메뉴 건너뛰기




Volumn 11, Issue 8, 2013, Pages 525-538

Breaking and joining single-stranded DNA: the HUH endonuclease superfamily

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DNA; ENDONUCLEASE; HELICASE; HUH ENDONUCLEASE; PHOSPHOTYROSINE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84880509250     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3067     Document Type: Review
Times cited : (213)

References (119)
  • 2
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
    • Ilyina, T. V. & Koonin, E. V. Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria. Nucleic Acids Res. 20, 3279-3285 (1992
    • (1992) Nucleic Acids Res , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 3
    • 0027205506 scopus 로고
    • Computer-assisted dissection of rolling circle DNA replication
    • Koonin, E. V. & Ilyina, T. V. Computer-assisted dissection of rolling circle DNA replication. Biosystems 30, 241-268 (1993
    • (1993) Biosystems , vol.30 , pp. 241-268
    • Koonin, E.V.1    Ilyina, T.V.2
  • 4
    • 0035902449 scopus 로고    scopus 로고
    • Rolling-circle transposons in eukaryotes
    • Kapitonov, V. V. & Jurka, J. Rolling-circle transposons in eukaryotes. Proc. Natl Acad. Sci. USA 98, 8714-8719 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8714-8719
    • Kapitonov, V.V.1    Jurka, J.2
  • 5
    • 0011417149 scopus 로고    scopus 로고
    • eds Craig, N. L., Craigie, R., Gellert, M., & Lambowitz, A. ASM Press
    • Garcillan-Barcia, M. P., Bernales, I., Mendiola, M. V. & De la Cruz, F. in Mobile DNA Vol. II (eds Craig, N. L., Craigie, R., Gellert, M., & Lambowitz, A.) 891-904 (ASM Press, 2002
    • (2002) Mobile DNA , vol.2 , pp. 891-904
    • Garcillan-Barcia, M.P.1    Bernales, I.2    Mendiola, M.V.3    De La Cruz, F.4
  • 6
    • 25144496154 scopus 로고    scopus 로고
    • Transposition of ISHp608, member of an unusual family of bacterial insertion sequences
    • Ton-Hoang, B. et al. Transposition of ISHp608, member of an unusual family of bacterial insertion sequences. EMBO J. 24, 3325-3338 (2005
    • (2005) EMBO J. , vol.24 , pp. 3325-3338
    • Ton-Hoang, B.1
  • 7
    • 25844521203 scopus 로고    scopus 로고
    • Active site sharing and subterminal hairpin recognition in a new class of DNA transposases
    • Ronning, D. R. et al. Active site sharing and subterminal hairpin recognition in a new class of DNA transposases. Mol. Cell 20, 143-154 (2005
    • (2005) Mol. Cell , vol.20 , pp. 143-154
    • Ronning, D.R.1
  • 8
    • 33745125702 scopus 로고    scopus 로고
    • ISCR elements: Novel gene-capturing systems of the 21st century?
    • Toleman, M. A., Bennett, P. M. & Walsh, T. R. ISCR elements: Novel gene-capturing systems of the 21st century? Microbiol. Mol. Biol. Rev. 70, 296-316 (2006
    • (2006) Microbiol Mol. Biol. Rev , vol.70 , pp. 296-316
    • Toleman, M.A.1    Bennett, P.M.2    Walsh, T.R.3
  • 9
    • 64349087867 scopus 로고    scopus 로고
    • The diversity of conjugative relaxases and its application in plasmid classification
    • Garcillan-Barcia, M. P., Francia, M. V. & de la Cruz, F. The diversity of conjugative relaxases and its application in plasmid classification. FEMS Microbiol. Rev. 33, 657-687 (2009
    • (2009) FEMS Microbiol. Rev , vol.33 , pp. 657-687
    • Garcillan-Barcia, M.P.1    Francia, M.V.2    De La Cruz, F.3
  • 10
    • 0024334198 scopus 로고
    • The family of highly interrelated single-stranded deoxyribonucleic acid plasmids
    • Gruss, A. & Ehrlich, S. D. The family of highly interrelated single-stranded deoxyribonucleic acid plasmids. Microbiol. Rev. 53, 231-241 (1989
    • (1989) Microbiol. Rev , vol.53 , pp. 231-241
    • Gruss, A.1    Ehrlich, S.D.2
  • 11
    • 84867142649 scopus 로고    scopus 로고
    • A field guide to eukaryotic circular single-stranded DNA viruses: Insights gained from metagenomics
    • Rosario, K., Duffy, S. & Breitbart, M. A field guide to eukaryotic circular single-stranded DNA viruses: Insights gained from metagenomics. Arch. Virol. 157, 1851-1871 (2012
    • (2012) Arch. Virol , vol.157 , pp. 1851-1871
    • Rosario, K.1    Duffy, S.2    Breitbart, M.3
  • 12
    • 0242636324 scopus 로고    scopus 로고
    • The outs and ins of transposition: From Mu to Kangaroo
    • Curcio, M. J. & Derbyshire, K. M. The outs and ins of transposition: From Mu to Kangaroo. Nature Rev. Mol. Cell Biol. 4, 865-877 (2003
    • (2003) Nature Rev. Mol. Cell Biol , vol.4 , pp. 865-877
    • Curcio, M.J.1    Derbyshire, K.M.2
  • 13
    • 0035957520 scopus 로고    scopus 로고
    • The two active-site tyrosine residues of the A protein play non-equivalent roles during initiation of rolling circle replication of bacteriophage p2
    • Odegrip, R. & Haggard-Ljungquist, E. The two active-site tyrosine residues of the A protein play non-equivalent roles during initiation of rolling circle replication of bacteriophage p2. J. Mol. Biol. 308, 147-163 (2001
    • (2001) J. Mol. Biol , vol.308 , pp. 147-163
    • Odegrip, R.1    Haggard-Ljungquist, E.2
  • 15
    • 78449306936 scopus 로고    scopus 로고
    • DNA recognition and the precleavage state during single-stranded DNA transposition in D radiodurans
    • Hickman, A. B. et al. DNA recognition and the precleavage state during single-stranded DNA transposition in D. radiodurans. EMBO J. 29, 3840-3852 (2010
    • (2010) EMBO J. , vol.29 , pp. 3840-3852
    • Hickman, A.B.1
  • 16
    • 33646850212 scopus 로고    scopus 로고
    • Unveiling the molecular mechanism of a conjugative relaxase: The structure of TrwC complexed with a 27 mer DNA comprising the recognition hairpin and the cleavage site
    • Boer, R. et al. Unveiling the molecular mechanism of a conjugative relaxase: The structure of TrwC complexed with a 27 mer DNA comprising the recognition hairpin and the cleavage site. J. Mol. Biol. 358, 857-869 (2006
