메뉴 건너뛰기




Volumn 164, Issue 6, 2013, Pages 596-604

Type I secretion systems - a story of appendices

Author keywords

ABC transporters; C39 peptidase domain; Haemolysin; Type I secretion systems

Indexed keywords

ABC TRANSPORTER; ADHESIN; ALKALINE PROTEINASE; BACTERIOCIN; C39 PEPTIDASE LIKE DOMAIN; MESSENGER RNA; PEPTIDASE; PROTEINASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84879885088     PISSN: 09232508     EISSN: 17697123     Source Type: Journal    
DOI: 10.1016/j.resmic.2013.03.011     Document Type: Article
Times cited : (94)

References (78)
  • 2
    • 0028842445 scopus 로고
    • The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide
    • Akatsuka H., Kawai E., Omori K., Shibatani T. The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide. J. Bacteriol. 1995, 177:6381-6389.
    • (1995) J. Bacteriol. , vol.177 , pp. 6381-6389
    • Akatsuka, H.1    Kawai, E.2    Omori, K.3    Shibatani, T.4
  • 4
    • 0031748720 scopus 로고    scopus 로고
    • The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus
    • Awram P., Smit J. The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus. J. Bacteriol. 1998, 180:3062-3069.
    • (1998) J. Bacteriol. , vol.180 , pp. 3062-3069
    • Awram, P.1    Smit, J.2
  • 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., Schmitt L. The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system. J. Biol. Chem. 2010, 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
    • Balakrishnan L., Hughes C., Koronakis V. Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli. J. Mol. Biol. 2001, 313:501-510.
    • (2001) J. Mol. Biol. , vol.313 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3
  • 7
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
    • Baumann U., Wu S., Flaherty K.M., McKay D.B. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 1993, 12:3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 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
    • Benabdelhak H., Kiontke S., Horn C., Ernst R., Blight M.A., Holland I.B., Schmitt L. 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. 2003, 327:1169-1179.
    • (2003) J. Mol. Biol. , vol.327 , 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
    • 0029806326 scopus 로고    scopus 로고
    • Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: a TolC analogue
    • Binet R., Wandersman C. Cloning of the Serratia marcescens hasF gene encoding the Has ABC exporter outer membrane component: a TolC analogue. Mol. Microbiol. 1996, 22:265-273.
    • (1996) Mol. Microbiol. , vol.22 , pp. 265-273
    • Binet, R.1    Wandersman, C.2
  • 11
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J., Lu G., Lin J., Davidson A.L., Quiocho F.A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell. 2003, 12:651-661.
    • (2003) Mol. Cell. , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 12
    • 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., Holland I.B. 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. 1996, 178:1232-1236.
    • (1996) J. Bacteriol. , vol.178 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 13
    • 79954529507 scopus 로고    scopus 로고
    • ProtTest 3: fast selection of best-fit models of protein evolution
    • Darriba D., Taboada G.L., Doallo R., Posada D. ProtTest 3: fast selection of best-fit models of protein evolution. Bioinformatics 2011, 27:1164-1165.
    • (2011) Bioinformatics , vol.27 , pp. 1164-1165
    • Darriba, D.1    Taboada, G.L.2    Doallo, R.3    Posada, D.4
  • 14
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson A.L., Dassa E., Orelle C., Chen J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 2008, 72:317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 15
    • 0035801397 scopus 로고    scopus 로고
    • Folded HasA inhibits its own secretion through its ABC exporter
    • Debarbieux L., Wandersman C. Folded HasA inhibits its own secretion through its ABC exporter. EMBO J. 2001, 20:4657-4663.
    • (2001) EMBO J. , vol.20 , pp. 4657-4663
    • Debarbieux, L.1    Wandersman, C.2
  • 16
    • 8844241421 scopus 로고    scopus 로고
    • Type I secretion in gram-negative bacteria
    • Delepelaire P. Type I secretion in gram-negative bacteria. Biochim. Biophys. Acta 2004, 1694:149-161.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 149-161
    • Delepelaire, P.1
  • 17
    • 0032481311 scopus 로고    scopus 로고
    • The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter
    • Delepelaire P., Wandersman C. The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter. EMBO J. 1998, 17:936-944.
