메뉴 건너뛰기




Volumn 394, Issue 11, 2013, Pages 1371-1384

Molecular insights into type i secretion systems

Author keywords

ATP binding cassette (ABC) transporter; ATPase; Haemolysin A; Membrane fusion protein; Outer membrane protein; Type 1 secretion

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; AMINO ACID; CARRIER PROTEIN; FATTY ACID BINDING PROTEIN 2; HEMOLYSIN; MACROLIDE; MALTOSE BINDING PROTEIN; MEMBRANE FUSION PROTEIN; MONOMER; OUTER MEMBRANE PROTEIN; TRANSLOCON;

EID: 84888089248     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0171     Document Type: Review
Times cited : (22)

References (115)
  • 1
    • 11144222920 scopus 로고    scopus 로고
    • Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: Dual modes of membrane anchoring and occluded cavity end
    • DOI 10.1074/jbc.C400445200
    • Akama, H., Kanemaki, M., Yoshimura, M., Tsukihara, T., Kashiwagi, T., Yoneyama, H., Narita, S., Nakagawa, A., and Nakae, T. (2004a). Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 279, 52816-52819. (Pubitemid 40051780)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 52816-52819
    • Akama, H.1    Kanemaki, M.2    Yoshimura, M.3    Tsukihara, T.4    Kashiwagi, T.5    Yoneyama, H.6    Narita, S.-I.7    Nakagawa, A.8    Nakae, T.9
  • 3
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G.F., Mimura, C.S., Holbrook, S.R., and Shyamala, V. (1992). Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. Relat. Areas. Mol. Biol. 65, 1-47.
    • (1992) Adv. Enzymol. Relat. Areas. Mol. Biol , vol.65 , pp. 1-47
    • Ames, G.F.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 5
    • 78650363963 scopus 로고    scopus 로고
    • The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system
    • Bakkes, P.J., Jenewein, S., Smits, S.H., Holland, I.B., and Schmitt, L. (2010). The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system. J. Biol. Chem. 285, 40573-40580.
    • (2010) J. Biol. Chem , vol.285 , pp. 40573-40580
    • Bakkes, P.J.1    Jenewein, S.2    Smits, S.H.3    Holland, I.B.4    Schmitt, L.5
  • 6
    • 0035955547 scopus 로고    scopus 로고
    • Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli
    • DOI 10.1006/jmbi.2001.5038
    • Balakrishnan, L., Hughes, C., and Koronakis, V. (2001). Substratetriggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli. J. Mol. Bol. 313, 501-510. (Pubitemid 33052283)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.3 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3
  • 8
    • 0344405700 scopus 로고    scopus 로고
    • A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A
    • DOI 10.1016/S0022-2836(03)00204-3
    • Benabdelhak, H., Kiontke, S., Horn, C., Ernst, R., Blight, M.A., Holland, I.B., and Schmitt, L. (2003). A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A. J. Mol. Biol. 327, 1169-1179. (Pubitemid 36363721)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.5 , pp. 1169-1179
    • Benabdelhak, H.1    Kiontke, S.2    Horn, C.3    Ernst, R.4    Blight, M.A.5    Holland, I.B.6    Schmitt, L.7
  • 9
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: Specific functions of the membrane ATPase and the membrane fusion protein
    • Binet, R. and Wandersman, C. (1995). Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein. EMBO J. 14, 2298-2306.
    • (1995) EMBO J , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 10
    • 0028533504 scopus 로고
    • Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator
    • DOI 10.1016/0167-7799(94)90020-5
    • Blight, M.A. and Holland, I.B. (1994). Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator. Trends. Biotechnol. 12, 450-455. (Pubitemid 24327510)
    • (1994) Trends in Biotechnology , vol.12 , Issue.11 , pp. 450-455
    • Blight, M.A.1    Barry Holland, I.2
  • 11
    • 33947422975 scopus 로고    scopus 로고
    • Probing the in vivo dynamics of type I protein secretion complex association through sensitivity to detergents
    • DOI 10.1128/JB.01480-06
    • Cescau, S., Debarbieux, L., and Wandersman, C. (2007). Probing the in vivo dynamics of type I protein secretion complex association through sensitivity to detergents. bacteriology Bacteriol. 189, 1496-1504. (Pubitemid 46446110)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1496-1504
    • Cescau, S.1    Debarbieux, L.2    Wandersman, C.3
  • 12
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • DOI 10.1016/j.molcel.2003.08.004
    • Chen, J., Lu, G., Lin, J., Davidson, A.L., and Quiocho, F.A. (2003). A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 651-661. (Pubitemid 37222486)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 13
    • 8544269408 scopus 로고    scopus 로고
    • Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
    • DOI 10.1074/jbc.M404042200
    • Chen, M., Abele, R., and Tampe, R. (2004). Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP). J. Biol. Chem. 279, 46073-46081. (Pubitemid 39491601)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 46073-46081
    • Chen, M.1    Abele, R.2    Tampe, R.3
  • 14
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of Helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin
    • Chervaux, C. and Holland, I.B. (1996). Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin. J. Bacteriol. 178, 1232-1236. (Pubitemid 26048049)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 15
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • DOI 10.1128/MMBR.00031-07
    • Davidson, A.L., Dassa, E., Orelle, C., and Chen, J. (2008). Structure, function, and evolution of bacterial ATP-binding cassette systems. MMBR 72, 317-364. (Pubitemid 351822295)
    • (2008) Microbiology and Molecular Biology Reviews , vol.72 , Issue.2 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 16
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • DOI 10.1038/nature05155, PII NATURE05155
    • Dawson, R.J. and Locher, K.P. (2006). Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185. (Pubitemid 44387602)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 17
    • 0035801397 scopus 로고    scopus 로고
    • Folded HasA inhibits its own secretion through its ABC exporter
    • DOI 10.1093/emboj/20.17.4657
    • Debarbieux, L. and Wandersman, C. (2001). Folded HasA inhibits its own secretion through its ABC exporter. EMBO J. 20, 4657-4663. (Pubitemid 32848619)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4657-4663
    • Debarbieux, L.1    Wandersman, C.2
  • 18
    • 0028051797 scopus 로고
    • PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signalregulated ATPase activity
    • Delepelaire, P. (1994). PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signalregulated ATPase activity. J. Biol. Chem. 269, 27952-27957.