    • (2006) J. Mol. Biol , vol.358 , pp. 857-869
    • Boer, R.1
  • 17
    • 67349214924 scopus 로고    scopus 로고
    • Plasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domains
    • Boer, D. R. et al. Plasmid replication initiator RepB forms a hexamer reminiscent of ring helicases and has mobile nuclease domains. EMBO J. 28, 1666-1678 (2009
    • (2009) EMBO J. , vol.28 , pp. 1666-1678
    • Boer, D.R.1
  • 18
    • 0242542025 scopus 로고    scopus 로고
    • Structural insights into single-stranded DNA binding and cleavage by F factor TraI
    • Datta, S., Larkin, C. & Schildbach, J. F. Structural insights into single-stranded DNA binding and cleavage by F factor TraI. Structure 11, 1369-1379 (2003
    • (2003) Structure , vol.11 , pp. 1369-1379
    • Datta, S.1    Larkin, C.2    Schildbach, J.F.3
  • 19
    • 26444521223 scopus 로고    scopus 로고
    • Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase
    • Larkin, C. et al. Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase. Structure 13, 1533-1544 (2005
    • (2005) Structure , vol.13 , pp. 1533-1544
    • Larkin, C.1
  • 20
    • 84874248186 scopus 로고    scopus 로고
    • Molecular basis of antibiotic multiresistance transfer in Staphylococcus aureus
    • Edwards, J. S. et al. Molecular basis of antibiotic multiresistance transfer in Staphylococcus aureus. Proc. Natl Acad. Sci. USA http://dx.doi.org/10.1073/pnas.1219701110 (2013
    • (2013) Proc. Natl Acad. Sci. USA
    • Edwards, J.S.1
  • 21
    • 0242710964 scopus 로고    scopus 로고
    • A mob of reps
    • Dyda, F. & Hickman, A. B. A Mob of Reps. Structure 11, 1310-1311 (2003
    • (2003) Structure , vol.11 , pp. 1310-1311
    • Dyda, F.1    Hickman, A.B.2
  • 22
    • 0344628800 scopus 로고    scopus 로고
    • Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC
    • Guasch, A. et al. Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC. Nature Struct. Biol. 10, 1002-1010 (2003
    • (2003) Nature Struct. Biol , vol.10 , pp. 1002-1010
    • Guasch, A.1
  • 23
    • 1242339574 scopus 로고    scopus 로고
    • The nuclease domain of adeno-associated virus Rep coordinates replication initiation using two distinct DNA recognition interfaces
    • Hickman, A. B., Ronning, D. R., Perez, Z. N., Kotin, R. M. & Dyda, F. The nuclease domain of adeno-associated virus Rep coordinates replication initiation using two distinct DNA recognition interfaces. Mol. Cell 13, 403-414 (2004
    • (2004) Mol. Cell , vol.13 , pp. 403-414
    • Hickman, A.B.1    Ronning, D.R.2    Perez, Z.N.3    Kotin, R.M.4    Dyda, F.5
  • 24
    • 33750691714 scopus 로고    scopus 로고
    • DNA helicase activity is associated with the replication initiator protein Rep of tomato yellow leaf curl geminivirus
    • Clerot, D. & Bernardi, F. DNA helicase activity is associated with the replication initiator protein Rep of tomato yellow leaf curl geminivirus. J. Virol. 80, 11322-11330 (2006
    • (2006) J. Virol , vol.80 , pp. 11322-11330
    • Clerot, D.1    Bernardi, F.2
  • 25
    • 0033994310 scopus 로고    scopus 로고
    • The interaction of bacteriophage P2 B protein with Escherichia coli DnaB helicase
    • Odegrip, R., Schoen, S., Haggard-Ljungquist, E., Park, K. & Chattoraj, D. K. The interaction of bacteriophage P2 B protein with Escherichia coli DnaB helicase. J. Virol. 74, 4057-4063 (2000
    • (2000) J. Virol , vol.74 , pp. 4057-4063
    • Odegrip, R.1    Schoen, S.2    Haggard-Ljungquist, E.3    Park, K.4    Chattoraj, D.K.5
  • 26
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication
    • Petit, M. A. et al. PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication. Mol. Microbiol. 29, 261-273 (1998
    • (1998) Mol. Microbiol , vol.29 , pp. 261-273
    • Petit, M.A.1
  • 27
    • 0033958431 scopus 로고    scopus 로고
    • UvrD-dependent replication of rolling-circle plasmids in Escherichia coli
    • Bruand, C. & Ehrlich, S. D. UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol. Microbiol. 35, 204-210 (2000
    • (2000) Mol. Microbiol , vol.35 , pp. 204-210
    • Bruand, C.1    Ehrlich, S.D.2
  • 28
    • 0037195801 scopus 로고    scopus 로고
    • Biochemical characterization of the Staphylococcus aureus PcrA helicase and its role in plasmid rolling circle replication
    • Chang, T. L. et al. Biochemical characterization of the Staphylococcus aureus PcrA. helicase and its role in plasmid rolling circle replication. J. Biol. Chem. 277, 45880-45886 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 45880-45886
    • Chang, T.L.1
  • 29
    • 0032853990 scopus 로고    scopus 로고
    • Rep-mediated nicking of the adeno-associated virus origin requires two biochemical activities dna helicase activity and transesterification
    • Brister, J. R. & Muzyczka, N. Rep-mediated nicking of the adeno-associated virus origin requires two biochemical activities, DNA helicase activity and transesterification. J. Virol. 73, 9325-9336 (1999
    • (1999) J. Virol , vol.73 , pp. 9325-9336
    • Brister, J.R.1    Muzyczka, N.2
  • 30
    • 0025362618 scopus 로고
    • The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity
    • Im, D. S. & Muzyczka, N. The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity. Cell 61, 447-457 (1990
    • (1990) Cell , vol.61 , pp. 447-457
    • Im, D.S.1    Muzyczka, N.2
  • 31
    • 0033899961 scopus 로고    scopus 로고
    • Mechanism of Rep-mediated adeno-associated virus origin nicking
    • Brister, J. R. & Muzyczka, N. Mechanism of Rep-mediated adeno-associated virus origin nicking. J. Virol. 74, 7762-7771 (2000
    • (2000) J. Virol , vol.74 , pp. 7762-7771
    • Brister, J.R.1    Muzyczka, N.2
  • 32
    • 84860354792 scopus 로고    scopus 로고
