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Volumn 17, Issue 6, 2010, Pages 325-342

Conflicts targeting epigenetic systems and their resolution by cell death: Novel concepts for methyl-specific and other restriction systems

Author keywords

epigenetic DNA methylation; intragenomic conflict; McrBC; programmed cell death; restriction modification system

Indexed keywords

DEOXYRIBONUCLEASE; DNA HOMOLOG; DNA METHYLTRANSFERASE; RESTRICTION ENDONUCLEASE;

EID: 78649821044     PISSN: 13402838     EISSN: 17561663     Source Type: Journal    
DOI: 10.1093/dnares/dsq027     Document Type: Review
Times cited : (51)

References (144)
  • 1
    • 57649174743 scopus 로고    scopus 로고
    • Cell death upon epigenetic genome methylation: A novel function of methyl-specific deoxyribonucleases
    • Fukuda, E., Kaminska, K.H., Bujnicki, J.M. and Kobayashi, I. 2008, Cell death upon epigenetic genome methylation: a novel function of methyl-specific deoxyribonucleases, Genome Biol., 9, R163.
    • (2008) Genome Biol. , vol.9
    • Fukuda, E.1    Kaminska, K.H.2    Bujnicki, J.M.3    Kobayashi, I.4
  • 2
    • 0032697888 scopus 로고    scopus 로고
    • Mammalian (cytosine-5) methyltransferases cause genomic DNA methylation and lethality in Drosophila
    • Lyko, F., Ramsahoye, B.H., Kashevsky, H., et al. 1999, Mammalian (cytosine-5) methyltransferases cause genomic DNA methylation and lethality in Drosophila, Nat. Genet., 23, 363-6.
    • (1999) Nat. Genet. , vol.23 , pp. 363-6
    • Lyko, F.1    Ramsahoye, B.H.2    Kashevsky, H.3
  • 3
    • 0036594258 scopus 로고    scopus 로고
    • Exogenous expression of mouse Dnmt3 induces apoptosis in Xenopus early embryos
    • Kimura, H., Suetake, I. and Tajima, S. 2002, Exogenous expression of mouse Dnmt3 induces apoptosis in Xenopus early embryos, J. Biochem., 131, 933-41.
    • (2002) J. Biochem. , vol.131 , pp. 933-41
    • Kimura, H.1    Suetake, I.2    Tajima, S.3
  • 4
    • 33747884339 scopus 로고    scopus 로고
    • DNA damage-induced cell death by apoptosis
    • Roos, W.P. and Kaina, B. 2006, DNA damage-induced cell death by apoptosis, Trends Mol. Med., 12, 440-50.
    • (2006) Trends Mol. Med. , vol.12 , pp. 440-50
    • Roos, W.P.1    Kaina, B.2
  • 5
    • 0019248608 scopus 로고
    • Modified bases in bacteriophage DNAs
    • Warren, R.A. 1980, Modified bases in bacteriophage DNAs, Annu. Rev. Microbiol., 34, 137-58.
    • (1980) Annu. Rev. Microbiol. , vol.34 , pp. 137-58
    • Warren, R.A.1
  • 6
    • 58049217393 scopus 로고    scopus 로고
    • Phage phi29 protein p56 prevents viral DNA replication impairment caused by uracil excision activity of uracil-DNA glycosylase
    • Serrano-Heras, G., Bravo, A. and Salas, M. 2008, Phage phi29 protein p56 prevents viral DNA replication impairment caused by uracil excision activity of uracil-DNA glycosylase, Proc. Natl Acad. Sci. USA, 105, 19044-9.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19044-9
    • Serrano-Heras, G.1    Bravo, A.2    Salas, M.3
  • 7
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones, P.A. and Baylin, S.B. 2002, The fundamental role of epigenetic events in cancer, Nat. Rev. Genet., 3, 415-28.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 415-28
    • Jones, P.A.1    Baylin, S.B.2
  • 8
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epige-netic memory
    • Bird, A. 2002, DNA methylation patterns and epige-netic memory, Genes Dev., 16, 6-21.
    • (2002) Genes Dev. , vol.16 , pp. 6-21
    • Bird, A.1
  • 9
    • 13844320649 scopus 로고    scopus 로고
    • Aberrant DNA methylation as a cancer-inducing mechanism
    • Esteller, M. 2005, Aberrant DNA methylation as a cancer-inducing mechanism, Annu. Rev. Pharmacol. Toxicol., 45, 629-56.
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 629-56
    • Esteller, M.1
  • 10
    • 33646008874 scopus 로고    scopus 로고
    • N6-methyl-adenine: An epigenetic signal for DNA-protein interactions
    • Wion, D. and Casadesus, J. 2006, N6-methyl-adenine: an epigenetic signal for DNA-protein interactions, Nat. Rev. Microbiol., 4, 183-92.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 183-92
    • Wion, D.1    Casadesus, J.2
  • 11
    • 33749246561 scopus 로고    scopus 로고
    • Epigenetic gene regulation in the bacterial world
    • Collier, J
    • Casadesus, J. and Low, D. 2006, Epigenetic gene regulation in the bacterial world, Microbiol. Mol. Biol. Rev., 70, 830-56.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 830-56
    • Casadesus, J.1    Low, D.2
  • 12
    • 64349112326 scopus 로고    scopus 로고
    • Roles of DNA adenine methylation in host-pathogen interactions: Mismatch repair, transcriptional regulation, and more
    • Marinus, M.G. and Casadesus, J. 2009, Roles of DNA adenine methylation in host-pathogen interactions: mismatch repair, transcriptional regulation, and more, FEMS Microbiol. Rev., 33, 488-503.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 488-503
    • Marinus, M.G.1    Casadesus, J.2
  • 13
    • 19444361995 scopus 로고    scopus 로고
    • Genomic imprinting and methyl-ation: Epigenetic canalization and conflict
    • Wilkins, J.F. 2005, Genomic imprinting and methyl-ation: epigenetic canalization and conflict, Trends Genet., 21, 356-65.
    • (2005) Trends Genet. , vol.21 , pp. 356-65
    • Wilkins, J.F.1
  • 14
    • 17344370012 scopus 로고    scopus 로고
    • The phase-varion: A genetic system controlling coordinated, random switching of expression of multiple genes
    • Srikhanta, Y.N., Maguire, T.L., Stacey, K.J., Grimmond, S.M. and Jennings, M.P. 2005, The phase-varion: a genetic system controlling coordinated, random switching of expression of multiple genes, Proc. Natl Acad. Sci. USA, 102, 5547-51.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5547-51
    • Srikhanta, Y.N.1    Maguire, T.L.2    Stacey, K.J.3    Grimmond, S.M.4    Jennings, M.P.5
  • 15
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • Li, E., Bestor, T.H. and Jaenisch, R. 1992, Targeted mutation of the DNA methyltransferase gene results in embryonic lethality, Cell, 69, 915-26.
    • (1992) Cell , vol.69 , pp. 915-26
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 16
    • 1842499716 scopus 로고    scopus 로고
    • Windows for sex-specific methylation marked by DNA methyltransfer-ase expression profiles in mouse germ cells
    • La Salle, S., Mertineit, C., Taketo, T., Moens, P.B., Bestor, T.H. and Trasler, J.M. 2004, Windows for sex-specific methylation marked by DNA methyltransfer-ase expression profiles in mouse germ cells, Dev. Biol., 268, 403-15.
    • (2004) Dev. Biol. , vol.268 , pp. 403-15
    • La Salle, S.1    Mertineit, C.2    Taketo, T.3    Moens, P.B.4    Bestor, T.H.5    Trasler, J.M.6
  • 17
    • 0035837378 scopus 로고    scopus 로고
    • Mobilization of transposons by a mutation abolishing full DNA methylation in Arabidopsis
    • Miura, A., Yonebayashi, S., Watanabe, K., Toyama, T., Shimada, H. and Kakutani, T. 2001, Mobilization of transposons by a mutation abolishing full DNA methylation in Arabidopsis, Nature, 411, 212-4.