    • (1994) J. Biol. Chem , vol.269 , pp. 27952-27957
    • Delepelaire, P.1
  • 19
    • 8844241421 scopus 로고    scopus 로고
    • Type I secretion in gram-negative bacteria
    • DOI 10.1016/j.bbamcr.2004.05.001, PII S0167488904001168
    • Delepelaire, P. (2004). Type I secretion in gram-negative bacteria. Biochim. Biophys. Acta. 1694, 149-161. (Pubitemid 39535067)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1694 , Issue.SPEC.ISS. , pp. 149-161
    • Delepelaire, P.1
  • 20
    • 0032481311 scopus 로고    scopus 로고
    • The SecB chaperone is involved in the secretion of the serratia marcescens HasA protein through an ABC transporter
    • DOI 10.1093/emboj/17.4.936
    • Delepelaire, P. and Wandersman, C. (1998). The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. EMBO J. 17, 936-944. (Pubitemid 28077648)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 936-944
    • Delepelaire, P.1    Wandersman, C.2
  • 21
    • 27944436251 scopus 로고    scopus 로고
    • Protein export and secretion in Gram-negative bacteria
    • G. Winkelmann, ed. (Weinheim: Wiley VCH Verlag GmbH & Co. KGaA)
    • Delepelaire, P. and Wandersman, C. (2003). Protein export and secretion in Gram-negative bacteria. In: Microbial Transport Systems, G. Winkelmann, ed. (Weinheim: Wiley-VCH Verlag GmbH & Co. KGaA), pp. 165-208.
    • (2003) Microbial Transport Systems , pp. 165-208
    • Delepelaire, P.1    Wandersman, C.2
  • 22
    • 0037459244 scopus 로고    scopus 로고
    • Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus
    • DOI 10.1016/S0022-2836(03)00116-5
    • Eswaran, J., Hughes, C., and Koronakis, V. (2003). Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus. J. Mol. Biol. 327, 309-315. (Pubitemid 36298702)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.2 , pp. 309-315
    • Eswaran, J.1    Hughes, C.2    Koronakis, V.3
  • 23
    • 0031919405 scopus 로고    scopus 로고
    • Characterization of Rhizobium leguminosarum exopolysaccharide glycanases that are secreted via a type I exporter and have a novel heptapeptide repeat motif
    • Finnie, C., Zorreguieta, A., Hartley, N.M., and Downie, J.A. (1998). Characterization of Rhizobium leguminosarum exopolysaccharide glycanases that are secreted via a type I exporter and have a novel heptapeptide repeat motif. J. Bacteriol. 180, 1691-1699. (Pubitemid 28173046)
    • (1998) Journal of Bacteriology , vol.180 , Issue.7 , pp. 1691-1699
    • Finnie, C.1    Zorreguieta, A.2    Hartley, N.M.3    Downie, J.A.4
  • 24
    • 0023656068 scopus 로고
    • Maintenance of intracellular calcium in Escherichia coli
    • Gangola, P. and Rosen, B.P. (1987). Maintenance of intracellular calcium in Escherichia coli. J. Biol. Chem. 262, 12570-12574.
    • (1987) J. Biol. Chem , vol.262 , pp. 12570-12574
    • Gangola, P.1    Rosen, B.P.2
  • 25
    • 0036149305 scopus 로고    scopus 로고
    • The E coli α-hemolysin secretion system and its use in vaccine development
    • DOI 10.1016/S0966-842X(01)02259-4, PII S0966842X01022594
    • Gentschev, I., Dietrich, G., and Goebel, W. (2002). The E. coli alpha-hemolysin secretion system and its use in vaccine development. Trends. Microbiol. 10, 39-45. (Pubitemid 34075263)
    • (2002) Trends in Microbiology , vol.10 , Issue.1 , pp. 39-45
    • Gentschev, I.1    Dietrich, G.2    Goebel, W.3
  • 27
    • 0022800438 scopus 로고
    • The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli
    • Gray, L., Mackman, N., Nicaud, J.M., and Holland, I.B. (1986). The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli. Mol. Gen. Genet. 205, 127-133.
