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Volumn 43, Issue 8, 2015, Pages 4296-4308

Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: Potential implications for methylation-independent transcriptional repression

Author keywords

[No Author keywords available]

Indexed keywords

DNA ADENINE METHYLTRANSFERASE; BACTERIAL DNA; DAM PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; REPRESSOR PROTEIN; SITE SPECIFIC DNA METHYLTRANSFERASE (ADENINE SPECIFIC);

EID: 84930216291     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv251     Document Type: Article
Times cited : (13)

References (57)
  • 1
    • 0017411721 scopus 로고
    • Complementary specificity of restriction endonucleases of Diplococcus pneumoniae with respect to DNA methylation
    • Lacks, S. and Greenberg, B. (1977) Complementary specificity of restriction endonucleases of Diplococcus pneumoniae with respect to DNA methylation. J. Mol. Biol., 114, 153-168.
    • (1977) J. Mol. Biol. , vol.114 , pp. 153-168
    • Lacks, S.1    Greenberg, B.2
  • 2
    • 0018214882 scopus 로고
    • Sequence specificity of the P1 modification methylase (M. Eco P1) and the DNA methylase (M. Eco dam) controlled by the Escherichia coli dam gene
    • Hattman, S., Brooks, J.E. and Masurekar, M. (1978) Sequence specificity of the P1 modification methylase (M. Eco P1) and the DNA methylase (M. Eco dam) controlled by the Escherichia coli dam gene. J. Mol. Biol., 126, 367-380.
    • (1978) J. Mol. Biol. , vol.126 , pp. 367-380
    • Hattman, S.1    Brooks, J.E.2    Masurekar, M.3
  • 3
    • 0021100583 scopus 로고
    • The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene
    • Brooks, J.E., Blumenthal, R.M. and Gingeras, T.R. (1983) The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene. Nucleic Acids Res., 11, 837-851.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 837-851
    • Brooks, J.E.1    Blumenthal, R.M.2    Gingeras, T.R.3
  • 4
    • 4143112208 scopus 로고    scopus 로고
    • Bacteriophage T2Dam and T4Dam DNA-[N6-adenine]-methyltransferases
    • Hattman, S. and Malygin, E.G. (2004) Bacteriophage T2Dam and T4Dam DNA-[N6-adenine]-methyltransferases. Prog. Nucleic Res. Mol. Biol., 77, 67-126.
    • (2004) Prog. Nucleic Res. Mol. Biol. , vol.77 , pp. 67-126
    • Hattman, S.1    Malygin, E.G.2
  • 6
    • 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
  • 8
    • 77955302574 scopus 로고    scopus 로고
    • Replication of vibrio cholerae chromosome I in Escherichia coli: Dependence on dam methylation
    • Koch, B., Ma, X. and Lobner-Olesen, A. (2010) Replication of Vibrio cholerae chromosome I in Escherichia coli: dependence on dam methylation. J. Bacteriol., 192, 3903-3914.
    • (2010) J. Bacteriol. , vol.192 , pp. 3903-3914
    • Koch, B.1    Ma, X.2    Lobner-Olesen, A.3
  • 9
    • 0023677502 scopus 로고
    • Timing and targeting: The biological functions of Dam methylation in E. Coli
    • Messer, W. and Noyer-Weidner, M. (1988) Timing and targeting: the biological functions of Dam methylation in E. coli. Cell, 54, 735-737.
    • (1988) Cell , vol.54 , pp. 735-737
    • Messer, W.1    Noyer-Weidner, M.2
  • 10
    • 0024297464 scopus 로고
    • The rate of Dam-mediated DNA adenine methylation in Escherichia coli
    • Campbell, J.L. and Kleckner, N. (1988) The rate of Dam-mediated DNA adenine methylation in Escherichia coli. Gene, 74, 189-190.
    • (1988) Gene , vol.74 , pp. 189-190
    • Campbell, J.L.1    Kleckner, N.2
  • 11
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination, and cancer biology
    • Modrich, P. and Lahue, R. (1996) Mismatch repair in replication fidelity, genetic recombination, and cancer biology. Annu. Rev. Biochem., 65, 101-133.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 12
    • 0036366541 scopus 로고    scopus 로고
    • Genome-wide analysis of deoxyadenosine methyltransferase-mediated control of gene expression in Escherichia coli
    • Oshima, T., Wada, C., Kawagoe, Y., Ara, T., Maeda, M., Masuda, Y., Hiraga, S. and Mori, H. (2002) Genome-wide analysis of deoxyadenosine methyltransferase-mediated control of gene expression in Escherichia coli. Mol. Microbiol., 45, 673-695.