    • (2001) Nature , vol.411 , pp. 212-4
    • Miura, A.1    Yonebayashi, S.2    Watanabe, K.3    Toyama, T.4    Shimada, H.5    Kakutani, T.6
  • 18
    • 0026332291 scopus 로고
    • Evidence for horizontal gene transfer in Escherichia coli speciation
    • Medigue, C., Rouxel, T., Vigier, P., Henaut, A. and Danchin, A. 1991, Evidence for horizontal gene transfer in Escherichia coli speciation, J. Mol. Biol., 222, 851-6.
    • (1991) J. Mol. Biol. , vol.222 , pp. 851-6
    • Medigue, C.1    Rouxel, T.2    Vigier, P.3    Henaut, A.4    Danchin, A.5
  • 19
    • 0021307706 scopus 로고
    • DNA methyl-transferases of Bacillus subtilis and its bacteriophages
    • Gunthert, U. and Trautner, T.A. 1984, DNA methyl-transferases of Bacillus subtilis and its bacteriophages, Curr. Top Microbiol. Immunol., 108, 11-22.
    • (1984) Curr. Top Microbiol. Immunol. , vol.108 , pp. 11-22
    • Gunthert, U.1    Trautner, T.A.2
  • 20
    • 0033571544 scopus 로고    scopus 로고
    • Molecular evolution of DNA-(cytosine-N4) methyltransferases: Evidence for their polyphyletic origin
    • Bujnicki, J.M. and Radlinska, M. 1999, Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin, Nucleic Acids Res., 27, 4501-9.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4501-9
    • Bujnicki, J.M.1    Radlinska, M.2
  • 21
    • 0034707207 scopus 로고    scopus 로고
    • Diversity of restriction-modification gene homologues in Helicobacter pylori
    • Nobusato, A., Uchiyama, I. and Kobayashi, I. 2000, Diversity of restriction-modification gene homologues in Helicobacter pylori, Gene, 259, 89-98.
    • (2000) Gene , vol.259 , pp. 89-98
    • Nobusato, A.1    Uchiyama, I.2    Kobayashi, I.3
  • 22
    • 0034707190 scopus 로고    scopus 로고
    • Insertion with long target duplication: A mechanism for gene mobility suggested from comparison of two related bacterial genomes
    • Nobusato, A., Uchiyama, I., Ohashi, S. and Kobayashi, I. 2000, Insertion with long target duplication: a mechanism for gene mobility suggested from comparison of two related bacterial genomes, Gene, 259, 99-108.
    • (2000) Gene , vol.259 , pp. 99-108
    • Nobusato, A.1    Uchiyama, I.2    Ohashi, S.3    Kobayashi, I.4
  • 23
    • 0035883519 scopus 로고    scopus 로고
    • Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution
    • Kobayashi, I. 2001, Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution, Nucleic Acids Res., 29, 3742-56.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3742-56
    • Kobayashi, I.1
  • 24
  • 25
    • 17044403057 scopus 로고    scopus 로고
    • Type II restriction endonucleases: Structure and mechanism
    • Pingoud, A., Fuxreiter, M., Pingoud, V. and Wende, W. 2005, Type II restriction endonucleases: structure and mechanism, Cell Mol. Life Sci., 62, 685-707.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 685-707
    • Pingoud, A.1    Fuxreiter, M.2    Pingoud, V.3    Wende, W.4
  • 26
    • 0037389511 scopus 로고    scopus 로고
    • A nomenclature for restriction enzymes, DNA methyl-transferases, homing endonucleases and their genes
    • Roberts, R.J., Belfort, M., Bestor, T., et al. 2003, A nomenclature for restriction enzymes, DNA methyl-transferases, homing endonucleases and their genes, Nucleic Acids Res., 31, 1805-12.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1805-12
    • Roberts, R.J.1    Belfort, M.2    Bestor, T.3
  • 27
    • 46349101158 scopus 로고    scopus 로고
    • Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses
    • Orlowski, J. and Bujnicki, J.M. 2008, Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses, Nucleic Acids Res., 36, 3552-69.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3552-69
    • Orlowski, J.1    Bujnicki, J.M.2
  • 28
    • 0023732866 scopus 로고
    • Model for how type i restriction enzymes select cleavage sites in DNA
    • Studier, F.W. and Bandyopadhyay, P.K. 1988, Model for how type I restriction enzymes select cleavage sites in DNA, Proc. Natl Acad. Sci. USA, 85, 4677-81.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4677-81
    • Studier, F.W.1    Bandyopadhyay, P.K.2
  • 29
    • 0016359197 scopus 로고    scopus 로고
    • Restriction of ltrp Bacteriophages by Escherichia coli K
    • Brammar, W.J., Murray, N.E. and Winton, S. 1999, Restriction of ltrp Bacteriophages by Escherichia coli K, J. Mol. Biol., 90, 633-47.
    • (1999) J. Mol. Biol. , vol.90 , pp. 633-47
    • Brammar, W.J.1    Murray, N.E.2    Winton, S.3
  • 30
    • 0033522512 scopus 로고    scopus 로고
    • DNA translocation blockage, a general mechanism of cleavage site selection by type i restriction enzymes
    • Janscak, P., MacWilliams, M.P., Sandmeier, U., Nagaraja, V. and Bickle, T.A. 1999, DNA translocation blockage, a general mechanism of cleavage site selection by type I restriction enzymes, EMBO J., 18, 2638-47.
    • (1999) EMBO J. , vol.18 , pp. 2638-47
    • Janscak, P.1    MacWilliams, M.P.2    Sandmeier, U.3    Nagaraja, V.4    Bickle, T.A.5
  • 32
    • 67649862214 scopus 로고    scopus 로고
    • Cleavage of a model DNA replication fork by a Type i restriction endonuclease
    • Ishikawa, K., Handa, N. and Kobayashi, I. 2009, Cleavage of a model DNA replication fork by a Type I restriction endonuclease, Nucleic Acids Res., 37, 3531-44.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3531-44
    • Ishikawa, K.1    Handa, N.2    Kobayashi, I.3
  • 33
    • 0001952059 scopus 로고
    • Linn, SM, Lloyd, RS and Roberts, R.J., eds Cold Spring Harbor Laboratory Press: New York
    • Bickle, T.A. 1993, In: Linn, SM, Lloyd, RS and Roberts, R.J., eds, Nucleases, Cold Spring Harbor Laboratory Press: New York, pp. 89-109.
    • (1993) Nucleases , pp. 89-109
    • Bickle, T.A.1
  • 34
    • 0035883536 scopus 로고    scopus 로고
    • Nucleoside triphosphate-dependent restriction enzymes
    • Dryden, D.T.F., Murray, N.E. and Rao, D.N. 2001, Nucleoside triphosphate-dependent restriction enzymes, Nucleic Acids Res., 29, 3728-41.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3728-41
    • Dryden, D.T.F.1    Murray, N.E.2    Rao, D.N.3
  • 35
    • 0029045067 scopus 로고
    • Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis
    • Meisel, A., Mackeldanz, P., Bickle, T.A., Kruger, D.H. and Schroeder, C. 1995, Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis, EMBO J., 14, 2958-66.
    • (1995) EMBO J. , vol.14 , pp. 2958-66
    • Meisel, A.1    MacKeldanz, P.2    Bickle, T.A.3    Kruger, D.H.4    Schroeder, C.5
  • 36
    • 3342967880 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA transloca-tion by the Type III restriction enzyme EcoP15I
    • Reich, S., Gossl, I., Reuter, M., Rabe, J.P. and Kruger, D.H. 2004, Scanning force microscopy of DNA transloca-tion by the Type III restriction enzyme EcoP15I, J. Mol. Biol., 341, 337-43.
    • (2004) J. Mol. Biol. , vol.341 , pp. 337-43
    • Reich, S.1    Gossl, I.2    Reuter, M.3    Rabe, J.P.4    Kruger, D.H.5
  • 37
    • 34547883904 scopus 로고    scopus 로고
    • Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping
    • Crampton, N., Yokokawa, M., Dryden, D.T.F., et al. 2007, Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping, Proc. Natl Acad. Sci. USA, 104, 12755-60.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12755-60
    • Crampton, N.1    Yokokawa, M.2    Dryden, D.T.F.3
  • 38
    • 34548105170 scopus 로고    scopus 로고
    • DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
    • Crampton, N., Roes, S., Dryden, D.T.F., Rao, D.N., Edwardson, J.M. and Henderson, R.M. 2007, DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes, EMBO J., 26, 3815-25.