    • (1986) Mol. Gen. Genet , vol.205 , pp. 127-133
    • Gray, L.1    Mackman, N.2    Nicaud, J.M.3    Holland, I.B.4
  • 28
    • 0026621245 scopus 로고
    • ABC Transporters: From microorganisms to man
    • Higgins, C.F. (1992). ABC transporters: from microorganisms to man. Ann. Rev. Cell Biol. 8, 67-113. (Pubitemid 23000992)
    • (1992) Annual Review of Cell Biology , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 30
    • 0042065283 scopus 로고    scopus 로고
    • Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein
    • DOI 10.1046/j.1365-2958.2003.03615.x
    • Hinsa, S.M., Espinosa-Urgel, M., Ramos, J.L., and O'Toole, G.A. (2003). Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol. Microbiol. 49, 905-918. (Pubitemid 36981338)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 905-918
    • Hinsa, S.M.1    Espinosa-Urgel, M.2    Ramos, J.L.3    O'Toole, G.A.4
  • 31
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway
    • DOI 10.1080/09687860500042013
    • Holland, I.B., Schmitt, L., and Young, J. (2005). Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review). Mol. Membr. Biol. 22, 29-39. (Pubitemid 40692152)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.1-2 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 32
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • DOI 10.1038/nature05626, PII NATURE05626
    • Hollenstein, K., Frei, D.C., and Locher, K.P. (2007). Structure of an ABC transporter in complex with its binding protein. Nature 446, 213-216. (Pubitemid 46398672)
    • (2007) Nature , vol.446 , Issue.7132 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 33
    • 0037197670 scopus 로고    scopus 로고
    • A combinatorial approach toward analyzing functional elements of the Escherichia coli hemolysin signal sequence
    • DOI 10.1021/bi011425g
    • Hui, D. and Ling, V. (2002). A combinatorial approach toward analyzing functional elements of the Escherichia coli hemolysin signal sequence. Biochem 41, 5333-5339. (Pubitemid 34429367)
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5333-5339
    • Hui, D.1    Ling, V.2
  • 34
    • 0034723207 scopus 로고    scopus 로고
    • Combinatorial analysis of the structural requirements of the Escherichia coli hemolysin signal sequence
    • DOI 10.1074/jbc.275.4.2713
    • Hui, D., Morden, C., Zhang, F., and Ling, V. (2000). Combinatorial analysis of the structural requirements of the Escherichia coli hemolysin signal sequence. J. Biol. Chem. 275, 2713-2720. (Pubitemid 30082041)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2713-2720
    • Hui, D.1    Morden, C.2    Zhang, F.3    Ling, V.4
  • 35
    • 0032866569 scopus 로고    scopus 로고
    • Mutational analysis of CvaA in the highly conserved domain of the membrane fusion protein family
    • DOI 10.1007/s002849900444
    • Hwang, J. and Tai, P.C. (1999). Mutational analysis of CvaA in the highly conserved domain of the membrane fusion protein family. Curr. Microbiol. 39, 195-199. (Pubitemid 29468057)
    • (1999) Current Microbiology , vol.39 , Issue.4 , pp. 195-199
    • Hwang, J.1    Tai, P.C.2
  • 36
    • 77951235672 scopus 로고    scopus 로고
    • Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway
    • Ishii, S., Yano, T., Ebihara, A., Okamoto, A., Manzoku, M., and Hayashi, H. (2010). Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway. J. Biol. Chem. 285, 10777-10785.
    • (2010) J. Biol. Chem , vol.285 , pp. 10777-10785
    • Ishii, S.1    Yano, T.2    Ebihara, A.3    Okamoto, A.4    Manzoku, M.5    Hayashi, H.6
  • 37
    • 0028019381 scopus 로고
    • Selection for transport competence of C-terminal polypeptides derived from Escherichia coli hemolysin: The shortest peptide capable of autonomous HlyB/HlyD-dependent secretion comprises the C-terminal 62 amino acids of HlyA
    • DOI 10.1007/BF00279750
    • Jarchau, T., Chakraborty, T., Garcia, F., and Goebel, W. (1994). Selection for transport competence of C-terminal polypeptides derived from Escherichia coli hemolysin: the shortest peptide capable of autonomous HlyB/HlyD-dependent secretion comprises the C-terminal 62 amino acids of HlyA. Mol. Gen. Genet. 245, 53-60. (Pubitemid 24353689)
    • (1994) Molecular and General Genetics , vol.245 , Issue.1 , pp. 53-60
    • Jarchau, T.1    Chakraborty, T.2    Garcia, F.3    Goebel, W.4
  • 38
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • DOI 10.1006/jmbi.1999.2630
    • Johnson, J.M. and Church, G.M. (1999). Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J. Mol. Biol. 287, 695-715. (Pubitemid 29168442)
    • (1999) Journal of Molecular Biology , vol.287 , Issue.3 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 39
    • 0033105139 scopus 로고    scopus 로고
    • 2+ in Escherichia coli highlight two putative influx mechanisms in response to changes in extracellular calcium
    • 2+ in Escherichia coli highlight two putative influx mechanisms in response to changes in extracellular calcium. Cell Calcium 25, 265-274.
    • (1999) Cell Calcium , vol.25 , pp. 265-274
    • Jones, H.E.1    Holland, I.B.2    Baker, H.L.3    Campbell, A.K.4
  • 40
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • DOI 10.1016/S0378-1097(99)00411-5, PII S0378109799004115
    • Jones, P.M. and George, A.M. (1999). Subunit interactions in ABC transporters: towards a functional architecture. FEMS Micriobiol. Lett. 179, 187-202. (Pubitemid 29460678)
    • (1999) FEMS Microbiology Letters , vol.179 , Issue.2 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 41
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. Coli methionine ABC transporter: Structure and allosteric regulation
    • DOI 10.1126/science.1157987
    • Kadaba, N.S., Kaiser, J.T., Johnson, E., Lee, A., and Rees, D.C. (2008). The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321, 250-253. (Pubitemid 351989096)
    • (2008) Science , vol.321 , Issue.5886 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 42
    • 0028308070 scopus 로고
    • Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator
    • DOI 10.1111/j.1365-2958.1994.tb00293.x
    • Kenny, B., Chervaux, C., and Holland, I.B. (1994). Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator. Mol. Microbiol. 11, 99-109. (Pubitemid 24205445)
    • (1994) Molecular Microbiology , vol.11 , Issue.1 , pp. 99-109
    • Kenny, B.1    Chervaux, C.2    Holland, I.B.3
  • 43
    • 0026095620 scopus 로고
    • Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or β-galactosidase fused to the Hly C-terminal signal domain
    • Kenny, B., Haigh, R., and Holland, I.B. (1991). Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or beta-galactosidase fused to the Hly C-terminal signal domain. Mol. Microbiol. 5, 2557-2568. (Pubitemid 21895987)
    • (1991) Molecular Microbiology , vol.5 , Issue.10 , pp. 2557-2568
    • Kenny, B.1    Haigh, R.2    Holland, I.B.3
  • 44
    • 0037133735 scopus 로고    scopus 로고
    • Structure and association of ATP-binding cassette transporter nucleotide-binding domains
    • DOI 10.1016/S0304-4157(01)00008-9, PII S0304415701000089
    • Kerr, I.D. (2002). Structure and association of ATP-binding cassette transporter nucleotide-binding domains. Biochim. Biophys. Acta 1561, 47-64. (Pubitemid 34442244)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1561 , Issue.1 , pp. 47-64
    • Kerr, I.D.1
  • 45
    • 77956524004 scopus 로고    scopus 로고
    • Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC
    • Kim, H.M., Xu, Y., Lee, M., Piao, S., Sim, S.H., Ha, N.C., and Lee, K. (2010). Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC. J. Bacteriol. 192, 4498-4503.
