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Volumn 194, Issue 15, 2012, Pages 4041-4051

Enterococcus faecalis PrgJ, a VirB4-Like ATPase, Mediates pCF10 conjugative transfer through substrate binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DIMER; DOUBLE STRANDED DNA; FORMALDEHYDE; MUTANT PROTEIN; NUCLEOSIDE TRIPHOSPHATE; PHEROMONE; SINGLE STRANDED DNA;

EID: 84866310251     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00648-12     Document Type: Article
Times cited : (40)

References (47)
  • 1
    • 33947121550 scopus 로고    scopus 로고
    • A type IV-secretion-like system is required for conjugative DNA transport of broad-host-range plasmid pIP501 in grampositive bacteria
    • Abajy MY, et al. 2007. A type IV-secretion-like system is required for conjugative DNA transport of broad-host-range plasmid pIP501 in grampositive bacteria. J. Bacteriol. 189:2487-2496.
    • (2007) J. Bacteriol , vol.189 , pp. 2487-2496
    • Abajy, M.Y.1
  • 3
    • 48149115518 scopus 로고    scopus 로고
    • ATPase activity and oligomeric state of TrwK, the VirB4 homologue of the plasmid R388 type IV secretion system
    • Arechaga I, et al. 2008. ATPase activity and oligomeric state of TrwK, the VirB4 homologue of the plasmid R388 type IV secretion system. J. Bacteriol. 190:5472-5479.
    • (2008) J. Bacteriol. , vol.190 , pp. 5472-5479
    • Arechaga, I.1
  • 4
    • 9644272811 scopus 로고    scopus 로고
    • Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion
    • Atmakuri K, Cascales E, Christie PJ. 2004. Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion. Mol. Microbiol. 54:1199-1211.
    • (2004) Mol. Microbiol , vol.54 , pp. 1199-1211
    • Atmakuri, K.1    Cascales, E.2    Christie, P.J.3
  • 5
    • 0141789692 scopus 로고    scopus 로고
    • VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens
    • Atmakuri K, Ding Z, Christie PJ. 2003. VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens. Mol. Microbiol. 49:1699-1713.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1699-1713
    • Atmakuri, K.1    Ding, Z.2    Christie, P.J.3
  • 6
    • 0033748351 scopus 로고    scopus 로고
    • Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins
    • Burgess RR, Arthur TM, Pietz BC. 2000. Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins. Methods Enzymol. 328:141-157.
    • (2000) Methods Enzymol , vol.328 , pp. 141-157
    • Burgess, R.R.1    Arthur, T.M.2    Pietz, B.C.3
  • 7
    • 2442682800 scopus 로고    scopus 로고
    • Definition of a bacterial type IV secretion pathway for a DNA substrate
    • Cascales E, Christie PJ. 2004. Definition of a bacterial type IV secretion pathway for a DNA substrate. Science. 304:1170-1173.
    • (2004) Science , vol.304 , pp. 1170-1173
    • Cascales, E.1    Christie, P.J.2
  • 8
    • 33847005432 scopus 로고    scopus 로고
    • Specificity determinants of conjugative DNA processing in the Enterococcus faecalis plasmid pCF10 and the Lactococcus lactis plasmid pRS01
    • Chen Y, Staddon JH, Dunny GM. 2007. Specificity determinants of conjugative DNA processing in the Enterococcus faecalis plasmid pCF10 and the Lactococcus lactis plasmid pRS01. Mol. Microbiol. 63:1549-1564.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1549-1564
    • Chen, Y.1    Staddon, J.H.2    Dunny, G.M.3
  • 9
    • 47049127816 scopus 로고    scopus 로고
    • Enterococcus faecalis PcfC, a spatially localized substrate receptor for type IV secretion of the pCF10 transfer intermediate
    • Chen Y, et al. 2008. Enterococcus faecalis PcfC, a spatially localized substrate receptor for type IV secretion of the pCF10 transfer intermediate. J. Bacteriol. 190:3632-3645.