    • (2007) EMBO J. , vol.26 , pp. 3815-25
    • Crampton, N.1    Roes, S.2    Dryden, D.T.F.3    Rao, D.N.4    Edwardson, J.M.5    Henderson, R.M.6
  • 39
    • 6344287290 scopus 로고    scopus 로고
    • Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme
    • Raghavendra, N.K. and Rao, D.N. 2004, Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme, Nucleic Acids Res., 32, 5703-11.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5703-11
    • Raghavendra, N.K.1    Rao, D.N.2
  • 40
    • 60549086229 scopus 로고    scopus 로고
    • Type III restriction enzymes communicate in 1D without looping between their target sites
    • Ramanathan, S.P., van Aelst, K., Sears, A., et al. 2009, Type III restriction enzymes communicate in 1D without looping between their target sites, Proc. Natl Acad. Sci. USA, 106, 1748-53.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1748-53
    • Ramanathan, S.P.1    Van Aelst, K.2    Sears, A.3
  • 41
    • 0026328384 scopus 로고
    • A novel activity in Escherichia coli K-12 that directs restriction of DNA modified at CG dinucleotides
    • Kelleher, J.E. and Raleigh, E.A. 1991, A novel activity in Escherichia coli K-12 that directs restriction of DNA modified at CG dinucleotides, J. Bacteriol., 173, 5220-23.
    • (1991) J. Bacteriol. , vol.173 , pp. 5220-23
    • Kelleher, J.E.1    Raleigh, E.A.2
  • 43
    • 77951229049 scopus 로고    scopus 로고
    • Differential binding of Escherichia coli McrA protein to DNA sequences that contain the dinucleotide m5CpG
    • Mulligan, E.A., Hatchwell, E., McCorkle, S.R. and Dunn, J.J. 2010, Differential binding of Escherichia coli McrA protein to DNA sequences that contain the dinucleotide m5CpG, Nucleic Acids Res., 38, 1997-2005.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1997-2005
    • Mulligan, E.A.1    Hatchwell, E.2    McCorkle, S.R.3    Dunn, J.J.4
  • 44
    • 52949085449 scopus 로고    scopus 로고
    • Cloning, purification and initial characterization of E. coli McrA, a putative 5-methylcytosine-specific nuclease
    • Mulligan, E.A. and Dunn, J.J. 2008, Cloning, purification and initial characterization of E. coli McrA, a putative 5-methylcytosine-specific nuclease, Protein Expr. Purif., 62, 98-103.
    • (2008) Protein Expr. Purif. , vol.62 , pp. 98-103
    • Mulligan, E.A.1    Dunn, J.J.2
  • 45
    • 17044401660 scopus 로고    scopus 로고
    • Pingoud, A., eds Springer-Verlag: Berlin
    • Kobayashi, I. 2004, In: Pingoud, A., eds, Restriction Endonucleases, Springer-Verlag: Berlin, pp. 19-62.
    • (2004) Restriction Endonucleases , pp. 19-62
    • Kobayashi, I.1
  • 46
    • 77952309317 scopus 로고    scopus 로고
    • Genome comparison and context analysis reveals putative mobile forms of restriction-modification systems and related rearrangements
    • Furuta, Y., Abe, K. and Kobayashi, I. 2010, Genome comparison and context analysis reveals putative mobile forms of restriction-modification systems and related rearrangements, Nucleic Acids Res., 38, 2428-43.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2428-43
    • Furuta, Y.1    Abe, K.2    Kobayashi, I.3
  • 48
    • 33747367212 scopus 로고    scopus 로고
    • Hyperthermophilic DNA methyltransferase M.PabI from the archaeon Pyrococcus abyssi
    • Watanabe, M., Yuzawa, H., Handa, N. and Kobayashi, I. 2006, Hyperthermophilic DNA methyltransferase M.PabI from the archaeon Pyrococcus abyssi, Appl. Environ. Microbiol., 72, 5367-75.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5367-75
    • Watanabe, M.1    Yuzawa, H.2    Handa, N.3    Kobayashi, I.4
  • 49
    • 77953268817 scopus 로고    scopus 로고
    • A putative mobile genetic element carrying a novel type IIF restriction-modification system (PluTI)
    • Khan, F., Furuta, Y., Kawai, M., et al. 2010, A putative mobile genetic element carrying a novel type IIF restriction-modification system (PluTI), Nucleic Acids Res., 38, 3019-30.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3019-30
    • Khan, F.1    Furuta, Y.2    Kawai, M.3
  • 50
    • 34247886142 scopus 로고    scopus 로고
    • Novel protein fold discovered in the PabI family of restriction enzymes
    • Miyazono, K., Watanabe, M., Kosinski, J., et al. 2007, Novel protein fold discovered in the PabI family of restriction enzymes, Nucleic Acids Res., 35, 1908-18.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1908-18
    • Miyazono, K.1    Watanabe, M.2    Kosinski, J.3
  • 51
    • 0037673304 scopus 로고    scopus 로고
    • Multiplication of a restriction-modification gene complex
    • Sadykov, M., Asami, Y., Niki, H., et al. 2003, Multiplication of a restriction-modification gene complex, Mol. Microbiol., 48, 417-27.
    • (2003) Mol. Microbiol. , vol.48 , pp. 417-27
    • Sadykov, M.1    Asami, Y.2    Niki, H.3
  • 52
    • 0035004723 scopus 로고    scopus 로고
    • Experimental genome evolution: Large-scale genome rearrangements associated with resistance to replacement of a chromosomal restriction- modification gene complex
    • Handa, N., Nakayama, Y., Sadykov, M. and Kobayashi, I. 2001, Experimental genome evolution: large-scale genome rearrangements associated with resistance to replacement of a chromosomal restriction-modification gene complex, Mol. Microbiol., 40, 932-40.
    • (2001) Mol. Microbiol. , vol.40 , pp. 932-40
    • Handa, N.1    Nakayama, Y.2    Sadykov, M.3    Kobayashi, I.4
  • 53
    • 0028803767 scopus 로고
    • Restriction-modification systems as genomic parasites in competition for specific sequences
    • Kusano, K., Naito, T., Handa, N. and Kobayashi, I. 1995, Restriction-modification systems as genomic parasites in competition for specific sequences, Proc. Natl Acad. Sci. USA, 92, 11095-99.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11095-99
    • Kusano, K.1    Naito, T.2    Handa, N.3    Kobayashi, I.4
  • 54
    • 0032568598 scopus 로고    scopus 로고
    • Restriction-modification gene complexes as selfish gene entities: Roles of a regulatory system in their establishment, maintenance, and apoptotic mutual exclusion
    • Nakayama, Y. and Kobayashi, I. 1998, Restriction-modification gene complexes as selfish gene entities: roles of a regulatory system in their establishment, maintenance, and apoptotic mutual exclusion, Proc. Natl Acad. Sci. USA, 95, 6442-7.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6442-7
    • Nakayama, Y.1    Kobayashi, I.2
  • 55
    • 0026633116 scopus 로고
    • Sequence and characterization of pvuIIR, the PvuII endonuclease gene, and of pvuIIC, its regulatory gene
    • Tao, T. and Blumenthal, R.M. 1992, Sequence and characterization of pvuIIR, the PvuII endonuclease gene, and of pvuIIC, its regulatory gene, J. Bacteriol., 174, 3395-8.
    • (1992) J. Bacteriol. , vol.174 , pp. 3395-8
    • Tao, T.1    Blumenthal, R.M.2
  • 56
    • 0027445666 scopus 로고
    • Autogenous regulation of the EcoRII methylase gene at the transcriptional level: Effect of 5-azacytidine
    • Som, S. and Friedman, S. 1993, Autogenous regulation of the EcoRII methylase gene at the transcriptional level: effect of 5-azacytidine, EMBO J., 12, 4297-303.