    • Structuring the bacterial genome: Y1 transposases associated with REP-BIME sequences
    • Ton-Hoang, B. et al. Structuring the bacterial genome: Y1 transposases associated with REP-BIME sequences. Nucleic Acids Res. 40, 3596-3609 (2012
    • (2012) Nucleic Acids Res , vol.40 , pp. 3596-3609
    • Ton-Hoang, B.1
  • 33
    • 84868147781 scopus 로고    scopus 로고
    • The processing of repetitive extragenic palindromes: The structure of a repetitive extragenic palindrome bound to its associated nuclease
    • Messing, S. A. et al. The processing of repetitive extragenic palindromes: The structure of a repetitive extragenic palindrome bound to its associated nuclease. Nucleic Acids Res. 40, 9964-9979 (2012
    • (2012) Nucleic Acids Res , vol.40 , pp. 9964-9979
    • Messing, S.A.1
  • 34
    • 0029655926 scopus 로고    scopus 로고
    • DNA structure is required for geminivirus replication origin function
    • Orozco, B. M. & Hanley-Bowdoin, L. A. DNA structure is required for geminivirus replication origin function. J. Virol. 70, 148-158 (1996
    • (1996) J. Virol , vol.70 , pp. 148-158
    • Orozco, B.M.1    Hanley-Bowdoin, L.A.2
  • 36
    • 78650095891 scopus 로고    scopus 로고
    • Folded DNA in action: Hairpin formation and biological functions in prokaryotes
    • Bikard, D., Loot, C., Baharoglu, Z. & Mazel, D. Folded DNA in action: Hairpin formation and biological functions in prokaryotes. Microbiol. Mol. Biol. Rev. 74, 570-588 (2011
    • (2011) Microbiol. Mol. Biol. Rev , vol.74 , pp. 570-588
    • Bikard, D.1    Loot, C.2    Baharoglu, Z.3    Mazel, D.4
  • 38
    • 34047146480 scopus 로고    scopus 로고
    • Interactions between the RepB initiator protein of plasmid pMV158 and two distant DNA regions within the origin of replication
    • Ruiz-Maso, J. A., Lurz, R., Espinosa, M. & del Solar, G. Interactions between the RepB initiator protein of plasmid pMV158 and two distant DNA regions within the origin of replication. Nucleic Acids Res. 35, 1230-1244 (2007
    • (2007) Nucleic Acids Res , vol.35 , pp. 1230-1244
    • Ruiz-Maso, J.A.1    Lurz, R.2    Espinosa, M.3    Del Solar, G.4
  • 40
    • 0033868154 scopus 로고    scopus 로고
    • Plasmid rolling-circle replication: Recent developments
    • Khan, S. A. Plasmid rolling-circle replication: Recent developments. Mol. Microbiol. 37, 477-484 (2000
    • (2000) Mol. Microbiol , vol.37 , pp. 477-484
    • Khan, S.A.1
  • 41
    • 0020300665 scopus 로고
    • DNA structures required for ?X174 A protein-directed initiation and termination of DNA replication
    • Brown, D. R. et al. DNA structures required for ?X174 A protein-directed initiation and termination of DNA replication. Cold Spring Harb. Symp. Quant. Biol. 47, 701-715 (1983
    • (1983) Cold Spring Harb. Symp. Quant. Biol , vol.47 , pp. 701-715
    • Brown, D.R.1
  • 42
    • 0021099671 scopus 로고
    • DNA sequences which support activities of the bacteriophage fX174 gene A protein
    • Brown, D. R., Schmidt-Glenewinkel, T., Reinberg, D. & Hurwitz, J. DNA sequences which support activities of the bacteriophage fX174 gene A protein. J. Biol. Chem. 258, 8402-8412 (1983
    • (1983) J. Biol. Chem , vol.258 , pp. 8402-8412
    • Brown, D.R.1    Schmidt-Glenewinkel, T.2    Reinberg, D.3    Hurwitz, J.4
  • 43
    • 0021285415 scopus 로고
    • Analysis of bacteriophage ?X174 gene A protein-mediated termination and reinitiation of ?X DNA synthesis II structural characterization of the covalent ?X A protein-DNA complex
    • Roth, M. J., Brown, D. R. & Hurwitz, J. Analysis of bacteriophage ?X174 gene A protein-mediated termination and reinitiation of ?X DNA synthesis. II. Structural characterization of the covalent ?X A protein-DNA complex. J. Biol. Chem. 259, 10556-10568 (1984
    • (1984) J. Biol. Chem , vol.259 , pp. 10556-10568
    • Roth, M.J.1    Brown, D.R.2    Hurwitz, J.3
  • 44
    • 0027436394 scopus 로고
    • The mechanism of sequence-specific DNA cleavage and strand transfer by ?X174 gene A* protein
    • Hanai, R. & Wang, J. C. The mechanism of sequence-specific DNA cleavage and strand transfer by ?X174 gene A* protein. J. Biol. Chem. 268, 23830-23836 (1993
    • (1993) J. Biol. Chem , vol.268 , pp. 23830-23836
    • Hanai, R.1    Wang, J.C.2
  • 45
    • 0023057871 scopus 로고
    • Two juxtaposed tyrosyl OH groups participate in ?X174 gene A protein catalysed cleavage and ligation of DNA
    • van Mansfeld, A. D., van Teeffelen, H. A., Baas, P. D. & Jansz, H. S. Two juxtaposed tyrosyl OH groups participate in ?X174 gene A protein catalysed cleavage and ligation of DNA. Nucleic Acids Res. 14, 4229-4238 (1986
    • (1986) Nucleic Acids Res , vol.14 , pp. 4229-4238
    • Van Mansfeld, A.D.1    Van Teeffelen, H.A.2    Baas, P.D.3    Jansz, H.S.4
  • 46
    • 38649116679 scopus 로고    scopus 로고
    • Mechanism of IS200/IS605 family DNA transposases: Activation and transposon-directed target site selection
    • Barabas, O. et al. Mechanism of IS200/IS605 family DNA transposases: Activation and transposon-directed target site selection. Cell 132, 208-220 (2008
    • (2008) Cell , vol.132 , pp. 208-220
    • Barabas, O.1
  • 47
    • 0029908732 scopus 로고    scopus 로고
    • Change of a catalytic reaction carried out by a DNA replication protein
    • Noirot-Gros, M. F. & Ehrlich, S. D. Change of a catalytic reaction carried out by a DNA replication protein. Science 274, 777-780 (1996
    • (1996) Science , vol.274 , pp. 777-780
    • Noirot-Gros, M.F.1    Ehrlich, S.D.2
  • 48
    • 0031739965 scopus 로고    scopus 로고
    • Contrasting lifestyles of rolling-circle phages and plasmids
    • Novick, R. P. Contrasting lifestyles of rolling-circle phages and plasmids. Trends Biochem. Sci. 23, 434-438 (1998