    • (2002) Mol. Microbiol. , vol.45 , pp. 673-695
    • Oshima, T.1    Wada, C.2    Kawagoe, Y.3    Ara, T.4    Maeda, M.5    Masuda, Y.6    Hiraga, S.7    Mori, H.8
  • 13
    • 0037446886 scopus 로고    scopus 로고
    • Role of SeqA and Dam in Escherichia coli gene expression: A global/microarray analysis
    • Lobner-Olesen, A., Marinus, M.G. and Hansen, F.G. (2003) Role of SeqA and Dam in Escherichia coli gene expression: a global/microarray analysis. Proc. Natl. Acad. Sci. U.S.A., 100, 4672-4677.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4672-4677
    • Lobner-Olesen, A.1    Marinus, M.G.2    Hansen, F.G.3
  • 14
    • 0242266619 scopus 로고    scopus 로고
    • The mechanism by which DNA adenine methylase and PapI activate the pap epigenetic switch
    • Hernday, A.D., Braaten, B.A. and Low, D.A. (2003) The mechanism by which DNA adenine methylase and PapI activate the pap epigenetic switch. Mol. Cell, 12, 947-957.
    • (2003) Mol. Cell , vol.12 , pp. 947-957
    • Hernday, A.D.1    Braaten, B.A.2    Low, D.A.3
  • 16
    • 33646088737 scopus 로고    scopus 로고
    • Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase
    • Horton, J.R., Liebert, K., Bekes, M., Jeltsch, A. and Cheng, X. (2006) Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase. J. Mol. Biol., 358, 559-570.
    • (2006) J. Mol. Biol. , vol.358 , pp. 559-570
    • Horton, J.R.1    Liebert, K.2    Bekes, M.3    Jeltsch, A.4    Cheng, X.5
  • 17
    • 34547929793 scopus 로고    scopus 로고
    • Two alternative conformations of S-adenosyl-L-homocysteine bound to Escherichia coli DNA adenine methyltransferase and the implication of conformational changes in regulating the catalytic cycle
    • Liebert, K., Horton, J.R., Chahar, S., Orwick, M., Cheng, X. and Jeltsch, A. (2007) Two alternative conformations of S-adenosyl-L-homocysteine bound to Escherichia coli DNA adenine methyltransferase and the implication of conformational changes in regulating the catalytic cycle. J. Biol. Chem., 282, 22848-22855.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22848-22855
    • Liebert, K.1    Horton, J.R.2    Chahar, S.3    Orwick, M.4    Cheng, X.5    Jeltsch, A.6
  • 18
    • 50649123011 scopus 로고    scopus 로고
    • Modulation of escherichia coli DNA methyltransferase activity by biologically derived GATC-flanking sequences
    • Coffin, S.R. and Reich, N.O. (2008) Modulation of Escherichia coli DNA methyltransferase activity by biologically derived GATC-flanking sequences. J. Biol. Chem., 283, 20106-20116.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20106-20116
    • Coffin, S.R.1    Reich, N.O.2
  • 19
    • 26444530070 scopus 로고    scopus 로고
    • Analysis of global gene expression and double-strand-break formation in DNA adenine methyltransferaseand mismatch repair-deficient Escherichia coli
    • Robbins-Manke, J.L., Zdraveski, Z.Z., Marinus, M. and Essigmann, J.M. (2005) Analysis of global gene expression and double-strand-break formation in DNA adenine methyltransferaseand mismatch repair-deficient Escherichia coli. J. Bacteriol., 187, 7027-7037.
    • (2005) J. Bacteriol. , vol.187 , pp. 7027-7037
    • Robbins-Manke, J.L.1    Zdraveski, Z.Z.2    Marinus, M.3    Essigmann, J.M.4
  • 20
    • 0021972860 scopus 로고
    • Viability of escherichia coli K-12 DNA adenine methylase (dam) mutants requires increased expression of specific genes in the SOS regulon
    • Peterson, K.R., Wertman, K.F., Mount, D.W. and Marinus, M.G. (1985) Viability of Escherichia coli K-12 DNA adenine methylase (dam) mutants requires increased expression of specific genes in the SOS regulon. Mol. Gene Genet., 201, 14-19.