    • (2008) J. Bacteriol , vol.190 , pp. 3632-3645
    • Chen, Y.1
  • 10
    • 84866341612 scopus 로고
    • Characterization of a pheromone-inducible plasmid transfer system and a conjugative transposon associated with the Streptococcus faecalis R-plasmid pCF10. Ph.D. thesis
    • Cornell University, Ithaca, NY
    • Christie PJ. 1987. Characterization of a pheromone-inducible plasmid transfer system and a conjugative transposon associated with the Streptococcus faecalis R-plasmid pCF10. Ph.D. thesis. Cornell University, Ithaca, NY.
    • (1987)
    • Christie, P.J.1
  • 12
    • 58449097088 scopus 로고    scopus 로고
    • Multiple functional domains of Enterococcus faecalis aggregation substance Asc10 contribute to endocarditis virulence
    • Chuang ON, et al. 2009. Multiple functional domains of Enterococcus faecalis aggregation substance Asc10 contribute to endocarditis virulence. Infect. Immun. 77:539-548.
    • (2009) Infect. Immun. , vol.77 , pp. 539-548
    • Chuang, O.N.1
  • 13
    • 35349020565 scopus 로고    scopus 로고
    • Properties of Enterococcus faecalis plasmid pAD1, a member of a widely disseminated family of pheromone-responding, conjugative, virulence elements encoding cytolysin
    • Clewell DB. 2007. Properties of Enterococcus faecalis plasmid pAD1, a member of a widely disseminated family of pheromone-responding, conjugative, virulence elements encoding cytolysin. Plasmid. 58:205-227.
    • (2007) Plasmid , vol.58 , pp. 205-227
    • Clewell, D.B.1
  • 14
    • 0031014646 scopus 로고    scopus 로고
    • The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface
    • Dang TA, Christie PJ. 1997. The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface. J. Bacteriol. 179:453-462.
    • (1997) J. Bacteriol. , vol.179 , pp. 453-462
    • Dang, T.A.1    Christie, P.J.2
  • 15
    • 0033037708 scopus 로고    scopus 로고
    • Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter
    • Dang TA, Zhou XR, Graf B, Christie PJ. 1999. Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter. Mol. Microbiol. 32:1239-1253.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1239-1253
    • Dang, T.A.1    Zhou, X.R.2    Graf, B.3    Christie, P.J.4
  • 16
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen AJ, Nouwen N. 2008. Protein translocation across the bacterial cytoplasmic membrane. Annu. Rev. Biochem. 77:643-667.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 17
    • 0019777947 scopus 로고
    • Direct stimulation of the transfer of antibiotic resistance by sex pheromones in Streptococcus faecalis
    • Dunny G, Funk C, Adsit J. 1981. Direct stimulation of the transfer of antibiotic resistance by sex pheromones in Streptococcus faecalis. Plasmid. 6:270-278.
    • (1981) Plasmid , vol.6 , pp. 270-278
    • Dunny, G.1    Funk, C.2    Adsit, J.3
  • 18
    • 34447566242 scopus 로고    scopus 로고
    • The peptide pheromone-inducible conjugation system of Enterococcus faecalis plasmid pCF10: cell-cell signalling, gene transfer, complexity and evolution
    • Dunny GM. 2007. The peptide pheromone-inducible conjugation system of Enterococcus faecalis plasmid pCF10: cell-cell signalling, gene transfer, complexity and evolution. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 362:1185-1193.
    • (2007) Philos. Trans. R. Soc. Lond. B. Biol. Sci , vol.362 , pp. 1185-1193
    • Dunny, G.M.1
  • 19
    • 0342867597 scopus 로고
    • Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone
    • Dunny GM, Brown BL, Clewell DB. 1978. Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone. Proc. Natl. Acad. Sci. U. S. A. 75:3479-3483.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 3479-3483
    • Dunny, G.M.1    Brown, B.L.2    Clewell, D.B.3
  • 20
    • 79954615144 scopus 로고    scopus 로고
    • Regulatory circuits controlling enterococcal conjugation: lessons for functional genomics
    • Dunny GM, Johnson CM. 2011. Regulatory circuits controlling enterococcal conjugation: lessons for functional genomics. Curr. Opin. Microbiol. 14:174-180.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 174-180
    • Dunny, G.M.1    Johnson, C.M.2
  • 21
    • 0022381366 scopus 로고
    • Induction of surface exclusion (entry exclusion) by Streptococcus faecalis sex pheromones: use of monoclonal antibodies to identify an inducible surface antigen involved in the exclusion process
    • Dunny GM, Zimmerman DL, Tortorello ML. 1985. Induction of surface exclusion (entry exclusion) by Streptococcus faecalis sex pheromones: use of monoclonal antibodies to identify an inducible surface antigen involved in the exclusion process. Proc. Natl. Acad. Sci. U. S. A. 82:8582-8586.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8582-8586
    • Dunny, G.M.1    Zimmerman, D.L.2    Tortorello, M.L.3
  • 22
    • 77951034296 scopus 로고    scopus 로고
    • Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery
    • Durand E, Oomen C, Waksman G. 2010. Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery. J. Bacteriol. 192:2315-2323.