    • (1998) Trends Biochem. Sci , vol.23 , pp. 434-438
    • Novick, R.P.1
  • 49
    • 0031584268 scopus 로고    scopus 로고
    • Initiation of replication of plasmid pMV158: Mechanisms of DNA strand-transfer reactions mediated by the initiator RepB protein
    • Moscoso, M., Eritja, R. & Espinosa, M. Initiation of replication of plasmid pMV158: Mechanisms of DNA strand-transfer reactions mediated by the initiator RepB protein. J. Mol. Biol. 268, 840-856 (1997
    • (1997) J. Mol. Biol , vol.268 , pp. 840-856
    • Moscoso, M.1    Eritja, R.2    Espinosa, M.3
  • 50
    • 0017167291 scopus 로고
    • Rolling hairpin model for replication of parvovirus and linear chromosomal DNA
    • Tattersall, P. & Ward, D. C. Rolling hairpin model for replication of parvovirus and linear chromosomal DNA. Nature 263, 106-109 (1976
    • (1976) Nature , vol.263 , pp. 106-109
    • Tattersall, P.1    Ward, D.C.2
  • 51
    • 0041630781 scopus 로고    scopus 로고
    • Crystal structure of the SF3 helicase from adeno-associated virus type 2
    • James, J. A. et al. Crystal structure of the SF3 helicase from adeno-associated virus type 2. Structure 11, 1025-1035 (2003
    • (2003) Structure , vol.11 , pp. 1025-1035
    • James, J.A.1
  • 52
    • 0031903004 scopus 로고    scopus 로고
    • The Rep52 gene product of adeno-associated virus is a DNA helicase with 3' to 5' polarity
    • Smith, R. H. & Kotin, R. M. The Rep52 gene product of adeno-associated virus is a DNA helicase with 3' to 5' polarity. J. Virol. 72, 4874-4881 (1998
    • (1998) J. Virol , vol.72 , pp. 4874-4881
    • Smith, R.H.1    Kotin, R.M.2
  • 53
    • 84857933340 scopus 로고    scopus 로고
    • The amino acid linker between the endonuclease and helicase domains of adeno-associated virus type 5 Rep plays a critical role in DNA-dependent oligomerization
    • Maggin, J. E., James, J. A., Chappie, J. S., Dyda, F. & Hickman, A. B. The amino acid linker between the endonuclease and helicase domains of adeno-associated virus type 5 Rep plays a critical role in DNA-dependent oligomerization. J. Virol. 86, 3337-3346 (2012
    • (2012) J. Virol , vol.86 , pp. 3337-3346
    • Maggin, J.E.1    James, J.A.2    Chappie, J.S.3    Dyda, F.4    Hickman, A.B.5
  • 54
    • 84864056927 scopus 로고    scopus 로고
    • The interdomain linker of AAV 2 Rep68 is an integral part of its oligomerization domain: Role of a conserved SF3 helicase residue in oligomerization
    • Zarate-Perez, F. et al. The interdomain linker of AAV 2 Rep68 is an integral part of its oligomerization domain: Role of a conserved SF3 helicase residue in oligomerization. PLoS Pathog. 8, e1002764 (2012
    • (2012) PLoS Pathog , vol.8
    • Zarate-Perez, F.1
  • 55
    • 0036671409 scopus 로고    scopus 로고
    • Structural unity among viral origin binding proteins: Crystal structure of the nuclease domain of adeno-associated virus Rep
    • Hickman, A. B., Ronning, D. R., Kotin, R. M. & Dyda, F. Structural unity among viral origin binding proteins: Crystal structure of the nuclease domain of adeno-associated virus Rep. Mol. Cell 10, 327-337 (2002
    • (2002) Mol. Cell , vol.10 , pp. 327-337
    • Hickman, A.B.1    Ronning, D.R.2    Kotin, R.M.3    Dyda, F.4
  • 56
    • 0035875669 scopus 로고    scopus 로고
    • DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids
    • King, J. A., Dubielzig, R., Grimm, D. & Kleinschmidt, J. A. DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids. EMBO J. 20, 3282-3291 (2001
    • (2001) EMBO J. , vol.20 , pp. 3282-3291
    • King, J.A.1    Dubielzig, R.2    Grimm, D.3    Kleinschmidt, J.A.4
  • 58
    • 34249700716 scopus 로고    scopus 로고
    • Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures
    • Vega-Rocha, S., Gronenborn, B., Gronenborn, A. M. & Campos-Olivas, R. Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures. Biochemistry 46, 6201-6212 (2007
    • (2007) Biochemistry , vol.46 , pp. 6201-6212
    • Vega-Rocha, S.1    Gronenborn, B.2    Gronenborn, A.M.3    Campos-Olivas, R.4
  • 59
    • 33847235317 scopus 로고    scopus 로고
    • Solution structure, divalent metal and DNA binding of the endonuclease domain from the replication initiation protein from porcine circovirus 2
    • Vega-Rocha, S., Byeon, I. J., Gronenborn, B., Gronenborn, A. M. & Campos-Olivas, R. Solution structure, divalent metal and DNA binding of the endonuclease domain from the replication initiation protein from porcine circovirus 2. J. Mol. Biol. 367, 473-487 (2007
    • (2007) J. Mol. Biol , vol.367 , pp. 473-487
    • Vega-Rocha, S.1    Byeon, I.J.2    Gronenborn, B.3    Gronenborn, A.M.4    Campos-Olivas, R.5
  • 60
    • 78650652308 scopus 로고    scopus 로고
    • A dimeric Rep protein initiates replication of a linear archaeal virus genome: Implications for the Rep mechanism and viral replication
    • Oke, M. et al. A dimeric Rep protein initiates replication of a linear archaeal virus genome: Implications for the Rep mechanism and viral replication. J. Virol. 85, 925-931 (2011
    • (2011) J. Virol , vol.85 , pp. 925-931
    • Oke, M.1
  • 61
    • 0028024632 scopus 로고
    • Active site of the replication protein of the rolling circle plasmid pC194
    • Noirot-Gros, M. F., Bidnenko, V. & Ehrlich, S. D. Active site of the replication protein of the rolling circle plasmid pC194. EMBO J. 13, 4412-4420 (1994
    • (1994) EMBO J. , vol.13 , pp. 4412-4420
    • Noirot-Gros, M.F.1    Bidnenko, V.2    Ehrlich, S.D.3
  • 62
    • 0030735429 scopus 로고    scopus 로고
    • How rolling circle plasmids control their copy number
    • Rasooly, A. & Rasooly, R. S. How rolling circle plasmids control their copy number. Trends Microbiol. 5, 440-446 (1997
    • (1997) Trends Microbiol , vol.5 , pp. 440-446
    • Rasooly, A.1    Rasooly, R.S.2