    • (1985) Mol. Gene Genet. , vol.201 , pp. 14-19
    • Peterson, K.R.1    Wertman, K.F.2    Mount, D.W.3    Marinus, M.G.4
  • 22
    • 55849132180 scopus 로고    scopus 로고
    • An assessment of the role of DNA adenine methyltransferase on gene expression regulation in e coli
    • Seshasayee, A.S. (2007) An assessment of the role of DNA adenine methyltransferase on gene expression regulation in E coli. PLoS ONE, 2, e273.
    • (2007) PLoS ONE , vol.2 , pp. e273
    • Seshasayee, A.S.1
  • 23
    • 18844448011 scopus 로고    scopus 로고
    • Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase
    • Horton, J.R., Liebert, K., Hattman, S., Jeltsch, A. and Cheng, X. (2005) Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase. Cell, 121, 349-361.
    • (2005) Cell , vol.121 , pp. 349-361
    • Horton, J.R.1    Liebert, K.2    Hattman, S.3    Jeltsch, A.4    Cheng, X.5
  • 25
    • 84907843278 scopus 로고    scopus 로고
    • DNA looping provides for "intersegmental hopping" by proteins: A mechanism for long-range site localization
    • Pollak, A.J., Chin, A.T., Brown, F.L. and Reich, N.O. (2014) DNA looping provides for "intersegmental hopping" by proteins: a mechanism for long-range site localization. J. Mol. Biol., 426, 3539-3552.
    • (2014) J. Mol. Biol. , vol.426 , pp. 3539-3552
    • Pollak, A.J.1    Chin, A.T.2    Brown, F.L.3    Reich, N.O.4
  • 26
    • 3343009003 scopus 로고    scopus 로고
    • Stopped-flow and mutational analysis of base flipping by the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase
    • Liebert, K., Hermann, A., Schlickenrieder, M. and Jeltsch, A. (2004) Stopped-flow and mutational analysis of base flipping by the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase. J. Mol. Biol., 341, 443-454.
    • (2004) J. Mol. Biol. , vol.341 , pp. 443-454
    • Liebert, K.1    Hermann, A.2    Schlickenrieder, M.3    Jeltsch, A.4
  • 27
    • 70350547773 scopus 로고    scopus 로고
    • Transition from EcoDam to T4Dam DNA recognition mechanism without loss of activity and specificity
    • Elsawy, H., Podobinschi, S., Chahar, S. and Jeltsch, A. (2009) Transition from EcoDam to T4Dam DNA recognition mechanism without loss of activity and specificity. Chembiochem, 10, 2488-2493.
    • (2009) Chembiochem , vol.10 , pp. 2488-2493
    • Elsawy, H.1    Podobinschi, S.2    Chahar, S.3    Jeltsch, A.4
  • 28
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif., 41, 207-234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 29
    • 0031058884 scopus 로고    scopus 로고
    • Rotation function calculations with GLRF program
    • Tong, L. and Rossmann, M.G. (1997) Rotation function calculations with GLRF program. Methods Enzymol., 276, 594-611.
    • (1997) Methods Enzymol. , vol.276 , pp. 594-611
    • Tong, L.1    Rossmann, M.G.2
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
  • 35
    • 84871083428 scopus 로고    scopus 로고
    • Carbon-oxygen hydrogen bonding in biological structure and function
    • Horowitz, S. and Trievel, R.C. (2012) Carbon-oxygen hydrogen bonding in biological structure and function. J. Biol. Chem., 287, 41576-41582.
    • (2012) J. Biol. Chem. , vol.287 , pp. 41576-41582
    • Horowitz, S.1    Trievel, R.C.2
  • 36
    • 52049097777 scopus 로고    scopus 로고
    • Competitive Lrp and Dam assembly at the pap regulatory region: Implications for mechanisms of epigenetic regulation
    • Peterson, S.N. and Reich, N.O. (2008) Competitive Lrp and Dam assembly at the pap regulatory region: implications for mechanisms of epigenetic regulation. J. Mol. Biol., 383, 92-105.
    • (2008) J. Mol. Biol. , vol.383 , pp. 92-105
    • Peterson, S.N.1    Reich, N.O.2
  • 37
    • 79956133928 scopus 로고    scopus 로고
    • The design involved in PapI and Lrp regulation of the pap operon
    • Kawamura, T., Vartanian, A.S., Zhou, H. and Dahlquist, F.W. (2011) The design involved in PapI and Lrp regulation of the pap operon. J. Mol. Biol., 409, 311-332.