    • (2010) J. Bacteriol , vol.192 , pp. 2315-2323
    • Durand, E.1    Oomen, C.2    Waksman, G.3
  • 23
    • 78951474759 scopus 로고    scopus 로고
    • Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system
    • Durand E, Waksman G, Receveur-Brechot V. 2011. Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system. BMC Struct. Biol. 11:4.
    • (2011) BMC Struct. Biol. , vol.11 , pp. 4
    • Durand, E.1    Waksman, G.2    Receveur-Brechot, V.3
  • 25
    • 2342445023 scopus 로고    scopus 로고
    • Coupling factors in macromolecular type-IV secretion machineries
    • Gomis-Ruth FX, Sola M, de la Cruz F, Coll M. 2004. Coupling factors in macromolecular type-IV secretion machineries. Curr. Pharm. Des. 10:1551-1565.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1551-1565
    • Gomis-Ruth, F.X.1    Sola, M.2    de la Cruz, F.3    Coll, M.4
  • 26
    • 0034053027 scopus 로고    scopus 로고
    • TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58
    • Hamilton CM, et al. 2000. TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58. J. Bacteriol. 182:1541-1548.
    • (2000) J. Bacteriol. , vol.182 , pp. 1541-1548
    • Hamilton, C.M.1
  • 27
    • 13244271302 scopus 로고    scopus 로고
    • Characterization of the pheromone response of the Enterococcus faecalis conjugative plasmid pCF10: complete sequence and comparative analysis of the transcriptional and phenotypic responses of pCF10-containing cells to pheromone induction
    • Hirt H, et al. 2005. Characterization of the pheromone response of the Enterococcus faecalis conjugative plasmid pCF10: complete sequence and comparative analysis of the transcriptional and phenotypic responses of pCF10-containing cells to pheromone induction. J. Bacteriol. 187:1044-1054.
    • (2005) J. Bacteriol. , vol.187 , pp. 1044-1054
    • Hirt, H.1
  • 28
    • 18244405305 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis
    • Jakubowski SJ, Cascales E, Krishnamoorthy V, Christie PJ. 2005. Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis. J. Bacteriol. 187:3486-3495.
    • (2005) J. Bacteriol , vol.187 , pp. 3486-3495
    • Jakubowski, S.J.1    Cascales, E.2    Krishnamoorthy, V.3    Christie, P.J.4
  • 29
    • 77957348046 scopus 로고    scopus 로고
    • Evidence for VirB4-mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system
    • Kerr JE, Christie PJ. 2010. Evidence for VirB4-mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system. J. Bacteriol. 192:4923-4934.
    • (2010) J. Bacteriol , vol.192 , pp. 4923-4934
    • Kerr, J.E.1    Christie, P.J.2
  • 30
    • 33846993832 scopus 로고    scopus 로고
    • Development of a hostgenotype-independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis
    • Kristich CJ, Chandler JR, Dunny GM. 2007. Development of a hostgenotype-independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis. Plasmid. 57:131-144.