    • (2010) J. Bacteriol , vol.192 , pp. 4498-4503
    • Kim, H.M.1    Xu, Y.2    Lee, M.3    Piao, S.4    Sim, S.H.5    Ha, N.C.6    Lee, K.7
  • 46
    • 0028915106 scopus 로고
    • Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • Koronakis, E., Hughes, C., Milisav, I., and Koronakis, V. (1995). Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB. Mol. Microbiol. 16, 87-96.
    • (1995) Mol. Microbiol , vol.16 , pp. 87-96
    • Koronakis, E.1    Hughes, C.2    Milisav, I.3    Koronakis, V.4
  • 47
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: The bacterial exit duct for proteins and drugs
    • DOI 10.1146/annurev.biochem.73.011303.074104
    • Koronakis, V., Eswaran, J., and Hughes, C. (2004). Structure and function of TolC: the bacterial exit duct for proteins and drugs. Ann. Rev. Biochem. 73, 467-489. (Pubitemid 39050377)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 48
    • 0025989941 scopus 로고
    • Energetically distinct early and late stages of HlyB/HlyD-dependent secretion across both Escherichia coli membranes
    • Koronakis, V., Hughes, C., and Koronakis, E. (1991). Energetically distinct early and late stages of HlyB/HlyD-dependent secretion across both Escherichia coli membranes. EMBO J. 10, 3263-3272. (Pubitemid 21905351)
    • (1991) EMBO Journal , vol.10 , Issue.11 , pp. 3263-3272
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 49
    • 0027190678 scopus 로고
    • ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HLyB
    • Koronakis, V., Hughes, C., and Koronakis, E. (1993). ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB. Mol. Microbiol. 8, 1163-1175. (Pubitemid 23187035)
    • (1993) Molecular Microbiology , vol.8 , Issue.6 , pp. 1163-1175
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 50
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • DOI 10.1038/35016007
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., and Hughes, C. (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405, 914-919. (Pubitemid 30435040)
    • (2000) Nature , vol.405 , Issue.6789 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 51
    • 84867404639 scopus 로고    scopus 로고
    • An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain
    • Lecher, J., Schwarz, C.K., Stoldt, M., Smits, S.H., Willbold, D., and Schmitt, L. (2012). An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain. Structure 20, 1778-1787.
    • (2012) Structure , vol.20 , pp. 1778-1787
    • Lecher, J.1    Schwarz, C.K.2    Stoldt, M.3    Smits, S.H.4    Willbold, D.5    Schmitt, L.6
  • 52
    • 84855370310 scopus 로고    scopus 로고
    • 1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB)
    • Lecher, J., Stoldt, M., Schwarz, C.K., Smits, S.H., Schmitt, L., and Willbold, D. (2011). 1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB). Biomol. NMR Assign. 5, 199-201.
    • (2011) Biomol. NMR Assign , vol.5 , pp. 199-201
    • Lecher, J.1    Stoldt, M.2    Schwarz, C.K.3    Smits, S.H.4    Schmitt, L.5    Willbold, D.6
  • 53
    • 84863712924 scopus 로고    scopus 로고
    • Membrane fusion proteins of type i secretion system and tripartite efflux pumps share a binding motif for TolC in gram-negative bacteria
    • Lee, M., Jun, S.Y., Yoon, B.Y., Song, S., Lee, K., and Ha, N.C. (2012). Membrane fusion proteins of type I secretion system and tripartite efflux pumps share a binding motif for TolC in gram-negative bacteria. PloS One 7, e40460.
    • (2012) PloS One , vol.7
    • Lee, M.1    Jun, S.Y.2    Yoon, B.Y.3    Song, S.4    Lee, K.5    Ha, N.C.6
  • 54
    • 0029908021 scopus 로고    scopus 로고
    • Protein secretion in Gram-negative bacteria: Assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding
    • Letoffe, S., Delepelaire, P., and Wandersman, C. (1996). Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J. 15, 5804-5811. (Pubitemid 26375502)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5804-5811
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 55
    • 0034908388 scopus 로고    scopus 로고
    • Haemophore-mediated bacterial haem transport: Evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor
    • DOI 10.1046/j.1365-2958.2001.02530.x
    • Letoffe, S., Deniau, C., Wolff, N., Dassa, E., Delepelaire, P., Lecroisey, A., and Wandersman, C. (2001). Haemophoremediated bacterial haem transport: evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor. Mol. Microbiol. 41, 439-450. (Pubitemid 32730542)
    • (2001) Molecular Microbiology , vol.41 , Issue.2 , pp. 439-450
    • Letoffe, S.1    Deniau, C.2    Wolff, N.3    Dassa, E.4    Delepelaire, P.5    Lecroisey, A.6    Wandersman, C.7
  • 56
    • 0028023120 scopus 로고
    • Secretion of the Serratia marcescens HasA protein by an ABC transporter
    • Letoffe, S., Ghigo, J.M., and Wandersman, C. (1994). Secretion of the Serratia marcescens HasA protein by an ABC transporter. J. Bacteriol. 176, 5372-5377. (Pubitemid 24273525)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5372-5377
    • Letoffe, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 59
    • 0037052565 scopus 로고    scopus 로고
    • The E. Coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • DOI 10.1126/science.1071142
    • Locher, K.P., Lee, A.T., and Rees, D.C. (2002). The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098. (Pubitemid 34517120)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 60
    • 84870240134 scopus 로고    scopus 로고
    • Role of ATP binding and hydrolysis in assembly of MacAB-TolC macrolide transporter
    • Lu, S., and Zgurskaya, H.I. (2012). Role of ATP binding and hydrolysis in assembly of MacAB-TolC macrolide transporter. Mol. Microbiol. 86, 1132-1143.