    • (1993) EMBO J. , vol.12 , pp. 4297-303
    • Som, S.1    Friedman, S.2
  • 57
    • 43349095997 scopus 로고    scopus 로고
    • Real-time kinetics of restriction-modification gene expression after entry into a new host cell
    • Mruk, I. and Blumenthal, R.M. 2008, Real-time kinetics of restriction-modification gene expression after entry into a new host cell, Nucleic Acids Res., 36, 2581-93.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2581-93
    • Mruk, I.1    Blumenthal, R.M.2
  • 58
    • 28844494799 scopus 로고    scopus 로고
    • Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site
    • Sawaya, M.R., Zhu, Z., Mersha, F., et al. 2005, Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site, Structure, 13, 1837-47.
    • (2005) Structure , vol.13 , pp. 1837-47
    • Sawaya, M.R.1    Zhu, Z.2    Mersha, F.3
  • 59
    • 49249132732 scopus 로고    scopus 로고
    • Structural analysis of the genetic switch that regulates the expression of restriction-modification genes
    • McGeehan, J.E., Streeter, S.D., Thresh, S.J., Ball, N., Ravelli, R.B. and Kneale, G.G. 2008, Structural analysis of the genetic switch that regulates the expression of restriction-modification genes, Nucleic Acids Res., 36, 4778-87.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4778-87
    • McGeehan, J.E.1    Streeter, S.D.2    Thresh, S.J.3    Ball, N.4    Ravelli, R.B.5    Kneale, G.G.6
  • 61
    • 0028901038 scopus 로고
    • Selfish behavior of restriction-modification systems
    • Naito, T., Kusano, K. and Kobayashi, I. 1995, Selfish behavior of restriction-modification systems, Science, 267, 897-9.
    • (1995) Science , vol.267 , pp. 897-9
    • Naito, T.1    Kusano, K.2    Kobayashi, I.3
  • 62
    • 25144458391 scopus 로고    scopus 로고
    • Stability of EcoRI restriction-modification enzymes in vivo differentiates the EcoRI restriction-modification system from other postsegregational cell killing systems
    • Ichige, A. and Kobayashi, I. 2005, Stability of EcoRI restriction-modification enzymes in vivo differentiates the EcoRI restriction-modification system from other postsegregational cell killing systems, J. Bacteriol., 187, 6612-21.
    • (2005) J. Bacteriol. , vol.187 , pp. 6612-21
    • Ichige, A.1    Kobayashi, I.2
  • 63
    • 25144449800 scopus 로고    scopus 로고
    • Funnell, B.E. and Phillips, G., eds ASM Press: Washington
    • Kobayashi, I. 2004, In: Funnell, B.E. and Phillips, G., eds, Plasmid Biology. ASM Press: Washington, pp. 105-44.
    • (2004) Plasmid Biology , pp. 105-44
    • Kobayashi, I.1
  • 64
    • 40449108318 scopus 로고    scopus 로고
    • Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity
    • Ohno, S., Handa, N., Watanabe-Matsui, M., Takahashi, N. and Kobayashi, I. 2008, Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity, J. Bacteriol., 190, 2039-49.
    • (2008) J. Bacteriol. , vol.190 , pp. 2039-49
    • Ohno, S.1    Handa, N.2    Watanabe-Matsui, M.3    Takahashi, N.4    Kobayashi, I.5
  • 65
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M.A., Dwyer, D.J., Hayete, B., Lawrence, C.A. and Collins, J.J. 2007, A common mechanism of cellular death induced by bactericidal antibiotics, Cell, 130, 797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 66
    • 77952884274 scopus 로고    scopus 로고
    • How antibiotics kill bacteria: From targets to networks
    • Kohanski, M.A., Dwyer, D.J. and Collins, J.J. 2010, How antibiotics kill bacteria: from targets to networks, Nat. Rev. Microbiol., 8, 423-35.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 423-35
    • Kohanski, M.A.1    Dwyer, D.J.2    Collins, J.J.3
  • 67
    • 66249109296 scopus 로고    scopus 로고
    • From damaged genome to cell surface: Transcriptome changes during bacterial cell death triggered by loss of a restriction-modification gene complex
    • Asakura, Y. and Kobayashi, I. 2009, From damaged genome to cell surface: transcriptome changes during bacterial cell death triggered by loss of a restriction-modification gene complex, Nucleic Acids Res., 37, 3021-31.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3021-31
    • Asakura, Y.1    Kobayashi, I.2
  • 68
    • 0034034023 scopus 로고    scopus 로고
    • Cellular responses to postsegregational killing by restriction- modification genes
    • Handa, N., Ichige, A., Kusano, K. and Kobayashi, I. 2000, Cellular responses to postsegregational killing by restriction-modification genes, J. Bacteriol., 182, 2218-29.
    • (2000) J. Bacteriol. , vol.182 , pp. 2218-29
    • Handa, N.1    Ichige, A.2    Kusano, K.3    Kobayashi, I.4
  • 69
    • 0036842035 scopus 로고    scopus 로고
    • A DNA methyltransferase can protect the genome from postdisturbance attack by a restriction-modification gene complex
    • Takahashi, N., Naito, Y., Handa, N. and Kobayashi, I. 2002, A DNA methyltransferase can protect the genome from postdisturbance attack by a restriction-modification gene complex, J. Bacteriol., 184, 6100-8.
    • (2002) J. Bacteriol. , vol.184 , pp. 6100-8
    • Takahashi, N.1    Naito, Y.2    Handa, N.3    Kobayashi, I.4
  • 70
    • 9644259059 scopus 로고    scopus 로고
    • Ca(2\+)-mediated site-specific DNA cleavage and suppression of promiscuous activity of KpnI restriction endonuclease
    • Chandrashekaran, S., Saravanan, M., Radha, D.R. and Nagaraja, V. 2004, Ca(2\+)-mediated site-specific DNA cleavage and suppression of promiscuous activity of KpnI restriction endonuclease, J. Biol. Chem., 279, 49736-40.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49736-40
    • Chandrashekaran, S.1    Saravanan, M.2    Radha, D.R.3    Nagaraja, V.4
  • 71
    • 0033745660 scopus 로고    scopus 로고
    • Evolution of sequence recognition by restriction-modification enzymes: Selective pressure for specificity decrease
    • Chinen, A., Naito, Y., Handa, N. and Kobayashi, I. 2000, Evolution of sequence recognition by restriction-modification enzymes: selective pressure for specificity decrease, Mol. Biol. Evol., 17, 1610-9.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1610-9
    • Chinen, A.1    Naito, Y.2    Handa, N.3    Kobayashi, I.4
  • 72
    • 0035147536 scopus 로고    scopus 로고
    • The proteolytic control of restriction activity in Escherichia coli K-12
    • Doronina, V.A. and Murray, N.E. 2001, The proteolytic control of restriction activity in Escherichia coli K-12, Mol. Microbiol., 39, 416-28.
    • (2001) Mol. Microbiol. , vol.39 , pp. 416-28
    • Doronina, V.A.1    Murray, N.E.2
  • 73
    • 0033578322 scopus 로고    scopus 로고
    • Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type i restriction enzymes
    • Makovets, S., Doronina, V.A. and Murray, N.E. 1999, Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes, Proc. Natl Acad. Sci. USA, 96, 9757-62.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9757-62
    • Makovets, S.1    Doronina, V.A.2    Murray, N.E.3
  • 74
    • 0348225084 scopus 로고    scopus 로고
    • Is modification sufficient to protect a bacterial chromosome from a resident restriction endonuclease?
    • Makovets, S., Powell, L.M., Titheradge, A.J., Blakely, G.W. and Murray, N.E. 2004, Is modification sufficient to protect a bacterial chromosome from a resident restriction endonuclease? Mol. Microbiol., 51, 135-47.
    • (2004) Mol. Microbiol. , vol.51 , pp. 135-47
    • Makovets, S.1    Powell, L.M.2    Titheradge, A.J.3    Blakely, G.W.4    Murray, N.E.5
  • 75
    • 28644433100 scopus 로고    scopus 로고
    • Dynamics of initiation, termination and reinitiation of DNA translocation by the motor protein EcoR124I
    • Seidel, R., Bloom, J.G., van Noort, J., et al. 2005, Dynamics of initiation, termination and reinitiation of DNA translocation by the motor protein EcoR124I, EMBO J., 24, 4188-97.