    • (1998) EMBO J. , vol.17 , pp. 936-944
    • Delepelaire, P.1    Wandersman, C.2
  • 18
    • 2942578482 scopus 로고    scopus 로고
    • Peptide signal molecules and bacteriocins in Gram-negative bacteria: a genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters
    • Dirix G., Monsieurs P., Dombrecht B., Daniels R., Marchal K., Vanderleyden J., Michiels J. Peptide signal molecules and bacteriocins in Gram-negative bacteria: a genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters. Peptides 2004, 25:1425-1440.
    • (2004) Peptides , vol.25 , pp. 1425-1440
    • Dirix, G.1    Monsieurs, P.2    Dombrecht, B.3    Daniels, R.4    Marchal, K.5    Vanderleyden, J.6    Michiels, J.7
  • 20
    • 0026475721 scopus 로고
    • Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways
    • Duong F., Lazdunski A., Cami B., Murgier M. Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways. Gene 1992, 121:47-54.
    • (1992) Gene , vol.121 , pp. 47-54
    • Duong, F.1    Lazdunski, A.2    Cami, B.3    Murgier, M.4
  • 22
    • 34548508225 scopus 로고    scopus 로고
    • Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria
    • Duquesne S., Petit V., Peduzzi J., Rebuffat S. Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J. Mol. Microbiol. Biotechnol. 2007, 13:200-209.
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 200-209
    • Duquesne, S.1    Petit, V.2    Peduzzi, J.3    Rebuffat, S.4
  • 24
    • 0034005123 scopus 로고    scopus 로고
    • Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds
    • Espinosa-Urgel M., Salido A., Ramos J.L. Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds. J. Bacteriol. 2000, 182:2363-2369.
    • (2000) J. Bacteriol. , vol.182 , pp. 2363-2369
    • Espinosa-Urgel, M.1    Salido, A.2    Ramos, J.L.3
  • 25
    • 0028271859 scopus 로고
    • Purification and characterization of colicin V from Escherichia coli culture supernatants
    • Fath M.J., Zhang L.H., Rush J., Kolter R. Purification and characterization of colicin V from Escherichia coli culture supernatants. Biochemistry 1994, 33:6911-6917.
    • (1994) Biochemistry , vol.33 , pp. 6911-6917
    • Fath, M.J.1    Zhang, L.H.2    Rush, J.3    Kolter, R.4
  • 26
    • 84871000484 scopus 로고    scopus 로고
    • ABC transporters of antimicrobial peptides in Firmicutes bacteria - phylogeny, function and regulation
    • Gebhard S. ABC transporters of antimicrobial peptides in Firmicutes bacteria - phylogeny, function and regulation. Mol. Microbiol. 2012, 86:1295-1317.
    • (2012) Mol. Microbiol. , vol.86 , pp. 1295-1317
    • Gebhard, S.1
  • 27
    • 0023181112 scopus 로고
    • Four plasmid genes are required for colicin V synthesis, export, and immunity
    • Gilson L., Mahanty H.K., Kolter R. Four plasmid genes are required for colicin V synthesis, export, and immunity. J. Bacteriol. 1987, 169:2466-2470.
    • (1987) J. Bacteriol. , vol.169 , pp. 2466-2470
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 28
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: the secretion of colicin V
    • Gilson L., Mahanty H.K., Kolter R. Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J. 1990, 9:3875-3884.
    • (1990) EMBO J. , vol.9 , pp. 3875-3884
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 29
    • 0024795976 scopus 로고
    • A novel C-terminal signal sequence targets Escherichia coli haemolysin directly to the medium
    • Gray L., Baker K., Kenny B., Mackman N., Haigh R., Holland I.B. A novel C-terminal signal sequence targets Escherichia coli haemolysin directly to the medium. J. Cell. Sci. Suppl. 1989, 11:45-57.
    • (1989) J. Cell. Sci. Suppl. , vol.11 , pp. 45-57
    • Gray, L.1    Baker, K.2    Kenny, B.3    Mackman, N.4    Haigh, R.5    Holland, I.B.6
  • 30
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S., Dufayard J.F., Lefort V., Anisimova M., Hordijk W., Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 2010, 59:307-321.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 31
    • 0026088819 scopus 로고
    • The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin
    • Guzzo J., Duong F., Wandersman C., Murgier M., Lazdunski A. The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin. Mol. Microbiol. 1991, 5:447-453.