    • (2012) Mol. Microbiol , vol.86 , pp. 1132-1143
    • Lu, S.1    Zgurskaya, H.I.2
  • 61
    • 0002846942 scopus 로고    scopus 로고
    • The family of the multigenic encoded RTX toxin
    • J.E. Alouf, and J.H. Freer, eds. (Amsterdam: Academic Press)
    • Ludwig, A. and Goebel, W. (1999). The family of the multigenic encoded RTX toxin. In: The Comprehensive Sourcebook of Bacterial Protein Toxins, J.E. Alouf, and J.H. Freer, eds. (Amsterdam: Academic Press), pp. 330-348.
    • (1999) The Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 330-348
    • Ludwig, A.1    Goebel, W.2
  • 63
    • 0023411758 scopus 로고
    • Release of a chimeric protein into the medium from Escherichia coli using the C-terminal secretion signal of haemolysin
    • Mackman, N., Baker, K., Gray, L., Haigh, R., Nicaud, J.M., and Holland, I.B. (1987). Release of a chimeric protein into the medium from Escherichia coli using the C-terminal secretion signal of haemolysin. EMBO J. 6, 2835-2841.
    • (1987) EMBO J , vol.6 , pp. 2835-2841
    • Mackman, N.1    Baker, K.2    Gray, L.3    Haigh, R.4    Nicaud, J.M.5    Holland, I.B.6
  • 64
    • 0021125517 scopus 로고
    • Functional characterization of a cloned haemolysin determinant from E coli of human origin, encoding information for the secretion of a 107K polypeptide
    • Mackman, N. and Holland, I.B. (1984). Functional characterization of a cloned haemolysin determinant from E. coli of human origin, encoding information for the secretion of a 107K polypeptide. Mol. Gen. Genet. 196, 129-134. (Pubitemid 14035797)
    • (1984) Molecular and General Genetics , vol.196 , Issue.1 , pp. 129-134
    • Mackman, N.1    Holland, I.B.2
  • 65
    • 0035951073 scopus 로고    scopus 로고
    • The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein
    • DOI 10.1021/bi011211z
    • Martin, C., Higgins, C.F., and Callaghan, R. (2001). The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein. Biochem. 40, 15733-15742. (Pubitemid 34015202)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15733-15742
    • Martin, C.1    Higgins, C.F.2    Callaghan, R.3
  • 66
    • 77955296461 scopus 로고    scopus 로고
    • Multiple signals direct the assembly and function of a type 1 secretion system
    • Masi, M. and Wandersman, C. (2010). Multiple signals direct the assembly and function of a type 1 secretion system. J. Bacteriol. 192, 3861-3869.
    • (2010) J. Bacteriol , vol.192 , pp. 3861-3869
    • Masi, M.1    Wandersman, C.2
  • 68
    • 34548491825 scopus 로고    scopus 로고
    • Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: Component interactions defined by the study of pump mutant suppressors
    • DOI 10.1128/JB.00718-07
    • Nehme, D. and Poole, K. (2007). Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors. J. Bacteriol. 189, 6118-6127. (Pubitemid 47378618)
    • (2007) Journal of Bacteriology , vol.189 , Issue.17 , pp. 6118-6127
    • Nehme, D.1    Poole, K.2
  • 69
    • 0023001581 scopus 로고
    • The C-terminal, 23 kDa peptide of E coli haemolysin 2001 contains all the information necessary for its secretion by the haemolysin (Hly) export machinery
    • DOI 10.1016/0014-5793(86)80838-9
    • Nicaud, J.M., Mackman, N., Gray, L., and Holland, I.B. (1986). The C-terminal, 23 kDa peptide of E. coli haemolysin 2001 contains all the information necessary for its secretion by the haemolysin (Hly) export machinery. FEBS Lett. 204, 331-335. (Pubitemid 17177123)
    • (1986) FEBS Letters , vol.204 , Issue.2 , pp. 331-335
    • Nicaud, J.-M.1    Mackman, N.2    Gray, L.3    Holland, I.B.4
  • 70
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • DOI 10.1038/nature06264
    • Oldham, M.L., Khare, D., Quiocho, F.A., Davidson, A.L., and Chen, J. (2007). Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521. (Pubitemid 350190241)
    • (2007) Nature , vol.450 , Issue.7169 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 72
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • DOI 10.1074/jbc.M304796200
    • Patzlaff, J.S., van der Heide, T., and Poolman, B. (2003). The ATP/ substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J. Biol. Chem. 278, 29546-29551. (Pubitemid 36962336)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 74
    • 27144531235 scopus 로고    scopus 로고
    • Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin
    • DOI 10.1128/JB.187.21.7471-7480.2005
    • Pimenta, A.L., Racher, K., Jamieson, L., Blight, M.A., and Holland, I.B. (2005). Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin. J. Bacteriol. 187, 7471-7480. (Pubitemid 41507803)
    • (2005) Journal of Bacteriology , vol.187 , Issue.21 , pp. 7471-7480
    • Pimenta, A.L.1    Racher, K.2    Jamieson, L.3    Blight, M.A.4    Holland, I.B.5
  • 75
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • DOI 10.1126/science.1133488
    • Pinkett, H.W., Lee, A.T., Lum, P., Locher, K.P., and Rees, D.C. (2007). An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373-377. (Pubitemid 46175517)
    • (2007) Science , vol.315 , Issue.5810 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 76
    • 0021887797 scopus 로고
    • Export and secretion of proteins by bacteria
    • Pugsley, A.P. and Schwartz, M. (1985). Export and secretion of proteins by bacteria. FEMS Microbiol. Lett. 32, 3-38. (Pubitemid 15048507)
    • (1985) FEMS Microbiology Reviews , vol.32 , Issue.1 , pp. 3-38
    • Pugsley, A.P.1    Schwartz, M.2
  • 78
    • 0028877021 scopus 로고
    • Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes
    • Rose, T., Sebo, P., Bellalou, J., and Ladant, D. (1995). Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes. J. Biol. Chem. 270, 26370-26376.