    • (2005) EMBO J. , vol.24 , pp. 4188-97
    • Seidel, R.1    Bloom, J.G.2    Van Noort, J.3
  • 76
    • 0034130457 scopus 로고    scopus 로고
    • Type i restriction systems: Sophisticated molecular machines (a legacy of Bertani and Weigle)
    • Murray, N.E. 2000, Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle), Microbiol. Mol. Biol. Rev., 64, 412-34.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 412-34
    • Murray, N.E.1
  • 77
    • 0035724134 scopus 로고    scopus 로고
    • Recombinational repair of chromosomal DNA double-strand breaks generated by a restriction endonuclease
    • Cromie, G.A. and Leach, D.R. 2001, Recombinational repair of chromosomal DNA double-strand breaks generated by a restriction endonuclease, Mol. Microbiol., 41, 873-83.
    • (2001) Mol. Microbiol. , vol.41 , pp. 873-83
    • Cromie, G.A.1    Leach, D.R.2
  • 78
    • 33646418420 scopus 로고    scopus 로고
    • Control of the endonuclease activity of type i restriction-modification systems is required to maintain chromosome integrity following homologous recombination
    • Blakely, G.W. and Murray, N.E. 2006, Control of the endonuclease activity of type I restriction-modification systems is required to maintain chromosome integrity following homologous recombination, Mol. Microbiol., 60, 883-93.
    • (2006) Mol. Microbiol. , vol.60 , pp. 883-93
    • Blakely, G.W.1    Murray, N.E.2
  • 79
    • 33845767396 scopus 로고    scopus 로고
    • Roles of PriA protein and double-strand DNA break repair functions in UV-induced restriction alleviation in Escherichia coli
    • Ivancic-Bacce, I., Vlasic, I., Cogelja-Cajo, G., Brcic-Kostic, K. and Salaj-Smic, E. 2006, Roles of PriA protein and double-strand DNA break repair functions in UV-induced restriction alleviation in Escherichia coli, Genetics, 174, 2137-49.
    • (2006) Genetics , vol.174 , pp. 2137-49
    • Ivancic-Bacce, I.1    Vlasic, I.2    Cogelja-Cajo, G.3    Brcic-Kostic, K.4    Salaj-Smic, E.5
  • 81
    • 0017412436 scopus 로고
    • UV-induced alleviation of K-specific restriction of bacteriophage lambda
    • Day, R.S. 3rd 1977, UV-induced alleviation of K-specific restriction of bacteriophage lambda, J. Virol., 21, 1249-51.
    • (1977) J. Virol. , vol.21 , pp. 1249-51
    • Day III, R.S.1
  • 82
    • 0024102490 scopus 로고
    • Alleviation of type i restriction in adenine methylase (dam) mutants of Escherichia coli
    • Efimova, E.P., Delver, E.P. and Belogurov, A.A. 1988, Alleviation of type I restriction in adenine methylase (dam) mutants of Escherichia coli, Mol. Gen. Genet., 214, 313-6.
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 313-6
    • Efimova, E.P.1    Delver, E.P.2    Belogurov, A.A.3
  • 83
    • 0033607255 scopus 로고    scopus 로고
    • Translocation and specific cleavage of bacteriophage T7 DNA in vivo by EcoKI
    • Garcia, L.R. and Molineux, I.J. 1999, Translocation and specific cleavage of bacteriophage T7 DNA in vivo by EcoKI, Proc. Natl Acad. Sci. USA, 96, 12430-5.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12430-5
    • Garcia, L.R.1    Molineux, I.J.2
  • 84
    • 27144511168 scopus 로고    scopus 로고
    • Type III restriction is alleviated by bacteriophage (RecE) homologous recombination function but enhanced by bacterial (RecBCD) function
    • Handa, N. and Kobayashi, I. 2005, Type III restriction is alleviated by bacteriophage (RecE) homologous recombination function but enhanced by bacterial (RecBCD) function, J. Bacteriol., 187, 7362-73.
    • (2005) J. Bacteriol. , vol.187 , pp. 7362-73
    • Handa, N.1    Kobayashi, I.2
  • 85
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman, M., Maeda, M., Itoh, A., et al. 2006, Large-scale identification of protein-protein interaction of Escherichia coli K-12, Genome Res., 16, 686-91.
    • (2006) Genome Res. , vol.16 , pp. 686-91
    • Arifuzzaman, M.1    Maeda, M.2    Itoh, A.3
  • 86
    • 0034595208 scopus 로고    scopus 로고
    • Measuring motion on DNA by the type i restriction endonuclease EcoR124I using triplex displacement
    • Firman, K. and Szczelkun, M.D. 2000, Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement, EMBO J., 19, 2094-102.
    • (2000) EMBO J. , vol.19 , pp. 2094-102
    • Firman, K.1    Szczelkun, M.D.2
  • 87
    • 77952722979 scopus 로고    scopus 로고
    • Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat
    • van Aelst, K., Toth, J., Ramanathan, S.P., Schwarz, F.W., Seidel, R. and Szczelkun, M.D. 2010, Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat, Proc. Natl Acad. Sci. USA, 107, 9123-8.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9123-8
    • Van Aelst, K.1    Toth, J.2    Ramanathan, S.P.3    Schwarz, F.W.4    Seidel, R.5    Szczelkun, M.D.6
  • 88
    • 0030582726 scopus 로고    scopus 로고
    • DNA cleavage by the type IC restriction-modification enzyme EcoR124II
    • Dreier, J., MacWilliams, M.P. and Bickle, T.A. 1996, DNA cleavage by the type IC restriction-modification enzyme EcoR124II, J. Mol. Biol., 264, 722-33.
    • (1996) J. Mol. Biol. , vol.264 , pp. 722-33
    • Dreier, J.1    MacWilliams, M.P.2    Bickle, T.A.3
  • 89
    • 0033516513 scopus 로고    scopus 로고
    • The McrBC endonuclease translocates DNA in a reaction dependent on GTP hydrolysis
    • Panne, D., Raleigh, E.A. and Bickle, T.A. 1999, The McrBC endonuclease translocates DNA in a reaction dependent on GTP hydrolysis, J. Mol. Biol., 290, 49-60.
    • (1999) J. Mol. Biol. , vol.290 , pp. 49-60
    • Panne, D.1    Raleigh, E.A.2    Bickle, T.A.3
  • 90
    • 0026602370 scopus 로고
    • Organization and function of the mcrBC genes of Escherichia coli K-12
    • Raleigh, E.A. 1992, Organization and function of the mcrBC genes of Escherichia coli K-12, Mol. Microbiol., 6, 1079-86.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1079-86
    • Raleigh, E.A.1
  • 91
    • 0024362775 scopus 로고
    • Genetic and physical mapping of the mcrA (rglA) and mcrB (rglB) loci of Escherichia coli K-12
    • Raleigh, E.A., Trimarchi, R. and Revel, H. 1989, Genetic and physical mapping of the mcrA (rglA) and mcrB (rglB) loci of Escherichia coli K-12, Genetics, 122, 279-96.
    • (1989) Genetics , vol.122 , pp. 279-96
    • Raleigh, E.A.1    Trimarchi, R.2    Revel, H.3
  • 92
    • 0023235828 scopus 로고
    • Localization of a genetic region involved in McrB restriction by Escherichia coli K-12
    • Ross, T.K. and Braymer, H.D. 1987, Localization of a genetic region involved in McrB restriction by Escherichia coli K-12, J. Bacteriol., 169, 1757-9.
    • (1987) J. Bacteriol. , vol.169 , pp. 1757-9
    • Ross, T.K.1    Braymer, H.D.2
  • 93
    • 0021981917 scopus 로고
    • Transposon mutagenesis and genetic mapping of the rglA and rglB loci of Escherichia coli
    • Ravi, R.S., Sozhamannan, S. and Dharmalingam, K. 1985, Transposon mutagenesis and genetic mapping of the rglA and rglB loci of Escherichia coli, Mol. Gen. Genet., 198, 390-2.