  • 63
    • 0029435124 scopus 로고
    • Geminivirus replication: Genetic and biochemical characterization of Rep protein function, a review
    • Laufs, J. et al. Geminivirus replication: Genetic and biochemical characterization of Rep protein function, a review. Biochimie 77, 765-773 (1995
    • (1995) Biochimie , vol.77 , pp. 765-773
    • Laufs, J.1
  • 64
    • 0004469657 scopus 로고
    • Sex in bacteria; genetic studies 1945-1952
    • Lederberg, J. & Tatum, E. L. Sex in bacteria; genetic studies, 1945-1952. Science 118, 169-175 (1953
    • (1953) Science , vol.118 , pp. 169-175
    • Lederberg, J.1    Tatum, E.L.2
  • 66
    • 80052333445 scopus 로고    scopus 로고
    • The repertoire of ICE in prokaryotes underscores the unity, diversity, and ubiquity of conjugation
    • Guglielmini, J., Quintais, L., Garcillan-Barcia, M. P., de la Cruz, F. & Rocha, E. P. The repertoire of ICE in prokaryotes underscores the unity, diversity, and ubiquity of conjugation. PLoS Genet. 7, e1002222 (2011
    • (2011) PLoS Genet , vol.7
    • Guglielmini, J.1    Quintais, L.2    Garcillan-Barcia, M.P.3    De La Cruz, F.4    Rocha, E.P.5
  • 68
    • 84876194345 scopus 로고    scopus 로고
    • Modular evolution of TnGBSs, a new family of integrative and conjugative elements associating insertion sequence transposition, plasmid replication, and conjugation for their spreading
    • Guerillot, R., Da Cunha, V., Sauvage, E., Bouchier, C. & Glaser, P. Modular evolution of TnGBSs, a new family of integrative and conjugative elements associating insertion sequence transposition, plasmid replication, and conjugation for their spreading. J. Bacteriol. 195, 1979-1990 (2013
    • (2013) J. Bacteriol , vol.195 , pp. 1979-1990
    • Guerillot, R.1    Da Cunha, V.2    Sauvage, E.3    Bouchier, C.4    Glaser, P.5
  • 69
    • 70349095361 scopus 로고    scopus 로고
    • Integrative and sequence characteristics of a novel genetic element ice6013 in staphylococcus aureus
    • Smyth, D. S. & Robinson, D. A. Integrative and sequence characteristics of a novel genetic element, ICE6013, in Staphylococcus aureus. J. Bacteriol. 191, 5964-5975 (2009
    • (2009) J. Bacteriol , vol.191 , pp. 5964-5975
    • Smyth, D.S.1    Robinson, D.A.2
  • 70
    • 33644862811 scopus 로고    scopus 로고
    • The integrase of the conjugative transposon Tn916 directs strand- and sequence-specific cleavage of the origin of conjugal transfer, oriT, by the endonuclease Orf20
    • Rocco, J. M. & Churchward, G. The integrase of the conjugative transposon Tn916 directs strand- and sequence-specific cleavage of the origin of conjugal transfer, oriT, by the endonuclease Orf20. J. Bacteriol. 188, 2207-2213 (2006
    • (2006) J. Bacteriol , vol.188 , pp. 2207-2213
    • Rocco, J.M.1    Churchward, G.2
  • 71
    • 74349093158 scopus 로고    scopus 로고
    • Autonomous plasmid-like replication of a conjugative transposon
    • Lee, C. A., Babic, A. & Grossman, A. D. Autonomous plasmid-like replication of a conjugative transposon. Mol. Microbiol. 75, 268-279 (2010
    • (2010) Mol. Microbiol , vol.75 , pp. 268-279
    • Lee, C.A.1    Babic, A.2    Grossman, A.D.3
  • 72
    • 28044438533 scopus 로고    scopus 로고
    • Site-specific recombinase and integrase activities of a conjugative relaxase in recipient cells
    • Draper, O., Cesar, C. E., Machon, C., de la Cruz, F. & Llosa, M. Site-specific recombinase and integrase activities of a conjugative relaxase in recipient cells. Proc. Natl Acad. Sci. USA 102, 16385-16390 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16385-16390
    • Draper, O.1    Cesar, C.E.2    Machon, C.3    De La Cruz, F.4    Llosa, M.5
  • 73
    • 0017840933 scopus 로고
    • The requirements for conjugal DNA synthesis in the donor strain during F lac transfer
    • Kingsman, A. & Willetts, N. The requirements for conjugal DNA synthesis in the donor strain during F lac transfer. J. Mol. Biol. 122, 287-300 (1978
    • (1978) J. Mol. Biol , vol.122 , pp. 287-300
    • Kingsman, A.1    Willetts, N.2
  • 74
    • 77957221192 scopus 로고    scopus 로고
    • The mechanism and control of DNA transfer by the conjugative relaxase of resistance plasmid pCU1
    • Nash, R. P., Habibi, S., Cheng, Y., Lujan, S. A. & Redinbo, M. R. The mechanism and control of DNA transfer by the conjugative relaxase of resistance plasmid pCU1. Nucleic Acids Res. 38, 5929-5943 (2010
    • (2010) Nucleic Acids Res , vol.38 , pp. 5929-5943
    • Nash, R.P.1    Habibi, S.2    Cheng, Y.3    Lujan, S.A.4    Redinbo, M.R.5
  • 75
    • 33846413933 scopus 로고    scopus 로고
    • The structure of the minimal relaxase domain of MobA at 2.1 ? resolution
    • Monzingo, A. F., Ozburn, A., Xia, S., Meyer, R. J. & Robertus, J. D. The structure of the minimal relaxase domain of MobA at 2.1 ? resolution. J. Mol. Biol. 366, 165-178 (2007
    • (2007) J. Mol. Biol , vol.366 , pp. 165-178
    • Monzingo, A.F.1    Ozburn, A.2    Xia, S.3    Meyer, R.J.4    Robertus, J.D.5
  • 76
    • 36349014398 scopus 로고    scopus 로고
    • Roles of active site residues and the HUH motif of the F plasmid TraI relaxase
    • Larkin, C., Haft, R. J. F., Harley, M. J., Traxler, B. & Schildbach, J. F. Roles of active site residues and the HUH motif of the F plasmid TraI relaxase. J. Biol. Chem. 282, 33707-33713 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 33707-33713
    • Larkin, C.1    Haft, R.J.F.2    Harley, M.J.3    Traxler, B.4    Schildbach, J.F.5
  • 77
    • 34548098369 scopus 로고    scopus 로고
    • Analysis of DNA processing reactions in bacterial conjugation by using suicide oligonucleotides
    • Gonzalez-Perez, B. et al. Analysis of DNA processing reactions in bacterial conjugation by using suicide oligonucleotides. EMBO J. 26, 3847-3857 (2007