    • (1991) Mol. Microbiol. , vol.5 , pp. 447-453
    • Guzzo, J.1    Duong, F.2    Wandersman, C.3    Murgier, M.4    Lazdunski, A.5
  • 32
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Havarstein L.S., Diep D.B., Nes I.F. A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol. Microbiol. 1995, 16:229-240.
    • (1995) Mol. Microbiol. , vol.16 , pp. 229-240
    • Havarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 34
    • 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
    • Hinsa S.M., Espinosa-Urgel M., Ramos J.L., O'Toole G.A. Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol. Microbiol. 2003, 49:905-918.
    • (2003) Mol. Microbiol. , vol.49 , pp. 905-918
    • Hinsa, S.M.1    Espinosa-Urgel, M.2    Ramos, J.L.3    O'Toole, G.A.4
  • 35
    • 85163467886 scopus 로고    scopus 로고
    • Bacterial ABC transporters involved in protein translocation
    • Academic Press, London, I.B. Holland, S.P. Cole, K. Kuchler, C. Higgins (Eds.)
    • Holland I.B., Benabdelhak H., Young J., De Lima Pimenta A., Schmitt L., Blight M.A. Bacterial ABC transporters involved in protein translocation. ABC Proteins: From Bacteria to Man 2003, 209-241. Academic Press, London. I.B. Holland, S.P. Cole, K. Kuchler, C. Higgins (Eds.).
    • (2003) ABC Proteins: From Bacteria to Man , pp. 209-241
    • Holland, I.B.1    Benabdelhak, H.2    Young, J.3    De Lima Pimenta, A.4    Schmitt, L.5    Blight, M.A.6
  • 36
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review)
    • Holland I.B., Schmitt L., Young J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review). Mol. Memb. Biol. 2005, 22:29-39.
    • (2005) Mol. Memb. Biol. , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 38
    • 0025370072 scopus 로고
    • Identification of amino acids in the gamma-carboxylation recognition site on the propeptide of prothrombin
    • Huber P., Schmitz T., Griffin J., Jacobs M., Walsh C., Furie B., Furie B.C. Identification of amino acids in the gamma-carboxylation recognition site on the propeptide of prothrombin. J. Biol. Chem. 1990, 265:12467-12473.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12467-12473
    • Huber, P.1    Schmitz, T.2    Griffin, J.3    Jacobs, M.4    Walsh, C.5    Furie, B.6    Furie, B.C.7
  • 39
    • 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., Hayashi H. Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway. J. Biol. Chem. 2010, 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
  • 40
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. Simple allosteric model for membrane pumps. Nature 1966, 211:969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 41
    • 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 1999, 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
  • 42
    • 70349335633 scopus 로고    scopus 로고
    • ABC transporters: a riddle wrapped in a mystery inside an enigma
    • Jones P.M., O'Mara M.L., George A.M. ABC transporters: a riddle wrapped in a mystery inside an enigma. TIBS 2009, 34:520-531.
    • (2009) TIBS , vol.34 , pp. 520-531
    • Jones, P.M.1    O'Mara, M.L.2    George, A.M.3
  • 43
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh K., Toh H. Recent developments in the MAFFT multiple sequence alignment program. Brief. Bioinform. 2008, 9:286-298.
    • (2008) Brief. Bioinform. , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 44
    • 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
    • Kenny B., Chervaux C., Holland I.B. 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. 1994, 11:99-109.
    • (1994) Mol. Microbiol. , vol.11 , pp. 99-109
    • Kenny, B.1    Chervaux, C.2    Holland, I.B.3
  • 45
    • 0026683501 scopus 로고
    • Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region
    • Kenny B., Taylor S., Holland I.B. Identification of individual amino acids required for secretion within the haemolysin (HlyA) C-terminal targeting region. Mol. Microbiol. 1992, 6:1477-1489.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1477-1489
    • Kenny, B.1    Taylor, S.2    Holland, I.B.3
  • 46
    • 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 2000, 405:914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 47
    • 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., Schmitt L. An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain. Structure 2012, 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
  • 48
    • 0025257358 scopus 로고
    • Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin
    • Letoffe S., Delepelaire P., Wandersman C. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin. EMBO J. 1990, 9:1375-1382.