    • (1985) Mol. Gen. Genet. , vol.198 , pp. 390-2
    • Ravi, R.S.1    Sozhamannan, S.2    Dharmalingam, K.3
  • 94
    • 0024653574 scopus 로고
    • Identification of a second polypeptide required for McrB restriction of 5-methylcytosine-containing DNA in Escherichia coli K12
    • Ross, T.K., Achberger, E.C. and Braymer, H.D. 1989, Identification of a second polypeptide required for McrB restriction of 5-methylcytosine-containing DNA in Escherichia coli K12, Mol. Gen. Genet., 216, 402-7.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 402-7
    • Ross, T.K.1    Achberger, E.C.2    Braymer, H.D.3
  • 95
    • 0024524023 scopus 로고
    • Nucleotide sequence of the McrB region of Escherichia coli K-12 and evidence for two independent translational initiation sites at the mcrB locus
    • Ross, T.K., Achberger, E.C. and Braymer, H.D. 1989, Nucleotide sequence of the McrB region of Escherichia coli K-12 and evidence for two independent translational initiation sites at the mcrB locus, J. Bacteriol., 171, 1974-81.
    • (1989) J. Bacteriol. , vol.171 , pp. 1974-81
    • Ross, T.K.1    Achberger, E.C.2    Braymer, H.D.3
  • 96
    • 0025035727 scopus 로고
    • Genetic and sequence organization of the mcrBC locus of Escherichia coli K-12
    • Dila, D., Sutherland, E., Moran, L., Slatko, B. and Raleigh, E.A. 1990, Genetic and sequence organization of the mcrBC locus of Escherichia coli K-12, J. Bacteriol., 172, 4888-900.
    • (1990) J. Bacteriol. , vol.172 , pp. 4888-900
    • Dila, D.1    Sutherland, E.2    Moran, L.3    Slatko, B.4    Raleigh, E.A.5
  • 97
    • 0026611235 scopus 로고
    • Characterization of the mcrBC region of Escherichia coli K-12 wild-type and mutant strains
    • Kruger, T., Grund, C., Wild, C. and Noyer-Weidner, M. 1992, Characterization of the mcrBC region of Escherichia coli K-12 wild-type and mutant strains, Gene, 114, 1-12.
    • (1992) Gene , vol.114 , pp. 1-12
    • Kruger, T.1    Grund, C.2    Wild, C.3    Noyer-Weidner, M.4
  • 98
    • 0026634757 scopus 로고
    • McrBC: A multisubunit GTP-dependent restriction endonu-clease
    • Sutherland, E., Coe, L. and Raleigh, E.A. 1992, McrBC: a multisubunit GTP-dependent restriction endonu-clease, J. Mol. Biol., 225, 327-48.
    • (1992) J. Mol. Biol. , vol.225 , pp. 327-48
    • Sutherland, E.1    Coe, L.2    Raleigh, E.A.3
  • 99
    • 0030782557 scopus 로고    scopus 로고
    • Evidence of participation of McrB(S) in McrBC restriction in Escherichia coli K-12
    • Beary, T.P., Braymer, H.D. and Achberger, E.C. 1997, Evidence of participation of McrB(S) in McrBC restriction in Escherichia coli K-12, J. Bacteriol., 179, 7768-75.
    • (1997) J. Bacteriol. , vol.179 , pp. 7768-75
    • Beary, T.P.1    Braymer, H.D.2    Achberger, E.C.3
  • 100
    • 0032530024 scopus 로고    scopus 로고
    • McrBs, a modulator peptide for McrBC activity
    • Panne, D., Raleigh, E.A. and Bickle, T.A. 1998, McrBs, a modulator peptide for McrBC activity, EMBO J., 17, 5477-83.
    • (1998) EMBO J. , vol.17 , pp. 5477-83
    • Panne, D.1    Raleigh, E.A.2    Bickle, T.A.3
  • 101
    • 0030850355 scopus 로고    scopus 로고
    • The recognition of methylated DNA by the GTP-dependent restriction endonuclease McrBC resides in the N-terminal domain of McrB
    • Gast, F.U., Brinkmann, T., Pieper, U., Kruger, T., Noyer-Weidner, M. and Pingoud, A. 1997, The recognition of methylated DNA by the GTP-dependent restriction endonuclease McrBC resides in the N-terminal domain of McrB, Biol. Chem., 378, 975-82.
    • (1997) Biol. Chem. , vol.378 , pp. 975-82
    • Gast, F.U.1    Brinkmann, T.2    Pieper, U.3    Kruger, T.4    Noyer-Weidner, M.5    Pingoud, A.6
  • 102
    • 0033600727 scopus 로고    scopus 로고
    • The GTP-binding domain of McrB: More than just a variation on a common theme?
    • Pieper, U., Schweitzer, T., Groll, D.H., Gast, F.U. and Pingoud, A. 1999, The GTP-binding domain of McrB: more than just a variation on a common theme? J. Mol. Biol., 292, 547-56.
    • (1999) J. Mol. Biol. , vol.292 , pp. 547-56
    • Pieper, U.1    Schweitzer, T.2    Groll, D.H.3    Gast, F.U.4    Pingoud, A.5
  • 103
    • 0037161259 scopus 로고    scopus 로고
    • A mutational analysis of the PD. . .D/EXK motif suggests that McrC harbors the catalytic center for DNA cleavage by the GTP-dependent restriction enzyme McrBC from Escherichia coli
    • Pieper, U. and Pingoud, A. 2002, A mutational analysis of the PD. . .D/EXK motif suggests that McrC harbors the catalytic center for DNA cleavage by the GTP-dependent restriction enzyme McrBC from Escherichia coli, Biochemistry, 41, 5236-44.
    • (2002) Biochemistry , vol.41 , pp. 5236-44
    • Pieper, U.1    Pingoud, A.2
  • 104
    • 0035151431 scopus 로고    scopus 로고
    • Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles
    • Bujnicki, J.M. and Rychlewski, L. 2001, Grouping together highly diverged PD-(D/E)XK nucleases and identification of novel superfamily members using structure-guided alignment of sequence profiles, J. Mol. Microbiol. Biotechnol., 3, 69-72.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 69-72
    • Bujnicki, J.M.1    Rychlewski, L.2
  • 105
    • 0031981857 scopus 로고    scopus 로고
    • Dependence of McrBC cleavage on distance between recognition elements
    • Stewart, F.J. and Raleigh, E.A. 1998, Dependence of McrBC cleavage on distance between recognition elements, Biol. Chem., 379, 611-16.
    • (1998) Biol. Chem. , vol.379 , pp. 611-16
    • Stewart, F.J.1    Raleigh, E.A.2
  • 106
    • 0642360275 scopus 로고
    • The course of infection with abnormal bacteriophage T4 containing non-glucosy-lated DNA on Escherichia coli strains
    • Fukasawa, T. 1964, The course of infection with abnormal bacteriophage T4 containing non-glucosy-lated DNA on Escherichia coli strains, J. Mol. Biol., 9, 525-36.
    • (1964) J. Mol. Biol. , vol.9 , pp. 525-36
    • Fukasawa, T.1
  • 107
    • 0014077176 scopus 로고
    • Restriction of nonglucosylated T-even bacteriophage: Properties of permissive mutants of Escherichia coli B and K12
    • Revel, H.R. 1967, Restriction of nonglucosylated T-even bacteriophage: properties of permissive mutants of Escherichia coli B and K12, Virology, 31, 688-701.
    • (1967) Virology , vol.31 , pp. 688-701
    • Revel, H.R.1
  • 108
  • 109
    • 0031588902 scopus 로고    scopus 로고
    • The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4
    • Monod, C., Repoila, F., Kutateladze, M., Tetart, F. and Krisch, H.M. 1997, The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4, J. Mol. Biol., 267, 237-49.