    • (1995) J. Biol. Chem , vol.270 , pp. 26370-26376
    • Rose, T.1    Sebo, P.2    Bellalou, J.3    Ladant, D.4
  • 79
    • 0037215533 scopus 로고    scopus 로고
    • The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter
    • DOI 10.1128/JB.185.1.80-88.2003
    • Sapriel, G., Wandersman, C., and Delepelaire, P. (2003). The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter. J. Bacteriol. 185, 80-88. (Pubitemid 36008824)
    • (2003) Journal of Bacteriology , vol.185 , Issue.1 , pp. 80-88
    • Sapriel, G.1    Wandersman, C.2    Delepelaire, P.3
  • 80
    • 80053286819 scopus 로고    scopus 로고
    • Structure and function of MARTX toxins and other large repetitive RTX proteins
    • Satchell, K.J. (2011). Structure and function of MARTX toxins and other large repetitive RTX proteins. Ann. Rev. Microbiol. 65, 71-90.
    • (2011) Ann. Rev. Microbiol , vol.65 , pp. 71-90
    • Satchell, K.J.1
  • 81
    • 0025694884 scopus 로고
    • Genetic analysis of protein export in Escherichia coli
    • Schatz, P.J. and Beckwith, J. (1990). Genetic analysis of protein export in Escherichia coli. Ann. Rev. Genet. 24, 215-248. (Pubitemid 120011547)
    • (1990) Annual Review of Genetics , vol.24 , Issue.1 , pp. 215-248
    • Schatz, P.J.1    Beckwith, J.2
  • 82
    • 0026073817 scopus 로고
    • Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase
    • Schiebel, E., Driessen, A.J., Hartl, F.U., and Wickner, W. (1991). Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64, 927-939. (Pubitemid 121001180)
    • (1991) Cell , vol.64 , Issue.5 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.M.2    Hartl, F.-U.3    Wickner, W.4
  • 83
    • 0038799733 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: Identification of a variable region within ABC helical domains
    • DOI 10.1016/S0022-2836(03)00592-8
    • Schmitt, L., Benabdelhak, H., Blight, M.A., Holland, I.B., and Stubbs, M.T. (2003). Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains. J. Mol. Biol. 330, 333-342. (Pubitemid 36773706)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.2 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, I.B.4    Stubbs, M.T.5
  • 84
    • 0028151060 scopus 로고
    • Identification and characterization of two functional domains of the hemolysin translocator protein hlyD
    • Schulein, R., Gentschev, I., Schlor, S., Gross, R., and Goebel, W. (1994). Identification and characterization of two functional domains of the hemolysin translocator protein HlyD. Mol. Gen. Genet. 245, 203-211. (Pubitemid 24357338)
    • (1994) Molecular and General Genetics , vol.245 , Issue.2 , pp. 203-211
    • Schulein, R.1    Gentschev, I.2    Schlor, S.3    Gross, R.4    Goebel, W.5
  • 85
    • 84860833922 scopus 로고    scopus 로고
    • Using an E coli Type 1 secretion system to secrete the mammalian, intracellular protein IFABP in its active form
    • Schwarz, C.K., Landsberg, C.D., Lenders, M.H., Smits, S.H., and Schmitt, L. (2012). Using an E. coli Type 1 secretion system to secrete the mammalian, intracellular protein IFABP in its active form. J. Biotechnol. 159, 155-161.