    • (1990) EMBO J. , vol.9 , pp. 1375-1382
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 49
    • 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., Wandersman C. 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. 1996, 15:5804-5811.
    • (1996) EMBO J. , vol.15 , pp. 5804-5811
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 50
    • 0028023120 scopus 로고
    • Secretion of the Serratia marcescens HasA protein by an ABC transporter
    • Létoffé S., Ghigo J.M., Wandersman C. Secretion of the Serratia marcescens HasA protein by an ABC transporter. J. Bacteriol. 1994, 176:5372-5377.
    • (1994) J. Bacteriol. , vol.176 , pp. 5372-5377
    • Létoffé, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 53
    • 0022411845 scopus 로고
    • Identification of polypeptides required for the export of haemolysin 2001 from E. coli
    • Mackman N., Nicaud J.M., Gray L., Holland I.B. Identification of polypeptides required for the export of haemolysin 2001 from E. coli. Mol. Gen. Genet. 1985, 201:529-536.
    • (1985) Mol. Gen. Genet. , vol.201 , pp. 529-536
    • Mackman, N.1    Nicaud, J.M.2    Gray, L.3    Holland, I.B.4
  • 54
    • 77955296461 scopus 로고    scopus 로고
    • Multiple signals direct the assembly and function of a type 1 secretion system
    • Masi M., Wandersman C. Multiple signals direct the assembly and function of a type 1 secretion system. J. Bacteriol. 2010, 192:3861-3869.
    • (2010) J. Bacteriol. , vol.192 , pp. 3861-3869
    • Masi, M.1    Wandersman, C.2
  • 55
    • 33644833626 scopus 로고    scopus 로고
    • Conformational flexibility in the multidrug efflux system protein AcrA
    • Mikolosko J., Bobyk K., Zgurskaya H.I., Ghosh P. Conformational flexibility in the multidrug efflux system protein AcrA. Structure 2006, 14:577-587.
    • (2006) Structure , vol.14 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 56
    • 84355166442 scopus 로고    scopus 로고
    • Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
    • Nakashima R., Sakurai K., Yamasaki S., Nishino K., Yamaguchi A. Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nature 2011, 480:565-569.
    • (2011) Nature , vol.480 , pp. 565-569
    • Nakashima, R.1    Sakurai, K.2    Yamasaki, S.3    Nishino, K.4    Yamaguchi, A.5
  • 57
    • 0021943351 scopus 로고
    • Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin
    • Nicaud J.M., Mackman N., Gray L., Holland I.B. Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin. Mol. Gen. Genet. 1985, 199:111-116.
    • (1985) Mol. Gen. Genet. , vol.199 , pp. 111-116
    • Nicaud, J.M.1    Mackman, N.2    Gray, L.3    Holland, I.B.4
  • 59
    • 0033020320 scopus 로고    scopus 로고
    • Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator
    • Pimenta A.L., Young J., Holland I.B., Blight M.A. Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator. Mol. Gen. Genet. 1999, 261:122-132.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 122-132
    • Pimenta, A.L.1    Young, J.2    Holland, I.B.3    Blight, M.A.4
  • 60
    • 64649100965 scopus 로고    scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • Pos K.M. Drug transport mechanism of the AcrB efflux pump. Biochim. Biophys. Acta 2009, 1794:782-793.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 782-793
    • Pos, K.M.1
  • 61
    • 0037155161 scopus 로고    scopus 로고
    • The N terminus of the HasA protein and the SecB chaperone cooperate in the efficient targeting and secretion of HasA via the ATP-binding cassette transporter
    • Sapriel G., Wandersman C., Delepelaire P. The N terminus of the HasA protein and the SecB chaperone cooperate in the efficient targeting and secretion of HasA via the ATP-binding cassette transporter. J. Biol. Chem. 2002, 277:6726-6732.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6726-6732
    • Sapriel, G.1    Wandersman, C.2    Delepelaire, P.3
  • 62
    • 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
    • Sapriel G., Wandersman C., Delepelaire P. 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. 2003, 185:80-88.
