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Volumn 383, Issue 5, 2008, Pages 970-981

The Orf18 Gene Product from Conjugative Transposon Tn916 Is an ArdA Antirestriction Protein that Inhibits Type I DNA Restriction-Modification Systems

Author keywords

antirestriction; Ard protein; conjugation; Tn916; transposon

Indexed keywords

ARTICLE; DNA MODIFICATION; DNA RESTRICTION; ESCHERICHIA COLI; GENE EXPRESSION; GENE TRANSFER; HORIZONTAL GENE TRANSFER; IMMUNITY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROKARYOTIC CELL; TRANSPOSON;

EID: 53549107458     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.06.005     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 73649191344 scopus 로고
    • Infective heredity of multiple drug resistance in bacteria
    • Watanabe T. Infective heredity of multiple drug resistance in bacteria. Bacteriol. Rev. 27 (1963) 87-115
    • (1963) Bacteriol. Rev. , vol.27 , pp. 87-115
    • Watanabe, T.1
  • 2
    • 0038170395 scopus 로고    scopus 로고
    • Horizontal gene transfer-emerging multidrug resistance in hospital bacteria
    • Dzidic S., and Bedekovic V. Horizontal gene transfer-emerging multidrug resistance in hospital bacteria. Acta Pharmacol. Sin. 24 (2003) 519-526
    • (2003) Acta Pharmacol. Sin. , vol.24 , pp. 519-526
    • Dzidic, S.1    Bedekovic, V.2
  • 3
    • 0019415205 scopus 로고
    • Evidence for a chromosome-borne resistance transposon (Tn916) in Streptococcus faecalis that is capable of "conjugal" transfer in the absence of a conjugative plasmid
    • Franke A.E., and Clewell B.D. Evidence for a chromosome-borne resistance transposon (Tn916) in Streptococcus faecalis that is capable of "conjugal" transfer in the absence of a conjugative plasmid. J. Bacteriol. 145 (1981) 494-502
    • (1981) J. Bacteriol. , vol.145 , pp. 494-502
    • Franke, A.E.1    Clewell, B.D.2
  • 4
    • 0027962445 scopus 로고
    • Nucleotide sequence of the 18-kb conjugative transposon Tn916 from Enterococcus faecalis
    • Flannagan S.E., Zitzow L.A., Su Y.A., and Clewell D.B. Nucleotide sequence of the 18-kb conjugative transposon Tn916 from Enterococcus faecalis. Plasmid 32 (1994) 350-354
    • (1994) Plasmid , vol.32 , pp. 350-354
    • Flannagan, S.E.1    Zitzow, L.A.2    Su, Y.A.3    Clewell, D.B.4
  • 5
    • 0029046947 scopus 로고
    • Unconstrained bacterial promiscuity: the Tn916-Tn1545 family of conjugative transposons
    • Clewell D.B., Flannagan S.E., and Jaworski D.D. Unconstrained bacterial promiscuity: the Tn916-Tn1545 family of conjugative transposons. Trends Microbiol. 3 (1995) 229-236
    • (1995) Trends Microbiol. , vol.3 , pp. 229-236
    • Clewell, D.B.1    Flannagan, S.E.2    Jaworski, D.D.3
  • 6
    • 0023158055 scopus 로고
    • Tn1545: a conjugative shuttle transposon
    • Courvalin P., and Carlier C. Tn1545: a conjugative shuttle transposon. Mol. Gen. Genet. 206 (1987) 259-264
    • (1987) Mol. Gen. Genet. , vol.206 , pp. 259-264
    • Courvalin, P.1    Carlier, C.2
  • 7
    • 0031887223 scopus 로고    scopus 로고
    • Transfer of Tn5385, a composite, multiresistance chromosomal element from Enterococcus faecalis
    • Rice L.B., and Carias L.L. Transfer of Tn5385, a composite, multiresistance chromosomal element from Enterococcus faecalis. J. Bacteriol. 180 (1998) 714-721
    • (1998) J. Bacteriol. , vol.180 , pp. 714-721
    • Rice, L.B.1    Carias, L.L.2
  • 8
    • 0037389511 scopus 로고    scopus 로고
    • A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes
    • Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., Bitinaite J., et al. A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res. 31 (2003) 1805-1812
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1805-1812
    • Roberts, R.J.1    Belfort, M.2    Bestor, T.3    Bhagwat, A.S.4    Bickle, T.A.5    Bitinaite, J.6
  • 9
    • 0019300793 scopus 로고
    • Restriction and modification in Bacillus subtilis: identification of a gene in the temperate phage SPβ coding for a BsuR-specific modification methyltransferase