    • (2012) J. Biotechnol , vol.159 , pp. 155-161
    • Schwarz, C.K.1    Landsberg, C.D.2    Lenders, M.H.3    Smits, S.H.4    Schmitt, L.5
  • 86
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger, M.A. and van Veen, H.W. (2009). Molecular basis of multidrug transport by ABC transporters. Biochim Biophys Acta 1794, 725-737.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 725-737
    • Seeger, M.A.1    Van Veen, H.W.2
  • 87
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • DOI 10.1016/S1097-2765(02)00576-2
    • Smith, P.C., Karpowich, N., Millen, L., Moody, J.E., Rosen, J., Thomas, P.J., and Hunt, J.F. (2002). ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10, 139-149. (Pubitemid 34876568)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 88
    • 0019121262 scopus 로고
    • Synthesis and secretion of hemolysin by Escherichia coli
    • Springer, W. and Goebel, W. (1980). Synthesis and secretion of hemolysin by Escherichia coli. J. Bacteriol. 144, 53-59. (Pubitemid 11208805)
    • (1980) Journal of Bacteriology , vol.144 , Issue.1 , pp. 53-59
    • Springer, W.1    Goebel, W.2
  • 89
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley, P., Koronakis, V., and Hughes, C. (1991). Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 5, 2391-2403. (Pubitemid 21895970)
    • (1991) Molecular Microbiology , vol.5 , Issue.10 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 90
    • 33748638824 scopus 로고    scopus 로고
    • Importance of the adaptor (membrane fusion) protein hairpin domain for the functionality of multidrug efflux pumps
    • DOI 10.1021/bi060320g
    • Stegmeier, J.F., Polleichtner, G., Brandes, N., Hotz, C., and Andersen, C. (2006). Importance of the adaptor (membrane fusion) protein hairpin domain for the functionality of multidrug efflux pumps. Biochem. 45, 10303-10312. (Pubitemid 44384805)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10303-10312
    • Stegmeier, J.F.1    Polleichtner, G.2    Brandes, N.3    Hotz, C.4    Andersen, C.5
  • 91
    • 0024552790 scopus 로고
    • Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella haemolytica leukotoxin determinant
    • Strathdee, C.A. and Lo, R.Y. (1989). Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella haemolytica leukotoxin determinant. J. Bacteriol. 171, 916-928. (Pubitemid 19053485)
    • (1989) Journal of Bacteriology , vol.171 , Issue.2 , pp. 916-928
    • Strathdee, C.A.1    Lo, R.Y.C.2
  • 93
    • 23944509010 scopus 로고    scopus 로고
    • Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking
    • DOI 10.1021/bi050452u
    • Tamura, N., Murakami, S., Oyama, Y., Ishiguro, M., and Yamaguchi, A. (2005). Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking. Biochem. 44, 11115-11121. (Pubitemid 41209047)
    • (2005) Biochemistry , vol.44 , Issue.33 , pp. 11115-11121
    • Tamura, N.1    Murakami, S.2    Oyama, Y.3    Ishiguro, M.4    Yamaguchi, A.5
  • 94
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu, T., Koronakis, E., Hughes, C., and Koronakis, V. (1998). Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an innermembrane translocase to an outer membrane exit pore. EMBO J. 17, 6487-6496. (Pubitemid 28521784)
    • (1998) EMBO Journal , vol.17 , Issue.22 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 96
    • 0029566085 scopus 로고
    • Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli
    • DOI 10.1074/jbc.270.52.30862
    • Uchida, K., Mori, H., and Mizushima, S. (1995). Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270, 30862-30868. (Pubitemid 26012167)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.52 , pp. 30862-30868
    • Uchida, K.1    Mori, H.2    Mizushima, S.3
  • 97
    • 58749106615 scopus 로고    scopus 로고
    • Gating at both ends and breathing in the middle: Conformational dynamics of TolC
    • Vaccaro, L., Scott, K.A., and Sansom, M.S. (2008). Gating at both ends and breathing in the middle: conformational dynamics of TolC. Biophys. J. 95, 5681-5691.
    • (2008) Biophys. J , vol.95 , pp. 5681-5691
    • Vaccaro, L.1    Scott, K.A.2    Sansom, M.S.3
  • 98
    • 0035174835 scopus 로고    scopus 로고
    • Isolation and characterization of Escherichia coli TolC mutants defective in secreting enzymatically active alpha-hemolysin
    • DOI 10.1128/JB.183.23.6908-6916.2001
    • Vakharia, H., German, G.J., and Misra, R. (2001). Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin. J. Bacteriol. 183, 6908-6916. (Pubitemid 33064205)
    • (2001) Journal of Bacteriology , vol.183 , Issue.23 , pp. 6908-6916
    • Vakharia, H.1    German, G.J.2    Misra, R.3
  • 99
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman, C. and Delepelaire, P. (1990). TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc. Nat. Acad. Sci. USA 87, 4776-4780.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 100
    • 0019792611 scopus 로고
    • Haemolysin contributes to virulence of extra-intestinal E coli infections
    • Welch, R.A., Dellinger, E.P., Minshew, B., and Falkow, S. (1981). Haemolysin contributes to virulence of extra-intestinal E. coli infections. Nature 294, 665-667. (Pubitemid 12213969)
    • (1981) Nature , vol.294 , Issue.5842 , pp. 665-667
    • Welch, R.A.1    Dellinger, E.P.2    Minshew, B.3    Falkow, S.4
  • 101
    • 0020591069 scopus 로고
    • Molecular cloning and physical characterization of a chromosomal hemolysin from Escherichia coli
    • Welch, R.A., Hull, R., and Falkow, S. (1983). Molecular cloning and physical characterization of a chromosomal hemolysin from Escherichia coli. Infect. Immun. 42, 178-186. (Pubitemid 13012451)
    • (1983) Infection and Immunity , vol.42 , Issue.1 , pp. 178-186
    • Welch, R.A.1    Hull, R.2    Falkow, S.3
  • 102
    • 0028285221 scopus 로고
    • C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptide-independent pathway: Proton NMR and CD conformational studies in membrane-mimetic environments
    • DOI 10.1021/bi00188a007
    • Wolff, N., Ghigo, J.M., Delepelaire, P., Wandersman, C., and Delepierre, M. (1994). C-terminal secretion signal of an Erwinia chrysanthemi protease secreted by a signal peptideindependent pathway: proton NMR and CD conformational studies in membrane-mimetic environments. Biochem. 33, 6792-6801. (Pubitemid 24190801)
    • (1994) Biochemistry , vol.33 , Issue.22 , pp. 6792-6801
    • Wolff, N.1    Ghigo, J.-M.2    Delepelaire, P.3    Wandersman, C.4    Delepierre, M.5
  • 103
    • 0141532228 scopus 로고    scopus 로고
    • Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate
    • DOI 10.1074/jbc.M302322200
    • Wolff, N., Sapriel, G., Bodenreider, C., Chaffotte, A., and Delepelaire, P. (2003). Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate. J. Biol. Chem. 278, 38247-38253. (Pubitemid 37221714)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38247-38253
    • Wolff, N.1    Sapriel, G.2    Bodenreider, C.3    Chaffotte, A.4    Delepelaire, P.5
  • 104
    • 77950858238 scopus 로고    scopus 로고
    • The tip region of the MacA alpha-hairpin is important for the binding to TolC to the Escherichia coli MacAB-TolC pump
    • Xu, Y., Sim, S.H., Song, S., Piao, S., Kim, H.M., Jin, X.L., Lee, K., and Ha, N.C. (2010). The tip region of the MacA alpha-hairpin is important for the binding to TolC to the Escherichia coli MacAB-TolC pump. Biochem. Biophys. Res. Commun. 394, 962-965.