    • (2011) J. Mol. Biol. , vol.409 , pp. 311-332
    • Kawamura, T.1    Vartanian, A.S.2    Zhou, H.3    Dahlquist, F.W.4
  • 38
    • 10644244206 scopus 로고    scopus 로고
    • Functional characterization of Escherichia coli DNA adenine methyltransferase, a novel target for antibiotics
    • Mashhoon, N., Carroll, M., Pruss, C., Eberhard, J., Ishikawa, S., Estabrook, R.A. and Reich, N. (2004) Functional characterization of Escherichia coli DNA adenine methyltransferase, a novel target for antibiotics. J. Biol. Chem., 279, 52075-52081.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52075-52081
    • Mashhoon, N.1    Carroll, M.2    Pruss, C.3    Eberhard, J.4    Ishikawa, S.5    Estabrook, R.A.6    Reich, N.7
  • 39
    • 0024594761 scopus 로고
    • Preferential site-specific hemimethylation of GATC sites in pBR322 DNA by Dam methyltransferase from Escherichia coli
    • Bergerat, A., Kriebardis, A. and Guschlbauer, W. (1989) Preferential site-specific hemimethylation of GATC sites in pBR322 DNA by Dam methyltransferase from Escherichia coli. J. Biol. Chem., 264, 4064-4070.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4064-4070
    • Bergerat, A.1    Kriebardis, A.2    Guschlbauer, W.3
  • 40
    • 53649089723 scopus 로고    scopus 로고
    • The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix
    • Hashimoto, H., Horton, J.R., Zhang, X., Bostick, M., Jacobsen, S.E. and Cheng, X. (2008) The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature, 455, 826-829.
    • (2008) Nature , vol.455 , pp. 826-829
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3    Bostick, M.4    Jacobsen, S.E.5    Cheng, X.6
  • 41
    • 48149108427 scopus 로고    scopus 로고
    • Structure of the E. Coli DNA glycosylase AlkA bound to the ends of duplex DNA: A system for the structure determination of lesion-containing DNA
    • Bowman, B.R., Lee, S., Wang, S. and Verdine, G.L. (2008) Structure of the E. coli DNA glycosylase AlkA bound to the ends of duplex DNA: a system for the structure determination of lesion-containing DNA. Structure, 16, 1166-1174.
    • (2008) Structure , vol.16 , pp. 1166-1174
    • Bowman, B.R.1    Lee, S.2    Wang, S.3    Verdine, G.L.4
  • 42
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • Wibley, J.E., Waters, T.R., Haushalter, K., Verdine, G.L. and Pearl, L.H. (2003) Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. Mol. Cell, 11, 1647-1659.
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 43
    • 0031827294 scopus 로고    scopus 로고
    • Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct
    • Barrett, T.E., Savva, R., Barlow, T., Brown, T., Jiricny, J. and Pearl, L.H. (1998) Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct. Nat. Struct. Biol., 5, 697-701.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 697-701
    • Barrett, T.E.1    Savva, R.2    Barlow, T.3    Brown, T.4    Jiricny, J.5    Pearl, L.H.6
  • 45
    • 0028990179 scopus 로고
    • M. HhaI binds tightly to substrates containing mismatches at the target base
    • Klimasauskas, S. and Roberts, R.J. (1995) M. HhaI binds tightly to substrates containing mismatches at the target base. Nucleic Acids Res., 23, 1388-1395.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1388-1395
    • Klimasauskas, S.1    Roberts, R.J.2
  • 46
    • 37549014569 scopus 로고    scopus 로고
    • The M. EcoRV DNA-(adenine N6)-methyltransferase uses DNA bending for recognition of an expanded EcoDam recognition site
    • Jurkowski, T.P., Anspach, N., Kulishova, L., Nellen, W. and Jeltsch, A. (2007) The M. EcoRV DNA-(adenine N6)-methyltransferase uses DNA bending for recognition of an expanded EcoDam recognition site. J. Biol. Chem., 282, 36942-36952.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36942-36952
    • Jurkowski, T.P.1    Anspach, N.2    Kulishova, L.3    Nellen, W.4    Jeltsch, A.5
  • 48
    • 84863319342 scopus 로고    scopus 로고
    • Proximal recognition sites facilitate intrasite hopping by DNA adenine methyltransferase: Mechanistic exploration of epigenetic gene regulation
    • Pollak, A.J. and Reich, N.O. (2012) Proximal recognition sites facilitate intrasite hopping by DNA adenine methyltransferase: mechanistic exploration of epigenetic gene regulation. J. Biol. Chem., 287, 22873-22881.