    • Trautner T.A., Pawlek B., Günthert U., Canosi U., Jentsch S., and Freund M. Restriction and modification in Bacillus subtilis: identification of a gene in the temperate phage SPβ coding for a BsuR-specific modification methyltransferase. Mol. Gen. Genet. 180 (1980) 361-367
    • (1980) Mol. Gen. Genet. , vol.180 , pp. 361-367
    • Trautner, T.A.1    Pawlek, B.2    Günthert, U.3    Canosi, U.4    Jentsch, S.5    Freund, M.6
  • 10
    • 0019256320 scopus 로고
    • DNA modification induced during infection of Bacillus subtilis by phage φ{symbol}3T
    • Cregg J.M., Nguyen A.H., and Ito J. DNA modification induced during infection of Bacillus subtilis by phage φ{symbol}3T. Gene 12 (1980) 17-24
    • (1980) Gene , vol.12 , pp. 17-24
    • Cregg, J.M.1    Nguyen, A.H.2    Ito, J.3
  • 11
    • 0018580204 scopus 로고
    • Unusual modification of bacteriophage Mu DNA
    • Hattman S. Unusual modification of bacteriophage Mu DNA. J. Virol. 32 (1979) 468-475
    • (1979) J. Virol. , vol.32 , pp. 468-475
    • Hattman, S.1
  • 12
    • 0018942446 scopus 로고
    • The ral gene of phage lambda: I. Identification of a non-essential gene that modulates restriction and modification in E. coli
    • Zabeau M., Friedman S., Van Montagu M., and Schell J. The ral gene of phage lambda: I. Identification of a non-essential gene that modulates restriction and modification in E. coli. Mol. Gen. Genet. 179 (1980) 63-73
    • (1980) Mol. Gen. Genet. , vol.179 , pp. 63-73
    • Zabeau, M.1    Friedman, S.2    Van Montagu, M.3    Schell, J.4
  • 13
    • 0029070828 scopus 로고
    • Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12
    • King G., and Murray N.E. Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12. Mol. Microbiol. 16 (1995) 769-777
    • (1995) Mol. Microbiol. , vol.16 , pp. 769-777
    • King, G.1    Murray, N.E.2
  • 14
    • 0020480208 scopus 로고
    • Digestion of highly modified bacteriophage DNA by restriction enzymes
    • Huang L.H., Forret K., Ehrlich C., and Ehrlich M. Digestion of highly modified bacteriophage DNA by restriction enzymes. Nucleic Acids Res. 10 (1982) 1579-1591
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1579-1591
    • Huang, L.H.1    Forret, K.2    Ehrlich, C.3    Ehrlich, M.4
  • 15
    • 0025999581 scopus 로고
    • Host-controlled modification and restriction as a criterion of evaluating the therapeutic potential of Pseudomonas phage
    • Gachechiladze K.K., Balardshishvili N.S., Adamia R.S., Chanishvili T.G., and Kruger D.H. Host-controlled modification and restriction as a criterion of evaluating the therapeutic potential of Pseudomonas phage. J. Basic Microbiol. 31 (1990) 101-106
    • (1990) J. Basic Microbiol. , vol.31 , pp. 101-106
    • Gachechiladze, K.K.1    Balardshishvili, N.S.2    Adamia, R.S.3    Chanishvili, T.G.4    Kruger, D.H.5
  • 16
    • 0024284313 scopus 로고
    • EcoRII can be activated to cleave refractory DNA recognition sites
    • Kruger D.H., Barcak G.J., Reuter M., and Smith H.O. EcoRII can be activated to cleave refractory DNA recognition sites. Nucleic Acids Res. 16 (1988) 3997-4008
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3997-4008
    • Kruger, D.H.1    Barcak, G.J.2    Reuter, M.3    Smith, H.O.4
  • 17
    • 0016707042 scopus 로고
    • Gene 0.3 of bacteriophage T7 acts to overcome the DNA restriction system of the host
    • Studier F.W. Gene 0.3 of bacteriophage T7 acts to overcome the DNA restriction system of the host. J. Mol. Biol. 94 (1975) 283-295
    • (1975) J. Mol. Biol. , vol.94 , pp. 283-295
    • Studier, F.W.1
  • 18
    • 0019460574 scopus 로고
    • Bacteriophage T3 and bacteriophage T7 virus-host cell interactions
    • Kruger D.H., and Schroeder C. Bacteriophage T3 and bacteriophage T7 virus-host cell interactions. Microbiol. Rev. 45 (1981) 9-51
    • (1981) Microbiol. Rev. , vol.45 , pp. 9-51
    • Kruger, D.H.1    Schroeder, C.2
  • 19
    • 0022345598 scopus 로고
    • Inhibition of the type I restriction-modification enzymes EcoB and EcoK by the gene 0.3 protein of bacteriophage T7