    • (2007) Plasmid , vol.57 , pp. 131-144
    • Kristich, C.J.1    Chandler, J.R.2    Dunny, G.M.3
  • 31
    • 26844580763 scopus 로고    scopus 로고
    • Development of a method for markerless genetic exchange in Enterococcus faecalis and its use in construction of a srtA mutant
    • Kristich CJ, Manias DA, Dunny GM. 2005. Development of a method for markerless genetic exchange in Enterococcus faecalis and its use in construction of a srtA mutant. Appl. Environ. Microbiol. 71:5837-5849.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 5837-5849
    • Kristich, C.J.1    Manias, D.A.2    Dunny, G.M.3
  • 32
    • 0029908131 scopus 로고    scopus 로고
    • A general system for generating unlabelled gene replacements in bacterial chromosomes
    • Leenhouts K, et al. 1996. A general system for generating unlabelled gene replacements in bacterial chromosomes. Mol. Gen. Genet. 253:217-224.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 217-224
    • Leenhouts, K.1
  • 33
    • 79953699014 scopus 로고    scopus 로고
    • Subsite specificity of anthrax lethal factor and its implications for inhibitor development
    • Li F, Terzyan S, Tang J. 2011. Subsite specificity of anthrax lethal factor and its implications for inhibitor development. Biochem. Biophys. Res. Commun. 407:400-405.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 400-405
    • Li, F.1    Terzyan, S.2    Tang, J.3
  • 34
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: structure and mechanism of hexameric FtsK
    • Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J. 2006. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell. 23:457-469.
    • (2006) Mol. Cell. , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Lowe, J.5
  • 35
    • 13444250892 scopus 로고    scopus 로고
    • Predicted hexameric structure of the Agrobacterium VirB4 C-terminus suggests VirB4 acts as a docking site during type IV secretion
    • Middleton R, Sjolander K, Krishamurthy N, Foley J, Zambryski P. 2005. Predicted hexameric structure of the Agrobacterium VirB4 C-terminus suggests VirB4 acts as a docking site during type IV secretion. Proc. Natl. Acad. Sci. U. S. A. 102:1685-1690.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1685-1690
    • Middleton, R.1    Sjolander, K.2    Krishamurthy, N.3    Foley, J.4    Zambryski, P.5
  • 36
    • 77952566137 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens type IV secretion protein VirB3 is an inner membrane protein and requires VirB4, VirB7, and VirB8 for stabilization
    • Mossey P, Hudacek A, Das A. 2010. Agrobacterium tumefaciens type IV secretion protein VirB3 is an inner membrane protein and requires VirB4, VirB7, and VirB8 for stabilization. J. Bacteriol. 192:2830-2838.
    • (2010) J. Bacteriol , vol.192 , pp. 2830-2838
    • Mossey, P.1    Hudacek, A.2    Das, A.3
  • 37
    • 0027501798 scopus 로고
    • Highresolution visualization by field emission scanning electron microscopy of Enterococcus faecalis surface proteins encoded by the pheromone-inducible conjugative plasmid pCF10
    • Olmsted SB, Erlandsen SL, Dunny GM, Wells CL. 1993. Highresolution visualization by field emission scanning electron microscopy of Enterococcus faecalis surface proteins encoded by the pheromone-inducible conjugative plasmid pCF10. J. Bacteriol. 175:6229-6237.
    • (1993) J. Bacteriol , vol.175 , pp. 6229-6237
    • Olmsted, S.B.1    Erlandsen, S.L.2    Dunny, G.M.3    Wells, C.L.4
  • 38
    • 0037307783 scopus 로고    scopus 로고
    • The VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorption
    • Rabel C, Grahn AM, Lurz R, Lanka E. 2003. The VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorption. J. Bacteriol. 185:1045-1058.
    • (2003) J. Bacteriol , vol.185 , pp. 1045-1058
    • Rabel, C.1    Grahn, A.M.2    Lurz, R.3    Lanka, E.4
  • 39
    • 77749310273 scopus 로고    scopus 로고
    • Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A
    • Rangrez AY, Abajy MY, Keller W, Shouche Y, Grohmann E. 2010. Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A. BMC Biochem. 11:10.
    • (2010) BMC Biochem , vol.11 , pp. 10
    • Rangrez, A.Y.1    Abajy, M.Y.2    Keller, W.3    Shouche, Y.4    Grohmann, E.5
  • 40
    • 0026623139 scopus 로고
    • Localization of TraC, a protein involved in assembly of the F conjugative pilus
    • Schandel KA, Muller MM, Webster RE. 1992. Localization of TraC, a protein involved in assembly of the F conjugative pilus. J. Bacteriol. 174:3800-3806.