    • (2012) J. Biol. Chem. , vol.287 , pp. 22873-22881
    • Pollak, A.J.1    Reich, N.O.2
  • 49
    • 0033829119 scopus 로고    scopus 로고
    • Effects of global regulatory proteins and environmental conditions on fimbrial gene expression of F165(1) and F165(2) produced by Escherichia coli causing septicaemia in pigs
    • Daigle, F., Forget, C., Martin, C., Drolet, M., Tessier, M.C., Dezfulian, H. and Harel, J. (2000) Effects of global regulatory proteins and environmental conditions on fimbrial gene expression of F165(1) and F165(2) produced by Escherichia coli causing septicaemia in pigs. Res. Microbiol., 151, 563-574.
    • (2000) Res. Microbiol. , vol.151 , pp. 563-574
    • Daigle, F.1    Forget, C.2    Martin, C.3    Drolet, M.4    Tessier, M.C.5    Dezfulian, H.6    Harel, J.7
  • 50
    • 0037336268 scopus 로고    scopus 로고
    • Leucine-responsive regulatory protein-mediated repression of clp (encoding CS31A) expression by L-leucine and L-alanine in Escherichia coli
    • Crost, C., Garrivier, A., Harel, J. and Martin, C. (2003) Leucine-responsive regulatory protein-mediated repression of clp (encoding CS31A) expression by L-leucine and L-alanine in Escherichia coli. J. Bacteriol., 185, 1886-1894.
    • (2003) J. Bacteriol. , vol.185 , pp. 1886-1894
    • Crost, C.1    Garrivier, A.2    Harel, J.3    Martin, C.4
  • 51
    • 0028200974 scopus 로고
    • Leucine-responsive regulatory protein and deoxyadenosine methylase control the phase variation and expression of the sfa and daa pili operons in Escherichia coli
    • van der Woude, M.W. and Low, D.A. (1994) Leucine-responsive regulatory protein and deoxyadenosine methylase control the phase variation and expression of the sfa and daa pili operons in Escherichia coli. Mol. Microbiol., 11, 605-618.
    • (1994) Mol. Microbiol. , vol.11 , pp. 605-618
    • Van Der-Woude, M.W.1    Low, D.A.2
  • 52
    • 0036231043 scopus 로고    scopus 로고
    • Competitive interaction of the OxyR DNA-binding protein and the Dam methylase at the antigen 43 gene regulatory region in Escherichia coli
    • Waldron, D.E., Owen, P. and Dorman, C.J. (2002) Competitive interaction of the OxyR DNA-binding protein and the Dam methylase at the antigen 43 gene regulatory region in Escherichia coli. Mol. Microbiol., 44, 509-520.
    • (2002) Mol. Microbiol. , vol.44 , pp. 509-520
    • Waldron, D.E.1    Owen, P.2    Dorman, C.J.3
  • 53
    • 0029095206 scopus 로고
    • Negative control of fae (K88) expression by the 'global' regulator Lrp is modulated by the 'local' regulator FaeA and affected by DNA methylation
    • Huisman, T.T. and de Graaf, F.K. (1995) Negative control of fae (K88) expression by the 'global' regulator Lrp is modulated by the 'local' regulator FaeA and affected by DNA methylation. Mol. Microbiol., 16, 943-953.
    • (1995) Mol. Microbiol. , vol.16 , pp. 943-953
    • Huisman, T.T.1    De Graaf, F.K.2
  • 56
    • 0035093828 scopus 로고    scopus 로고
    • Chromatin profiling using targeted DNA adenine methyltransferase
    • van Steensel, B., Delrow, J. and Henikoff, S. (2001) Chromatin profiling using targeted DNA adenine methyltransferase. Nat. Genet., 27, 304-308.
    • (2001) Nat. Genet. , vol.27 , pp. 304-308
    • Van Steensel, B.1    Delrow, J.2    Henikoff, S.3
  • 57
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., Blumenthal, R.M. and Cheng, X. (1995) Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol., 253, 618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3


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