    • Bandyopadhyay P.K., Studier F.W., Hamilton D.L., and Yuan R. Inhibition of the type I restriction-modification enzymes EcoB and EcoK by the gene 0.3 protein of bacteriophage T7. J. Mol. Biol. 182 (1985) 567-578
    • (1985) J. Mol. Biol. , vol.182 , pp. 567-578
    • Bandyopadhyay, P.K.1    Studier, F.W.2    Hamilton, D.L.3    Yuan, R.4
  • 21
    • 0037106445 scopus 로고    scopus 로고
    • Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/modification enzyme
    • Atanasiu C., Su T.-J., Sturrock S.S., and Dryden D.T.F. Interaction of the ocr gene 0.3 protein of bacteriophage T7 with EcoKI restriction/modification enzyme. Nucleic Acids Res. 30 (2002) 3936-3944
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3936-3944
    • Atanasiu, C.1    Su, T.-J.2    Sturrock, S.S.3    Dryden, D.T.F.4
  • 22
    • 0034598955 scopus 로고    scopus 로고
    • Antirestriction protein Ard (type C) encoded by the IncW plasmid pSa has a high similarity to the "protein transport" domain of TraC1 primase of promiscuous plasmid RP4
    • Belogurov A.A., Delver E.P., Agafononva O.V., Belogurova N.G., Lee L., and Kado C. Antirestriction protein Ard (type C) encoded by the IncW plasmid pSa has a high similarity to the "protein transport" domain of TraC1 primase of promiscuous plasmid RP4. J. Mol. Biol. 296 (2000) 969-977
    • (2000) J. Mol. Biol. , vol.296 , pp. 969-977
    • Belogurov, A.A.1    Delver, E.P.2    Agafononva, O.V.3    Belogurova, N.G.4    Lee, L.5    Kado, C.6
  • 23
    • 0028923463 scopus 로고
    • A motif conserved among the type I restriction-modification enzymes and antirestriction proteins: a possible basis for mechanism of action of plasmid-encoded antirestriction functions
    • Belogurov A.A., and Delver E.P. A motif conserved among the type I restriction-modification enzymes and antirestriction proteins: a possible basis for mechanism of action of plasmid-encoded antirestriction functions. Nucleic Acids Res. 23 (1995) 785-787
    • (1995) Nucleic Acids Res. , vol.23 , pp. 785-787
    • Belogurov, A.A.1    Delver, E.P.2
  • 24
    • 0036741145 scopus 로고    scopus 로고
    • Plasmid promiscuity: meeting the challenge of DNA immigration control
    • Wilkins B.M. Plasmid promiscuity: meeting the challenge of DNA immigration control. Environ. Microbiol. 4 (2002) 495-500
    • (2002) Environ. Microbiol. , vol.4 , pp. 495-500
    • Wilkins, B.M.1
  • 26
    • 0027275366 scopus 로고
    • Plasmid pKM101 encodes two nonhomologous antirestriction proteins (ArdA and ArdB) whose expression is controlled by homologous regulatory sequences
    • Belogurov A.A., Delver E.P., and Rodzevich O.V. Plasmid pKM101 encodes two nonhomologous antirestriction proteins (ArdA and ArdB) whose expression is controlled by homologous regulatory sequences. J. Bacteriol. 175 (1993) 4843-4850
    • (1993) J. Bacteriol. , vol.175 , pp. 4843-4850
    • Belogurov, A.A.1    Delver, E.P.2    Rodzevich, O.V.3
  • 27
    • 0037336209 scopus 로고    scopus 로고
    • Plasmid R16 ArdA protein preferentially targets restriction activity of the type I restriction-modification system EcoKI
    • Thomas A.T., Brammar W.J., and Wilkins B.M. Plasmid R16 ArdA protein preferentially targets restriction activity of the type I restriction-modification system EcoKI. J. Bacteriol. 185 (2003) 2022-2025
    • (2003) J. Bacteriol. , vol.185 , pp. 2022-2025
    • Thomas, A.T.1    Brammar, W.J.2    Wilkins, B.M.3
  • 28
    • 0034130457 scopus 로고    scopus 로고
    • Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)
    • Murray N.E. Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle). Microbiol. Mol. Biol. Rev. 64 (2000) 412-434
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 29
    • 0036880785 scopus 로고    scopus 로고
    • Complex restriction enzymes: NTP-driven molecular motors
    • Bourniquel A.A., and Bickle T.A. Complex restriction enzymes: NTP-driven molecular motors. Biochimie 84 (2002) 1047-1059
    • (2002) Biochimie , vol.84 , pp. 1047-1059
    • Bourniquel, A.A.1    Bickle, T.A.2
  • 30
    • 0035886602 scopus 로고    scopus 로고
    • Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems
    • Titheradge A.J., King J., Ryu J., and Murray N.E. Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems. Nucleic Acids Res. 20 (2001) 4195-4205
    • (2001) Nucleic Acids Res. , vol.20 , pp. 4195-4205
    • Titheradge, A.J.1    King, J.2    Ryu, J.3    Murray, N.E.4
  • 31
    • 19544389295 scopus 로고    scopus 로고
    • KpnBI is the prototype of a new family (IE) of bacterial type I restriction-modification system
    • Chin V., Valinluck V., Magaki S., and Ryu J. KpnBI is the prototype of a new family (IE) of bacterial type I restriction-modification system. Nucleic Acids Res. 32 (2004) e138
    • (2004) Nucleic Acids Res. , vol.32
    • Chin, V.1    Valinluck, V.2    Magaki, S.3    Ryu, J.4
  • 32
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 33
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade M.A., Chacón P., Merelo J.J., and Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 33751504620 scopus 로고    scopus 로고
    • Plasmid-encoded antirestriction protein ArdA can discriminate between type I methyltransferase and complete restriction-modification system
    • Nekrasov S.V., Agafonova O.V., Belogurova N.G., Delver E.P., and Belogurov A.A. Plasmid-encoded antirestriction protein ArdA can discriminate between type I methyltransferase and complete restriction-modification system. J. Mol. Biol. 365 (2007) 284-297
    • (2007) J. Mol. Biol. , vol.365 , pp. 284-297
    • Nekrasov, S.V.1    Agafonova, O.V.2    Belogurova, N.G.3    Delver, E.P.4    Belogurov, A.A.5
  • 37
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins: quantitative determination by fluorescence quenching studies
    • Eftink K., and Ghiron A.C. Exposure of tryptophanyl residues in proteins: quantitative determination by fluorescence quenching studies. Biochemistry 15 (1976) 672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, K.1    Ghiron, A.C.2
  • 38
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink K., and Ghiron A.C. Fluorescence quenching studies with proteins. Anal. Biochem. 144 (1981) 199-277
    • (1981) Anal. Biochem. , vol.144 , pp. 199-277
    • Eftink, K.1    Ghiron, A.C.2
  • 39
    • 0035878856 scopus 로고    scopus 로고
    • Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7
    • Atanasiu C., Byron O., McMiken H., Sturrock S., and Dryden D.T.F. Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7. Nucleic Acids Res. 29 (2001) 3059-3068
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3059-3068
    • Atanasiu, C.1    Byron, O.2    McMiken, H.3    Sturrock, S.4    Dryden, D.T.F.5
  • 41
    • 0031049939 scopus 로고    scopus 로고
    • The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications
    • Dryden D.T.F., Cooper L.P., Thorpe P.H., and Byron O. The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications. Biochemistry 5 (1997) 1065-1076
    • (1997) Biochemistry , vol.5 , pp. 1065-1076
    • Dryden, D.T.F.1    Cooper, L.P.2    Thorpe, P.H.3    Byron, O.4
  • 42
    • 0027497325 scopus 로고
    • Purification and characterization of the methyltransferase from the type I restriction and modification system of Escherichia coli K12
    • Dryden D.T.F., Cooper L.P., and Murray N.E. Purification and characterization of the methyltransferase from the type I restriction and modification system of Escherichia coli K12. J. Biol. Chem. 268 (1993) 13228-13236
    • (1993) J. Biol. Chem. , vol.268 , pp. 13228-13236
    • Dryden, D.T.F.1    Cooper, L.P.2    Murray, N.E.3
  • 43
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann E., Ochs B., and Abel K.J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69 (1988) 301-315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 44
    • 0033214565 scopus 로고    scopus 로고
    • The DNA translocation and ATPase activities of restriction-deficient mutants of EcoKI
    • Davies G.P., Kemp P., Molineux I.J., and Murray N.E. The DNA translocation and ATPase activities of restriction-deficient mutants of EcoKI. J. Mol. Biol. 292 (1999) 787-796
    • (1999) J. Mol. Biol. , vol.292 , pp. 787-796
    • Davies, G.P.1    Kemp, P.2    Molineux, I.J.3    Murray, N.E.4


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