    • (2007) EMBO J. , vol.26 , pp. 3847-3857
    • Gonzalez-Perez, B.1
  • 78
    • 79954444578 scopus 로고    scopus 로고
    • Tracking F plasmid TraI relaxase processing reactions provides insight into F plasmid transfer
    • Dostal, L., Shao, S. & Schildbach, J. F. Tracking F plasmid TraI relaxase processing reactions provides insight into F plasmid transfer. Nucleic Acids Res. 39, 2658-2670 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. 2658-2670
    • Dostal, L.1    Shao, S.2    Schildbach, J.F.3
  • 79
    • 77950587244 scopus 로고    scopus 로고
    • Relaxase DNA binding and cleavage are two distinguishable steps in conjugative DNA processing that involve different sequence elements of the nic site
    • Lucas, M. et al. Relaxase DNA binding and cleavage are two distinguishable steps in conjugative DNA processing that involve different sequence elements of the nic site. J. Biol. Chem. 285, 8918-8926 (2010
    • (2010) J. Biol. Chem , vol.285 , pp. 8918-8926
    • Lucas, M.1
  • 80
    • 0023493060 scopus 로고
    • Two domains at the origin are required for replication and maintenance of broad-host-range plasmid R1162
    • Kim, Y. J., Lin, L. S. & Meyer, R. J. Two domains at the origin are required for replication and maintenance of broad-host-range plasmid R1162. J. Bacteriol. 169, 5870-5872 (1987
    • (1987) J. Bacteriol , vol.169 , pp. 5870-5872
    • Kim, Y.J.1    Lin, L.S.2    Meyer, R.J.3
  • 81
    • 0028049489 scopus 로고
    • Concerted action of three distinct domains in the DNA cleaving-joining reaction catalyzed by relaxase (TraI) of conjugative plasmid RP4
    • Pansegrau, W., Schroder, W. & Lanka, E. Concerted action of three distinct domains in the DNA cleaving-joining reaction catalyzed by relaxase (TraI) of conjugative plasmid RP4. J. Biol. Chem. 269, 2782-2789 (1994
    • (1994) J. Biol. Chem , vol.269 , pp. 2782-2789
    • Pansegrau, W.1    Schroder, W.2    Lanka, E.3
  • 82
    • 67650753562 scopus 로고    scopus 로고
    • And conjugative mobilization of broad host-range IncQ plasmids
    • Meyer, R. Replication and conjugative mobilization of broad host-range IncQ plasmids. Plasmid 62, 57-70 (2009
    • (2009) Plasmid , vol.62 , pp. 57-70
    • Meyer R. Replication1
  • 83
    • 66049164017 scopus 로고    scopus 로고
    • Structure and function of primase RepB' encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode
    • Geibel, S., Banchenko, S., Engel, M., Lanka, E. & Saenger, W. Structure and function of primase RepB' encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode. Proc. Natl Acad. Sci. USA 106, 7810-7815 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7810-7815
    • Geibel, S.1    Banchenko, S.2    Engel, M.3    Lanka, E.4    Saenger, W.5
  • 84
    • 0024357142 scopus 로고
    • RepB' is required in trans for the two single-strand DNA initiation signals in oriV of plasmid RSF1010
    • Honda, Y., Sakai, H., Komano, T. & Bagdasarian, M. RepB' is required in trans for the two single-strand DNA initiation signals in oriV of plasmid RSF1010. Gene 80, 155-159 (1989
    • (1989) Gene , vol.80 , pp. 155-159
    • Honda, Y.1    Sakai, H.2    Komano, T.3    Bagdasarian, M.4
  • 85
    • 0028199682 scopus 로고
    • Differential roles of the transposon termini in IS91 transposition
    • Mendiola, M. V., Bernales, I. & de la Cruz, F. Differential roles of the transposon termini in IS91 transposition. Proc. Natl Acad. Sci. USA 91, 1922-1926 (1994
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1922-1926
    • Mendiola, M.V.1    Bernales, I.2    De La Cruz, F.3
  • 86
    • 0020503418 scopus 로고
    • IS200: A Salmonella-specific insertion sequence
    • Lam, S. & Roth, J. R. IS200: A Salmonella-specific insertion sequence. Cell 34, 951-960 (1983
    • (1983) Cell , vol.34 , pp. 951-960
    • Lam, S.1    Roth, J.R.2
  • 87
    • 0036154792 scopus 로고    scopus 로고
    • Transposable element ISHp608 of Helicobacter pylori: Nonrandom geographic distribution, functional organization, and insertion specificity
    • Kersulyte, D. et al. Transposable element ISHp608 of Helicobacter pylori: Nonrandom geographic distribution, functional organization, and insertion specificity. J. Bacteriol. 184, 992-1002 (2002
    • (2002) J. Bacteriol , vol.184 , pp. 992-1002
    • Kersulyte, D.1
  • 88
    • 0347363563 scopus 로고    scopus 로고
    • Characterization and distribution of IS8301 in the radioresistant bacterium Deinococcus radiodurans
    • Islam, S. M. et al. Characterization and distribution of IS8301 in the radioresistant bacterium Deinococcus radiodurans. Genes Genet. Syst. 78, 319-327 (2003
    • (2003) Genes Genet. Syst , vol.78 , pp. 319-327
    • Islam, S.M.1
  • 89
    • 77955332264 scopus 로고    scopus 로고
    • Single-stranded DNA transposition is coupled to host replication
    • Ton-Hoang, B. et al. Single-stranded DNA transposition is coupled to host replication. Cell 142, 398-408 (2010
    • (2010) Cell , vol.142 , pp. 398-408
    • Ton-Hoang, B.1
  • 90
    • 76749140477 scopus 로고    scopus 로고
    • Irradiation-induced Deinococcus radiodurans genome fragmentation triggers transposition of a single resident insertion sequence
    • Pasternak, C. et al. Irradiation-induced Deinococcus radiodurans genome fragmentation triggers transposition of a single resident insertion sequence. PLoS Genet. 6, e1000799 (2010
    • (2010) PLoS Genet , vol.6
    • Pasternak, C.1
  • 91
    • 33749533999 scopus 로고    scopus 로고
    • Reassembly of shattered chromosomes in Deinococcus radiodurans
    • Zahradka, K. et al. Reassembly of shattered chromosomes in Deinococcus radiodurans. Nature 443, 569-573 (2006
    • (2006) Nature , vol.443 , pp. 569-573
    • Zahradka, K.1
  • 92
    • 80455178800 scopus 로고    scopus 로고