    • (1997) J. Mol. Biol. , vol.267 , pp. 237-49
    • Monod, C.1    Repoila, F.2    Kutateladze, M.3    Tetart, F.4    Krisch, H.M.5
  • 110
    • 0022376069 scopus 로고
    • Cloning of a restriction-modification system from Proteus vulgaris and its use in analyzing a methy-lase-sensitive phenotype in Escherichia coli
    • Blumenthal, R.M., Gregory, S.A. and Cooperider, J.S. 1985, Cloning of a restriction-modification system from Proteus vulgaris and its use in analyzing a methy-lase-sensitive phenotype in Escherichia coli, J. Bacteriol., 164, 501-9.
    • (1985) J. Bacteriol. , vol.164 , pp. 501-9
    • Blumenthal, R.M.1    Gregory, S.A.2    Cooperider, J.S.3
  • 111
    • 0024270094 scopus 로고
    • Isolation of mutants in a DNA methyltransferase through mcrB-mediated restriction
    • Blumenthal, R.M. and Cotterman, M.M. 1988, Isolation of mutants in a DNA methyltransferase through mcrB-mediated restriction, Gene, 74, 271-3.
    • (1988) Gene , vol.74 , pp. 271-3
    • Blumenthal, R.M.1    Cotterman, M.M.2
  • 112
    • 0021111738 scopus 로고
    • DNA restriction-modification genes of phage P1 and plasmid p15B. Structure and in vitro transcription
    • Iida, S., Meyer, J., Bachi, B., et al. 1983, DNA restriction-modification genes of phage P1 and plasmid p15B. Structure and in vitro transcription, J. Mol. Biol., 165, 1-18.
    • (1983) J. Mol. Biol. , vol.165 , pp. 1-18
    • Iida, S.1    Meyer, J.2    Bachi, B.3
  • 113
    • 0028631018 scopus 로고
    • M.phi 3TII: A new monospe-cific DNA (cytosine-C5) methyltransferase with pronounced amino acid sequence similarity to a family of adenine-N6-DNA- methyltransferases
    • Noyer-Weidner, M., Walter, J., Terschuren, P.A., Chai, S. and Trautner, T.A. 1994, M.phi 3TII: a new monospe-cific DNA (cytosine-C5) methyltransferase with pronounced amino acid sequence similarity to a family of adenine-N6-DNA-methyltransferases, Nucleic Acids Res., 22, 5517-23.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5517-23
    • Noyer-Weidner, M.1    Walter, J.2    Terschuren, P.A.3    Chai, S.4    Trautner, T.A.5
  • 114
    • 0025922925 scopus 로고
    • M.H2I, a multispeci-fic 5C-DNA methyltransferase encoded by Bacillus amyloliquefaciens phage H2
    • Lange, C., Noyer-Weidner, M., Trautner, T.A., Weiner, M. and Zahler, S.A. 1991, M.H2I, a multispeci-fic 5C-DNA methyltransferase encoded by Bacillus amyloliquefaciens phage H2, Gene, 100, 213-8.
    • (1991) Gene , vol.100 , pp. 213-8
    • Lange, C.1    Noyer-Weidner, M.2    Trautner, T.A.3    Weiner, M.4    Zahler, S.A.5
  • 115
    • 0023322333 scopus 로고
    • Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages
    • Behrens, B., Noyer-Weidner, M., Pawlek, B., Lauster, R., Balganesh, T.S. and Trautner, T.A. 1987, Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages, EMBO J., 6, 1137-42.
    • (1987) EMBO J. , vol.6 , pp. 1137-42
    • Behrens, B.1    Noyer-Weidner, M.2    Pawlek, B.3    Lauster, R.4    Balganesh, T.S.5    Trautner, T.A.6
  • 116
    • 0023636120 scopus 로고
    • Characterization of the Escherichia coli modified cyto-sine restriction (mcrB) gene
    • Ross, T.K., Achberger, E.C. and Braymer, H.D. 1987, Characterization of the Escherichia coli modified cyto-sine restriction (mcrB) gene, Gene, 61, 277-89.
    • (1987) Gene , vol.61 , pp. 277-89
    • Ross, T.K.1    Achberger, E.C.2    Braymer, H.D.3
  • 117
    • 59149084538 scopus 로고    scopus 로고
    • The human colon cancer methylome shows similar hypo-and hypermethylation at conserved tissue-specific CpG island shores
    • Irizarry, R.A., Ladd-Acosta, C., Wen, B., et al. 2009, The human colon cancer methylome shows similar hypo-and hypermethylation at conserved tissue-specific CpG island shores, Nat. Genet., 41, 178-86.
    • (2009) Nat. Genet. , vol.41 , pp. 178-86
    • Irizarry, R.A.1    Ladd-Acosta, C.2    Wen, B.3
  • 118
    • 23044514626 scopus 로고    scopus 로고
    • Chromosome-wide and promoter-specific analyses identify sites of differential DNA methylation in normal and transformed human cells
    • Weber, M., Davies, J.J., Wittig, D., et al. 2005, Chromosome-wide and promoter-specific analyses identify sites of differential DNA methylation in normal and transformed human cells, Nat. Genet., 37, 853-62.
    • (2005) Nat. Genet. , vol.37 , pp. 853-62
    • Weber, M.1    Davies, J.J.2    Wittig, D.3
  • 119
    • 0028890128 scopus 로고
    • In vivo restriction by LlaI is encoded by three genes, arranged in an operon with llaIM, on the conju-gative Lactococcus plasmid pTR2030
    • O'Sullivan, D.J., Zagula, K. and Klaenhammer, T.R. 1995, In vivo restriction by LlaI is encoded by three genes, arranged in an operon with llaIM, on the conju-gative Lactococcus plasmid pTR2030, J. Bacteriol., 177, 134-43.
    • (1995) J. Bacteriol. , vol.177 , pp. 134-43
    • O'Sullivan, D.J.1    Zagula, K.2    Klaenhammer, T.R.3
  • 121
    • 3843128438 scopus 로고    scopus 로고
    • A plant vacuolar protease, VPE, mediates virus-induced hypersensitive cell death
    • Hatsugai, N., Kuroyanagi, M., Yamada, K., et al. 2004, A plant vacuolar protease, VPE, mediates virus-induced hypersensitive cell death, Science, 305, 855-8.
    • (2004) Science , vol.305 , pp. 855-8
    • Hatsugai, N.1    Kuroyanagi, M.2    Yamada, K.3
  • 122
    • 0028953424 scopus 로고
    • Phage-exclusion enzymes: A bonanza of biochemical and cell biology reagents?
    • Snyder, L. 1995, Phage-exclusion enzymes: a bonanza of biochemical and cell biology reagents? Mol. Microbiol., 15, 415-20.
    • (1995) Mol. Microbiol. , vol.15 , pp. 415-20
    • Snyder, L.1
  • 123
    • 0033515613 scopus 로고    scopus 로고
    • Detection of anticodon nuclease residues involved in tRNALys cleavage specificity
    • Meidler, R., Morad, I., Amitsur, M., Inokuchi, H. and Kaufmann, G. 1999, Detection of anticodon nuclease residues involved in tRNALys cleavage specificity, J. Mol. Biol., 287, 499-510.
    • (1999) J. Mol. Biol. , vol.287 , pp. 499-510
    • Meidler, R.1    Morad, I.2    Amitsur, M.3    Inokuchi, H.4    Kaufmann, G.5
  • 124
    • 33644774549 scopus 로고    scopus 로고
    • Genetic addiction: Selfish gene's strategy for symbiosis in the genome
    • Mochizuki, A., Yahara, K., Kobayashi, I. and Iwasa, Y. 2006, Genetic addiction: selfish gene's strategy for symbiosis in the genome, Genetics, 172, 1309-23.
    • (2006) Genetics , vol.172 , pp. 1309-23
    • Mochizuki, A.1    Yahara, K.2    Kobayashi, I.3    Iwasa, Y.4
  • 125
    • 0001615484 scopus 로고
    • Theoritical implications for the evolution of postsegregational killing by bacterial plasmid
    • Mongold, J.A. 1992, Theoritical implications for the evolution of postsegregational killing by bacterial plasmid, Am. Nat., 139, 677-89.