    • (1992) J. Bacteriol , vol.174 , pp. 3800-3806
    • Schandel, K.A.1    Muller, M.M.2    Webster, R.E.3
  • 41
    • 0036239133 scopus 로고    scopus 로고
    • TraG-like proteins of DNA transfer systems and of the Helicobacter pylori type IV secretion system: inner membrane gate for exported substrates?
    • Schroder G, et al. 2002. TraG-like proteins of DNA transfer systems and of the Helicobacter pylori type IV secretion system: inner membrane gate for exported substrates? J. Bacteriol. 184:2767-2779.
    • (2002) J Bacteriol , vol.184 , pp. 2767-2779
    • Schroder, G.1
  • 42
    • 0037767570 scopus 로고    scopus 로고
    • TraG-like proteins of type IV secretion systems: functional dissection of the multiple activities of TraG (RP4) and TrwB (R388)
    • Schroder G, Lanka E. 2003. TraG-like proteins of type IV secretion systems: functional dissection of the multiple activities of TraG (RP4) and TrwB (R388). J. Bacteriol. 185:4371-4381.
    • (2003) J. Bacteriol , vol.185 , pp. 4371-4381
    • Schroder, G.1    Lanka, E.2
  • 43
    • 33746425259 scopus 로고    scopus 로고
    • Genetic characterization of the conjugative DNA processing system of enterococcal plasmid pCF10
    • Staddon JH, Bryan EM, Manias DA, Chen Y, Dunny GM. 2006. Genetic characterization of the conjugative DNA processing system of enterococcal plasmid pCF10. Plasmid. 56:102-111.
    • (2006) Plasmid , vol.56 , pp. 102-111
    • Staddon, J.H.1    Bryan, E.M.2    Manias, D.A.3    Chen, Y.4    Dunny, G.M.5
  • 44
    • 1842558979 scopus 로고    scopus 로고
    • Conserved target for group II intron insertion in relaxase genes of conjugative elements of gram-positive bacteria
    • Staddon JH, Bryan EM, Manias DA, Dunny GM. 2004. Conserved target for group II intron insertion in relaxase genes of conjugative elements of gram-positive bacteria. J. Bacteriol. 186:2393-2401.
    • (2004) J. Bacteriol , vol.186 , pp. 2393-2401
    • Staddon, J.H.1    Bryan, E.M.2    Manias, D.A.3    Dunny, G.M.4
  • 45
    • 65549118438 scopus 로고    scopus 로고
    • The putative coupling protein TcpA interacts with other pCW3-encoded proteins to form an essential part of the conjugation complex
    • Steen JA, Bannam TL, Teng WL, Devenish RJ, Rood JI. 2009. The putative coupling protein TcpA interacts with other pCW3-encoded proteins to form an essential part of the conjugation complex. J. Bacteriol. 191:2926-2933.
    • (2009) J. Bacteriol , vol.191 , pp. 2926-2933
    • Steen, J.A.1    Bannam, T.L.2    Teng, W.L.3    Devenish, R.J.4    Rood, J.I.5
  • 46
    • 0033770898 scopus 로고    scopus 로고
    • Interaction between the RP4 coupling protein TraG and the pBHR1 mobilization protein Mob
    • Szpirer CY, Faelen M, Couturier M. 2000. Interaction between the RP4 coupling protein TraG and the pBHR1 mobilization protein Mob. Mol. Microbiol. 37:1283-1292.
    • (2000) Mol. Microbiol , vol.37 , pp. 1283-1292
    • Szpirer, C.Y.1    Faelen, M.2    Couturier, M.3
  • 47
    • 22544443955 scopus 로고    scopus 로고
    • Identification of the VirB4-VirB8-VirB5-VirB2 pilus assembly sequence of type IV secretion systems
    • Yuan Q, et al. 2005. Identification of the VirB4-VirB8-VirB5-VirB2 pilus assembly sequence of type IV secretion systems. J. Biol. Chem. 280:26349-26359.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26349-26359
    • Yuan, Q.1


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