    • Reconstitution of a functional IS608 single-strand transpososome: Role of non-canonical base pairing
    • He, S. et al. Reconstitution of a functional IS608 single-strand transpososome: Role of non-canonical base pairing. Nucleic Acids Res. 39, 8503-8512 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. 8503-8512
    • He, S.1
  • 93
    • 66449109201 scopus 로고    scopus 로고
    • Resetting the site: Redirecting integration of an insertion sequence in a predictable way
    • Guynet, C. et al. Resetting the site: Redirecting integration of an insertion sequence in a predictable way. Mol. Cell 34, 612-619 (2009
    • (2009) Mol. Cell , vol.34 , pp. 612-619
    • Guynet, C.1
  • 94
    • 0036848622 scopus 로고    scopus 로고
    • Distribution of IS91 family insertion sequences in bacterial genomes: Evolutionary implications
    • Garcillan-Barcia, M. P. & de la Cruz, F. Distribution of IS91 family insertion sequences in bacterial genomes: Evolutionary implications. FEMS Microbiol. Ecol. 42, 303-313 (2002
    • (2002) FEMS Microbiol. Ecol , vol.42 , pp. 303-313
    • Garcillan-Barcia, M.P.1    De La Cruz, F.2
  • 96
    • 62349089758 scopus 로고    scopus 로고
    • Molecular domestication of transposable elements: From detrimental parasites to useful host genes
    • Sinzelle, L., Izsvak, Z. & Ivics, Z. Molecular domestication of transposable elements: From detrimental parasites to useful host genes. Cell. Mol. Life Sci. 66, 1073-1093 (2009
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 1073-1093
    • Sinzelle, L.1    Izsvak, Z.2    Ivics, Z.3
  • 97
    • 34249003761 scopus 로고    scopus 로고
    • 1H, 13C, and 15N NMR assignment of the master Rep protein nuclease domain from the nanovirus FBNYV
    • Vega-Rocha, S., Gronenborn, A. M., Gronenborn, B. & Campos-Olivas, R. 1H, 13C, and 15N NMR assignment of the master Rep protein nuclease domain from the nanovirus FBNYV. J. Biomol. NMR 38, 169 (2007
    • (2007) J. Biomol. NMR , vol.38 , pp. 169
    • Vega-Rocha, S.1    Gronenborn, A.M.2    Gronenborn, B.3    Campos-Olivas, R.4
  • 98
    • 0038687623 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization
    • Varsaki, A., Lucas, M., Afendra, A. S., Drainas, C. & de la Cruz, F. Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization. Mol. Microbiol. 48, 481-493 (2003
    • (2003) Mol. Microbiol , vol.48 , pp. 481-493
    • Varsaki, A.1    Lucas, M.2    Afendra, A.S.3    Drainas, C.4    De La Cruz, F.5
  • 99
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G. & Dreyfuss, G. Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621 (1994
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 100
    • 0017332435 scopus 로고
    • A mechanism of duplex DNA replication revealed by enzymatic studies of phage ?X174: Catalytic strand separation in advance of replication
    • Scott, J. F., Eisenberg, S., Bertsch, L. L. & Kornberg, A. A mechanism of duplex DNA replication revealed by enzymatic studies of phage ?X174: Catalytic strand separation in advance of replication. Proc. Natl Acad. Sci. USA 74, 193-197 (1977
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 193-197
    • Scott, J.F.1    Eisenberg, S.2    Bertsch, L.L.3    Kornberg, A.4
  • 101
    • 0025214094 scopus 로고
    • Site-specific integration by adeno-associated virus
    • Kotin, R. M. et al. Site-specific integration by adeno-associated virus. Proc. Natl Acad. Sci. USA 87, 2211-2215 (1990
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2211-2215
    • Kotin, R.M.1
  • 102
    • 0030947409 scopus 로고    scopus 로고
    • The Rep78 gene product of adeno-associated virus (AAV) self-associates to form a hexameric complex in the presence of AAV ori sequences
    • Smith, R. H., Spano, A. J. & Kotin, R. M. The Rep78 gene product of adeno-associated virus (AAV) self-associates to form a hexameric complex in the presence of AAV ori sequences. J. Virol. 71, 4461-4471 (1997
    • (1997) J. Virol , vol.71 , pp. 4461-4471
    • Smith, R.H.1    Spano, A.J.2    Kotin, R.M.3
  • 103
    • 70049085266 scopus 로고    scopus 로고
    • DNA structure modulates the oligomerization properties of the AAV initiator protein Rep68
    • Mansilla-Soto, J. et al. DNA structure modulates the oligomerization properties of the AAV initiator protein Rep68. PLoS Pathog. 5, e1000513 (2009
    • (2009) PLoS Pathog , vol.5
    • Mansilla-Soto, J.1
  • 104
    • 10944269753 scopus 로고    scopus 로고
    • Integration of adeno-associated virus (AAV) and recombinant AAV vectors
    • McCarty, D. M., Young, S. M. Jr & Samulski, R. J. Integration of adeno-associated virus (AAV) and recombinant AAV vectors. Annu. Rev. Genet. 38, 819-845 (2004
    • (2004) Annu. Rev. Genet , vol.38 , pp. 819-845
    • McCarty, D.M.1    Young Jr., S.M.2    Samulski, R.J.3
  • 105
    • 33750485033 scopus 로고    scopus 로고
    • A new domain of conjugative relaxase TrwC responsible for efficient oriT-specific recombination on minimal target sequences
    • Cesar, C. E., Machon, C., de la Cruz, F. & Llosa, M. A new domain of conjugative relaxase TrwC responsible for efficient oriT-specific recombination on minimal target sequences. Mol. Microbiol. 62, 984-996 (2006
    • (2006) Mol. Microbiol , vol.62 , pp. 984-996
    • Cesar, C.E.1    Machon, C.2    De La Cruz, F.3    Llosa, M.4
  • 106
    • 37449007751 scopus 로고    scopus 로고
    • TrwC mediated site-specific recombination is controlled by host factors altering local DNA topology
    • Cesar, C. E. & Llosa, M. TrwC mediated site-specific recombination is controlled by host factors altering local DNA topology. J. Bacteriol. 189, 9037-9043 (2007
    • (2007) J. Bacteriol , vol.189 , pp. 9037-9043
    • Cesar, C.E.1    Llosa, M.2
  • 107
