, M., On translocation through a membrane channel via an internal binding site: kinetics and voltage dependence. Biophys. J. 84 (2003), 2990–2998, 10.1016/S0006-3495(03)70025-3.
    • (2003) Biophys. J. , vol.84 , pp. 2990-2998
    • Schwarz, G.1    Danelon, C.2    Winterhalter, M.3
  • 29
    • 84963756754 scopus 로고    scopus 로고
    • Role of electroosmosis in the permeation of neutral molecules: CymA and cyclodextrin as an example
    • Bhamidimarri, S.P., Prajapati, J.D., van den Berg, B., Winterhalter, M., Kleinekathöfer, U., Role of electroosmosis in the permeation of neutral molecules: CymA and cyclodextrin as an example. Biophys. J. 110 (2016), 600–611, 10.1016/j.bpj.2015.12.027.
    • (2016) Biophys. J. , vol.110 , pp. 600-611
    • Bhamidimarri, S.P.1    Prajapati, J.D.2    van den Berg, B.3    Winterhalter, M.4    Kleinekathöfer, U.5
  • 30
    • 84954287070 scopus 로고    scopus 로고
    • Methods for in vitro evaluating antimicrobial activity: a review
    • Balouiri, M., Sadiki, M., Ibnsouda, S.K., Methods for in vitro evaluating antimicrobial activity: a review. J. Pharm. Anal. 6 (2015), 71–79, 10.1016/j.jpha.2015.11.005.
    • (2015) J. Pharm. Anal. , vol.6 , pp. 71-79
    • Balouiri, M.1    Sadiki, M.2    Ibnsouda, S.K.3
  • 31
    • 0026588343 scopus 로고
    • Active efflux mechanisms for antimicrobial resistance
    • Levy, S.B., Active efflux mechanisms for antimicrobial resistance. Antimicrob. Agents Chemother. 36 (1992), 695–703.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 695-703
    • Levy, S.B.1
  • 33
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: the bacterial exit duct for proteins and drugs
    • Koronakis, V., Eswaran, J., Hughes, C., Structure and function of TolC: the bacterial exit duct for proteins and drugs. Annu. Rev. Biochem. 73 (2004), 467–489, 10.1146/annurev.biochem.73.011303.074104.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 34
    • 0032535149 scopus 로고    scopus 로고
    • Equilibrium analysis of high affinity interactions using BIACORE
    • Myszka, D.G., Jonsen, M.D., Graves, B.J., Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 265 (1998), 326–330, 10.1006/abio.1998.2937.
    • (1998) Anal. Biochem. , vol.265 , pp. 326-330
    • Myszka, D.G.1    Jonsen, M.D.2    Graves, B.J.3
  • 35
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido, H., Multidrug efflux pumps of gram-negative bacteria. J. Bacteriol. 178 (1996), 5853–5859.
    • (1996) J. Bacteriol. , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 36
    • 84874217352 scopus 로고    scopus 로고
    • On the role of TolC in multidrug efflux: the function and assembly of AcrAB-TolC tolerate significant depletion of intracellular TolC protein
    • Krishnamoorthy, G., Tikhonova, E.B., Dhamdhere, G., Zgurskaya, H.I., On the role of TolC in multidrug efflux: the function and assembly of AcrAB-TolC tolerate significant depletion of intracellular TolC protein. Mol. Microbiol. 87 (2013), 982–997, 10.1111/mmi.12143.
    • (2013) Mol. Microbiol. , vol.87 , pp. 982-997
    • Krishnamoorthy, G.1    Tikhonova, E.B.2    Dhamdhere, G.3    Zgurskaya, H.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.