    • (2010) Biochem. Biophys. Res. Commun , vol.394 , pp. 962-965
    • Xu, Y.1    Sim, S.H.2    Song, S.3    Piao, S.4    Kim, H.M.5    Jin, X.L.6    Lee, K.7    Ha, N.C.8
  • 105
    • 79955946992 scopus 로고    scopus 로고
    • Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria
    • Xu, Y., Lee, M., Moeller, A., Song, S., Yoon, B.Y., Kim, H.M., Jun, S.Y., Lee, K., and Ha, N.C. (2011a). Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria. J. Biol. Chem. 286, 17910-17920.
    • (2011) J. Biol. Chem , vol.286 , pp. 17910-17920
    • Xu, Y.1    Lee, M.2    Moeller, A.3    Song, S.4    Yoon, B.Y.5    Kim, H.M.6    Jun, S.Y.7    Lee, K.8    Ha, N.C.9
  • 106
    • 79953878893 scopus 로고    scopus 로고
    • Functional implications of an intermeshing cogwheel-like interaction between TolC and MacA in the action of macrolide-specific efflux pump MacAB-TolC
    • Xu, Y., Song, S., Moeller, A., Kim, N., Piao, S., Sim, S.H., Kang, M., Yu, W., Cho, H.S., Chang, I., et al. (2011b). Functional implications of an intermeshing cogwheel-like interaction between TolC and MacA in the action of macrolide-specific efflux pump MacAB-TolC. J. Biol. Chem. 286, 13541-13549.
    • (2011) J. Biol. Chem , vol.286 , pp. 13541-13549
    • Xu, Y.1    Song, S.2    Moeller, A.3    Kim, N.4    Piao, S.5    Sim, S.H.6    Kang, M.7    Yu, W.8    Cho, H.S.9    Chang, I.10
  • 107
    • 63449091256 scopus 로고    scopus 로고
    • Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump
    • Yum, S., Xu, Y., Piao, S., Sim, S.H., Kim, H.M., Jo, W.S., Kim, K.J., Kweon, H.S., Jeong, M.H., Jeon, H., et al. (2009). Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J. Mol. Biol. 387, 1286-1297.
    • (2009) J. Mol. Biol , vol.387 , pp. 1286-1297
    • Yum, S.1    Xu, Y.2    Piao, S.3    Sim, S.H.4    Kim, H.M.5    Jo, W.S.6    Kim, K.J.7    Kweon, H.S.8    Jeong, M.H.9    Jeon, H.10
  • 108
    • 22244452024 scopus 로고    scopus 로고
    • Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter
    • DOI 10.1021/bi0506122
    • Zaitseva, J., Jenewein, S., Wiedenmann, A., Benabdelhak, H., Holland, I.B., and Schmitt, L. (2005). Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter. Biochem. 44, 9680-9690. (Pubitemid 40994362)
    • (2005) Biochemistry , vol.44 , Issue.28 , pp. 9680-9690
    • Zaitseva, J.1    Jenewein, S.2    Wiedenmann, A.3    Benabdelhak, H.4    Holland, I.B.5    Schmitt, L.6
  • 109
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • DOI 10.1038/sj.emboj.7601208, PII 7601208
    • Zaitseva, J., Oswald, C., Jumpertz, T., Jenewein, S., Wiedenmann, A., Holland, I.B., and Schmitt, L. (2006). A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 25, 3432-3443. (Pubitemid 44141799)
    • (2006) EMBO Journal , vol.25 , Issue.14 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5    Holland, I.B.6    Schmitt, L.7
  • 110
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • DOI 10.1128/JB.182.15.4264-4267.2000
    • Zgurskaya, H.I. and Nikaido, H. (2000). Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. J. Bacteriol. 182, 4264-4267. (Pubitemid 30463790)
    • (2000) Journal of Bacteriology , vol.182 , Issue.15 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 112
    • 0027171205 scopus 로고
    • Complementation of transport-deficient mutants of Escherichia coli α- hemolysin by second-site mutations in the transporter hemolysin B
    • Zhang, F., Sheps, J.A., and Ling, V. (1993). Complementation of transport-deficient mutants of Escherichia coli alphahemolysin by second-site mutations in the transporter hemolysin B. J. Biol. Chem. 268, 19889-19895. (Pubitemid 23270785)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19889-19895
    • Zhang, F.1    Sheps, J.A.2    Ling, V.3
  • 113
    • 0028936779 scopus 로고
    • Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA
    • Zhang, F., Yin, Y., Arrowsmith, C.H., and Ling, V. (1995). Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. Biochem. 34, 4193-4201.
    • (1995) Biochem , vol.34 , pp. 4193-4201
    • Zhang, F.1    Yin, Y.2    Arrowsmith, C.H.3    Ling, V.4
  • 114
    • 33749039521 scopus 로고    scopus 로고
    • The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics
    • DOI 10.1085/jgp.200609622
    • Zhou, Z., Wang, X., Liu, H.Y., Zou, X., Li, M., and Hwang, T.C. (2006). The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics. J. Gen. Physiol. 128, 413-422. (Pubitemid 44455100)
    • (2006) Journal of General Physiology , vol.128 , Issue.4 , pp. 413-422
    • Zhou, Z.1    Wang, X.2    Liu, H.-Y.3    Zou, X.4    Li, M.5    Hwang, T.-C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.