    • 84856094543 scopus 로고    scopus 로고
    • Site-specific integration of foreign DNA into minimal bacterial and human target sequences mediated by a conjugative relaxase
    • Agundez, L., Gonzalez-Prieto, C., Machon, C. & Llosa, M. Site-specific integration of foreign DNA into minimal bacterial and human target sequences mediated by a conjugative relaxase. PLoS ONE 7, e31047 (2012
    • (2012) PLoS ONE , vol.7
    • Agundez, L.1    Gonzalez-Prieto, C.2    Machon, C.3    Llosa, M.4
  • 108
    • 79251612164 scopus 로고    scopus 로고
    • Nuclear targeting of a bacterial integrase that mediates site-specific recombination between bacterial and human target sequences
    • Agundez, L. et al. Nuclear targeting of a bacterial integrase that mediates site-specific recombination between bacterial and human target sequences. Appl. Environ. Microbiol. 77, 201-210 (2011
    • (2011) Appl. Environ. Microbiol , vol.77 , pp. 201-210
    • Agundez, L.1
  • 109
    • 80052291791 scopus 로고    scopus 로고
    • Conjugative DNA transfer into human cells by the VirB/VirD4 type IV secretion system of the bacterial pathogen Bartonella henselae
    • Schröder, G., Schuelein, R., Quebatte, M. & Dehio, C. Conjugative DNA transfer into human cells by the VirB/VirD4 type IV secretion system of the bacterial pathogen Bartonella henselae. Proc. Natl Acad. Sci. USA 108, 14643-14648 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14643-14648
    • Schröder, G.1    Schuelein, R.2    Quebatte, M.3    Dehio, C.4
  • 110
    • 80655146184 scopus 로고    scopus 로고
    • Transfer of R388 derivatives by a pathogenesis-associated type IV secretion system into both bacteria and human cells
    • Fernandez-Gonzalez, E. et al. Transfer of R388 derivatives by a pathogenesis-associated type IV secretion system into both bacteria and human cells. J. Bacteriol. 193, 6257-6265 (2011
    • (2011) J. Bacteriol , vol.193 , pp. 6257-6265
    • Fernandez-Gonzalez, E.1
  • 111
    • 84876699118 scopus 로고    scopus 로고
    • HUH site-specific recombinases for targeted modification of the human genome
    • González-Prieto, C., Agúndez, L., Linden, R. M. & Llosa, M. HUH site-specific recombinases for targeted modification of the human genome. Trends Biotechnol. 31, 305-312 (2013
    • (2013) Trends Biotechnol , vol.31 , pp. 305-312
    • González-Prieto, C.1    Agúndez, L.2    Linden, R.M.3    Llosa, M.4
  • 112
    • 33846931279 scopus 로고    scopus 로고
    • Massive amplification of rolling-circle transposons in the lineage of the bat Myotis lucifugus
    • Pritham, E. J. & Feschotte, C. Massive amplification of rolling-circle transposons in the lineage of the bat Myotis lucifugus. Proc. Natl Acad. Sci. USA 104, 1895-1900 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1895-1900
    • Pritham, E.J.1    Feschotte, C.2
  • 113
    • 34848876954 scopus 로고    scopus 로고
    • Helitrons on a roll: Eukaryotic rolling-circle transposons
    • Kapitonov, V. V. & Jurka, J. Helitrons on a roll: Eukaryotic rolling-circle transposons. Trends Genet. 23, 521-529 (2007
    • (2007) Trends Genet , vol.23 , pp. 521-529
    • Kapitonov, V.V.1    Jurka, J.2
  • 114
    • 0035979218 scopus 로고    scopus 로고
    • Treasures in the attic: Rolling circle transposons discovered in eukaryotic genomes
    • Feschotte, C. & Wessler, S. R. Treasures in the attic: Rolling circle transposons discovered in eukaryotic genomes. Proc. Natl Acad. Sci. USA 98, 8923-8924 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8923-8924
    • Feschotte, C.1    Wessler, S.R.2
  • 115
    • 0019947094 scopus 로고
    • A novel intercistronic regulatory element of prokaryotic operons
    • Higgins, C. F., Ames, G. F., Barnes, W. M., Clement,J. M. & Hofnung, M. A novel intercistronic regulatory element of prokaryotic operons. Nature 298, 760-762 (1982
    • (1982) Nature , vol.298 , pp. 760-762
    • Higgins, C.F.1    Ames, G.F.2    Barnes, W.M.3    Clement, J.M.4    Hofnung, M.5
  • 116
    • 0343114274 scopus 로고    scopus 로고
    • Short palindromic repetitive DNA elements in enterobacteria: A survey
    • Bachellier, S., Clément, J. M. & Hofnung, M. Short palindromic repetitive DNA elements in enterobacteria: A survey. Res. Microbiol. 150, 627-639 (1999
    • (1999) Res. Microbiol , vol.150 , pp. 627-639
    • Bachellier, S.1    Clément, J.M.2    Hofnung, M.3
  • 117
    • 76749135815 scopus 로고    scopus 로고
    • Identification and characterization of repetitive extragenic palindromes (REP)-associated tyrosine transposases: Implications for REP evolution and dynamics in bacterial genomes
    • Nunvar, J., Huckova, T. & Licha, I. Identification and characterization of repetitive extragenic palindromes (REP)-associated tyrosine transposases: Implications for REP evolution and dynamics in bacterial genomes. BMC Genomics 11, 44 (2010
    • (2010) BMC Genomics , vol.11 , Issue.44
    • Nunvar, J.1    Huckova, T.2    Licha, I.3
  • 118
    • 79959843994 scopus 로고    scopus 로고
    • Within-genome evolution of REPINs: A new family of miniature mobile DNA in bacteria
    • Bertels, F. & Rainey, P. B. Within-genome evolution of REPINs: A new family of miniature mobile DNA in bacteria. PLoS Genet. 7, e1002132 (2011
    • (2011) PLoS Genet , vol.7
    • Bertels, F.1    Rainey, P.B.2
  • 119
    • 0033933847 scopus 로고    scopus 로고
    • A chimeric ribozyme in Clostridium difficile combines features of group I introns and insertion elements
    • Braun, V. et al. A chimeric ribozyme in Clostridium difficile combines features of group I introns and insertion elements. Mol. Microbiol. 36, 1447-1459 (2000 Digestive and Kidney Diseases
    • (2000) Mol. Microbiol , vol.36 , pp. 1447-1459
    • Braun, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.