    • (2003) J. Bacteriol. , vol.185 , pp. 80-88
    • Sapriel, G.1    Wandersman, C.2    Delepelaire, P.3
  • 63
    • 80053286819 scopus 로고    scopus 로고
    • Structure and function of MARTX toxins and other large repetitive RTX proteins
    • Satchell K.J. Structure and function of MARTX toxins and other large repetitive RTX proteins. Annu. Rev. Microbiol. 2011, 65:71-90.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 71-90
    • Satchell, K.J.1
  • 64
    • 0029043806 scopus 로고
    • Hemolysin transport in Escherichia coli - point mutants in hlyb compensate for a deletion in the predicted amphiphilic helix region of the hlya signal
    • Sheps J.A., Cheung I., Ling V. Hemolysin transport in Escherichia coli - point mutants in hlyb compensate for a deletion in the predicted amphiphilic helix region of the hlya signal. J. Biol. Chem. 1995, 270:14829-14834.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14829-14834
    • Sheps, J.A.1    Cheung, I.2    Ling, V.3
  • 65
    • 0026778803 scopus 로고
    • The S-layer of Caulobacter crescentus: three-dimensional image reconstruction and structure analysis by electron microscopy
    • Smit J., Engelhardt H., Volker S., Smith S.H., Baumeister W. The S-layer of Caulobacter crescentus: three-dimensional image reconstruction and structure analysis by electron microscopy. J. Bacteriol. 1992, 174:6527-6538.
    • (1992) J. Bacteriol. , vol.174 , pp. 6527-6538
    • Smit, J.1    Engelhardt, H.2    Volker, S.3    Smith, S.H.4    Baumeister, W.5
  • 66
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., Hunt J.F. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 2002, 10:139-149.
    • (2002) Mol. Cell. , vol.10 , 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
  • 67
    • 79955750874 scopus 로고    scopus 로고
    • Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states
    • Sotomayor-Perez A.C., Ladant D., Chenal A. Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states. J. Biol. Chem. 2011, 286:16997-17004.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16997-17004
    • Sotomayor-Perez, A.C.1    Ladant, D.2    Chenal, A.3
  • 68
  • 70
    • 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., Koronakis V. 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. EMBO J. 1998, 17:6487-6496.
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 71
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman C., Delepelaire P. TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:4776-4780.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 72
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology
    • Welch R.A. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology. Curr. Top. Microbiol. Immunol. 2001, 257:85-111.
    • (2001) Curr. Top. Microbiol. Immunol. , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 73
    • 0019792611 scopus 로고
    • Haemolysin contributes to virulence of extra-intestinal E. coli infections
    • Welch R.A., Dellinger E.P., Minshew B., Falkow S. Haemolysin contributes to virulence of extra-intestinal E. coli infections. Nature 1981, 294:665-667.
    • (1981) Nature , vol.294 , pp. 665-667
    • Welch, R.A.1    Dellinger, E.P.2    Minshew, B.3    Falkow, S.4
  • 74
    • 84859994125 scopus 로고    scopus 로고
    • Mutational analysis of Cvab, an ABC transporter involved in the secretion of active colicin V
    • Wu K.H., Hsieh Y.H., Tai P.C. Mutational analysis of Cvab, an ABC transporter involved in the secretion of active colicin V. PloS One 2012, 7:e35382.
    • (2012) PloS One , vol.7
    • Wu, K.H.1    Hsieh, Y.H.2    Tai, P.C.3
  • 75
    • 0345832155 scopus 로고    scopus 로고
    • Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter
    • Wu K.H., Tai P.C. Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter. J. Biol. Chem. 2004, 279:901-909.
    • (2004) J. Biol. Chem. , vol.279 , pp. 901-909
    • Wu, K.H.1    Tai, P.C.2
  • 77
    • 0029023510 scopus 로고
    • Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A
    • Yin Y., Zhang F., Ling V., Arrowsmith C.H. Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A. FEBS Lett. 1995, 366:1-5.
    • (1995) FEBS Lett. , vol.366 , pp. 1-5
    • Yin, Y.1    Zhang, F.2    Ling, V.3    Arrowsmith, C.H.4
  • 78
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewein S., Jumpertz T., Holland I.B., Schmitt L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 2005, 24:1901-1910.
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.