    • (1992) Am. Nat. , vol.139 , pp. 677-89
    • Mongold, J.A.1
  • 126
    • 0023274383 scopus 로고
    • Site-specific methy-lases induce the SOS DNA repair response in Escherichia coli
    • Heitman, J. and Model, P. 1987, Site-specific methy-lases induce the SOS DNA repair response in Escherichia coli, J. Bacteriol., 169, 3243-50.
    • (1987) J. Bacteriol. , vol.169 , pp. 3243-50
    • Heitman, J.1    Model, P.2
  • 127
    • 28244432478 scopus 로고    scopus 로고
    • Mrr instigates the SOS response after high pressure stress in Escherichia coli
    • Aertsen, A. and Michiels, C.W. 2005, Mrr instigates the SOS response after high pressure stress in Escherichia coli, Mol. Microbiol., 58, 1381-91.
    • (2005) Mol. Microbiol. , vol.58 , pp. 1381-91
    • Aertsen, A.1    Michiels, C.W.2
  • 128
    • 77956500617 scopus 로고    scopus 로고
    • A unique family of Mrr-like modification-dependent restriction endonucleases
    • Zheng, Y., Cohen-Karni, D., Xu, D., et al. 2010, A unique family of Mrr-like modification-dependent restriction endonucleases, Nucleic Acids Res., 38, 5527-34.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 5527-34
    • Zheng, Y.1    Cohen-Karni, D.2    Xu, D.3
  • 130
    • 33846591325 scopus 로고    scopus 로고
    • A type IV modification dependent restriction nuclease that targets glycosy-lated hydroxymethyl cytosine modified DNAs
    • Bair, C.L. and Black, L.W. 2007, A type IV modification dependent restriction nuclease that targets glycosy-lated hydroxymethyl cytosine modified DNAs, J. Mol. Biol., 366, 768-78.
    • (2007) J. Mol. Biol. , vol.366 , pp. 768-78
    • Bair, C.L.1    Black, L.W.2
  • 131
    • 0020480208 scopus 로고
    • Digestion of highly modified bacteriophage DNA by restriction endonucleases
    • Huang, L.H., Farnet, C.M., Ehrlich, K.C. and Ehrlich, M. 1982, Digestion of highly modified bacteriophage DNA by restriction endonucleases, Nucleic Acids Res., 10, 1579-91.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1579-91
    • Huang, L.H.1    Farnet, C.M.2    Ehrlich, K.C.3    Ehrlich, M.4
  • 133
    • 0017572099 scopus 로고
    • Endo R DpnI restriction of Escherichia coli DNA synthesized in vitro. Evidence that the ends of Okazaki pieces are determined by template deoxynucleotide sequence
    • Gomez-Eichelmann, M.C. and Lark, K.G. 1977, Endo R DpnI restriction of Escherichia coli DNA synthesized in vitro. Evidence that the ends of Okazaki pieces are determined by template deoxynucleotide sequence, J. Mol. Biol., 117, 621-35.
    • (1977) J. Mol. Biol. , vol.117 , pp. 621-35
    • Gomez-Eichelmann, M.C.1    Lark, K.G.2
  • 134
    • 0017667848 scopus 로고
    • Complementary action of restriction enzymes endo R-DpnI and Endo R-DpnII on bacteriophage f1 DNA
    • Vovis, G.F. and Lacks, S. 1977, Complementary action of restriction enzymes endo R-DpnI and Endo R-DpnII on bacteriophage f1 DNA, J. Mol. Biol., 115, 525-38.
    • (1977) J. Mol. Biol. , vol.115 , pp. 525-38
    • Vovis, G.F.1    Lacks, S.2
  • 135
    • 0023005977 scopus 로고
    • Genetic basis of the complementary DpnI and DpnII restriction systems of S. pneumo-niae: An intercellular cassette mechanism
    • Lacks, S.A., Mannarelli, B.M., Springhorn, S.S. and Greenberg, B. 1986, Genetic basis of the complementary DpnI and DpnII restriction systems of S. pneumo-niae: an intercellular cassette mechanism, Cell, 46, 993-1000.
    • (1986) Cell , vol.46 , pp. 993-1000
    • Lacks, S.A.1    Mannarelli, B.M.2    Springhorn, S.S.3    Greenberg, B.4
  • 136
    • 39849085506 scopus 로고    scopus 로고
    • Substrate specificity of new methyl-directed DNA endonuclease GlaI
    • Tarasova, G.V., Nayakshina, T.N. and Degtyarev, S.K. 2008, Substrate specificity of new methyl-directed DNA endonuclease GlaI, BMC Mol. Biol., 9, 7.
    • (2008) BMC Mol. Biol. , vol.9 , pp. 7
    • Tarasova, G.V.1    Nayakshina, T.N.2    Degtyarev, S.K.3
  • 137
    • 22544464152 scopus 로고    scopus 로고
    • The biology of restriction and anti-restriction
    • Tock, M.R. and Dryden, D.T.F. 2005, The biology of restriction and anti-restriction, Curr. Opin. Microbiol., 8, 466-72.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 466-72
    • Tock, M.R.1    Dryden, D.T.F.2
  • 138
    • 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. 1985, Inhibition of the type I restriction-modification enzymes EcoB and EcoK by the gene 0.3 protein of bacteriophage T7, J. Mol. Biol., 182, 567-78.
    • (1985) J. Mol. Biol. , vol.182 , pp. 567-78
    • Bandyopadhyay, P.K.1    Studier, F.W.2    Hamilton, D.L.3    Yuan, R.4
  • 139
    • 0036161805 scopus 로고    scopus 로고
    • Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA
    • Walkinshaw, M.D., Taylor, P., Sturrock, S.S., et al. 2002, Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA, Mol. Cell, 9, 187-94.
    • (2002) Cell , vol.9 , pp. 187-94
    • Walkinshaw, M.D.1    Taylor, P.2    Sturrock, S.S.3
  • 140
    • 0022410842 scopus 로고
    • DNA methylation of bacterial viruses T3 and T7 by different DNA methylases in Escherichia coli K12 cells
    • Kruger, D.H., Schroeder, C., Reuter, M., Bogdarina, I.G., Buryanov, Y.I. and Bickle, T.A. 1985, DNA methylation of bacterial viruses T3 and T7 by different DNA methylases in Escherichia coli K12 cells, Eur. J. Biochem., 150, 323-30.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 323-30
    • Kruger, D.H.1    Schroeder, C.2    Reuter, M.3    Bogdarina, I.G.4    Buryanov, Y.I.5    Bickle, T.A.6
  • 141
    • 0022476166 scopus 로고
    • Modification enhancement by the restriction alleviation protein (Ral) of bacteriophage lambda
    • Loenen, W.A. and Murray, N.E. 1986, Modification enhancement by the restriction alleviation protein (Ral) of bacteriophage lambda,J.Mol. Biol.,190,11-22.
    • (1986) J.Mol. Biol. , vol.190 , pp. 11-22
    • Loenen, W.A.1    Murray, N.E.2
  • 142
    • 0029070828 scopus 로고
    • Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12
    • King, G. and Murray, N.E. 1995, Restriction alleviation and modification enhancement by the Rac prophage of Escherichia coli K-12, Mol. Microbiol., 16, 769-77.
    • (1995) Mol. Microbiol. , vol.16 , pp. 769-77
    • King, G.1    Murray, N.E.2
  • 143
    • 35348999539 scopus 로고    scopus 로고
    • Phosphorothioation of DNA in bacteria by dnd genes
    • Wang, L., Chen, S., Xu, T., et al. 2007, Phosphorothioation of DNA in bacteria by dnd genes, Nat. Chem. Biol., 3, 709-10.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 709-10
    • Wang, L.1    Chen, S.2    Xu, T.3
  • 144
    • 78650700875 scopus 로고    scopus 로고
    • A novel host-specific restriction system associated with DNA backbone S-modification in Salmonella
    • Press
    • Xu, T., Yao, F., Zhou, X., Deng, Z. and You, D. In press. A novel host-specific restriction system associated with DNA backbone S-modification in Salmonella, Nucleic Acids Res, in press.
    • Nucleic Acids Res
    • Xu, T.1    Yao, F.2    Zhou, X.3    Deng, Z.4    You, D.5


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