메뉴 건너뛰기




Volumn 34, Issue 3, 2006, Pages 806-815

Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; BACTERIAL ENZYME; DIMER; DNA; DNA METHYLTRANSFERASE; RSRL METHYLTRANSFERASE; UNCLASSIFIED DRUG; DNA MODIFICATION METHYLASE ECORI; SITE SPECIFIC DNA METHYLTRANSFERASE (ADENINE SPECIFIC);

EID: 33644870800     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkj486     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud,A. and Jeltsch,A. (2001) Structure and function of type II restriction endonucleases. Nucleic Acids Res., 29, 3705-3727.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 2
    • 0017730133 scopus 로고
    • EcoRI methylase. Physical and catalytic properties of the homogeneous enzyme
    • Rubin,R. and Modrich,P. (1977) EcoRI methylase. Physical and catalytic properties of the homogeneous enzyme. J. Biol. Chem., 252, 7265-7272.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7265-7272
    • Rubin, R.1    Modrich, P.2
  • 3
    • 0020430519 scopus 로고
    • Studies on sequence recognition by type II restriction and modification enzymes
    • Modrich,P. (1982) Studies on sequence recognition by type II restriction and modification enzymes. CRC Crit. Rev. Biochem., 13, 287-323.
    • (1982) CRC Crit. Rev. Biochem. , vol.13 , pp. 287-323
    • Modrich, P.1
  • 4
    • 0027222612 scopus 로고
    • Presteady state kinetics of an S-adenosylmethionine-dependent enzyme. Evidence for a unique binding orientation requirement for EcoRI DNA methyltransferase
    • Reich,N. and Mashhoon,M. (1993) Presteady state kinetics of an S-adenosylmethionine-dependent enzyme. Evidence for a unique binding orientation requirement for EcoRI DNA methyltransferase. J. Biol. Chem., 268, 9191-9193.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9191-9193
    • Reich, N.1    Mashhoon, M.2
  • 5
    • 0017130530 scopus 로고
    • EcoRI endonuclease. Physical and catalytic properties of the homogenous enzyme
    • Modrich,P. and Zabel,D. (1976) EcoRI endonuclease. Physical and catalytic properties of the homogenous enzyme. J. Biol. Chem., 251, 5866-5874.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5866-5874
    • Modrich, P.1    Zabel, D.2
  • 6
    • 0023645197 scopus 로고
    • Proteins encoded by the DpnII restriction gene cassette. Two methylases and an endonuclease
    • de laCampa,A., Kale,P., Springhorn,S. and Lacks,S. (1987) Proteins encoded by the DpnII restriction gene cassette. Two methylases and an endonuclease. J. Mol. Biol., 196, 457-469.
    • (1987) J. Mol. Biol. , vol.196 , pp. 457-469
    • de laCampa, A.1    Kale, P.2    Springhorn, S.3    Lacks, S.4
  • 7
    • 0026577062 scopus 로고
    • Purification and characterization of the MspI DNA methyltransferase cloned and overexpressed in E.coli
    • Dubey,A., Mollet,B. and Roberts,R. (1992) Purification and characterization of the MspI DNA methyltransferase cloned and overexpressed in E.coli. Nucleic Acids Res., 20, 1579-1585.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1579-1585
    • Dubey, A.1    Mollet, B.2    Roberts, R.3
  • 8
    • 2942706016 scopus 로고    scopus 로고
    • Structure of the Q237W mutant of HhaI DNA methyltransferase: An insight into protein-protein interactions
    • Dong,A., Zhou,L., Zhang,X., Stickel,S., Roberts,R. and Cheng,X. (2004) Structure of the Q237W mutant of HhaI DNA methyltransferase: An insight into protein-protein interactions. Biol. Chem., 385, 373-379.
    • (2004) Biol. Chem. , vol.385 , pp. 373-379
    • Dong, A.1    Zhou, L.2    Zhang, X.3    Stickel, S.4    Roberts, R.5    Cheng, X.6
  • 9
    • 0026698903 scopus 로고
    • Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli
    • Kaszubska,W., Webb,H. and Gumport,R. (1992) Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli. Gene, 118, 5-11.
    • (1992) Gene , vol.118 , pp. 5-11
    • Kaszubska, W.1    Webb, H.2    Gumport, R.3
  • 10
    • 0037424385 scopus 로고    scopus 로고
    • Kinetic and catalytic properties of dimeric KpnI DNA methyltransferase
    • Bheemanaik,S., Chandrashekaran,S., Nagaraja,V. and Rao,D. (2003) Kinetic and catalytic properties of dimeric KpnI DNA methyltransferase. J. Biol. Chem., 278, 7863-7874.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7863-7874
    • Bheemanaik, S.1    Chandrashekaran, S.2    Nagaraja, V.3    Rao, D.4
  • 11
    • 0344012007 scopus 로고    scopus 로고
    • Characterization of the LlaCI methyltransferase from Lactococcus lactis subsp. cremoris W15 provides new insights into the biology of type II restriction-modification systems
    • Mruk,I., Cichowicz,M. and Kaczorowski,T. (2003) Characterization of the LlaCI methyltransferase from Lactococcus lactis subsp. cremoris W15 provides new insights into the biology of type II restriction-modification systems. Microbio., 149, 3331-3341.
    • (2003) Microbio. , vol.149 , pp. 3331-3341
    • Mruk, I.1    Cichowicz, M.2    Kaczorowski, T.3
  • 12
    • 0035805507 scopus 로고    scopus 로고
    • Identification of the active oligomeric state of an essential adenine DNA methyltransferase from Caulobacter crescentus
    • Shier,V., Hancey,C. and Benkovic,S. (2001) Identification of the active oligomeric state of an essential adenine DNA methyltransferase from Caulobacter crescentus. J. Biol. Chem., 276, 14744-14751.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14744-14751
    • Shier, V.1    Hancey, C.2    Benkovic, S.3
  • 13
    • 9644307892 scopus 로고    scopus 로고
    • Bacteriophage T4Dam DNA-(adenine-N(6))-methyltransferase. Comparison of pre-steady state and single turnover methylation of 40mer duplexes containing two (un)modified target sites
    • Malygin,E.G., Sclavi,B., Zinoviev,V.V., Evdokimov,A.A., Hattman,S. and Buckle,M. (2004) Bacteriophage T4Dam DNA-(adenine-N(6))-methyltransferase. Comparison of pre-steady state and single turnover methylation of 40mer duplexes containing two (un)modified target sites. J. Biol. Chem., 279, 50012-50018.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50012-50018
    • Malygin, E.G.1    Sclavi, B.2    Zinoviev, V.V.3    Evdokimov, A.A.4    Hattman, S.5    Buckle, M.6
  • 15
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • Janin,J. (1997) Specific versus non-specific contacts in protein crystals. Nature Struct. Biol., 4, 973-974.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 973-974
    • Janin, J.1
  • 16
    • 0344443347 scopus 로고    scopus 로고
    • Crystal structure of MboIIA methyltransferase
    • Osipiuk,J., Walsh,M. and Joachimiak,A. (2003) Crystal structure of MboIIA methyltransferase. Nucleic Acids Res., 31, 5440-5448.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5440-5448
    • Osipiuk, J.1    Walsh, M.2    Joachimiak, A.3
  • 17
    • 0034667760 scopus 로고    scopus 로고
    • Substrate binding in vitro and kinetics of RsrI (N6-adenine) DNA methyltransferase
    • Szegedi,S., Reich,N. and Gumport,R. (2000) Substrate binding in vitro and kinetics of RsrI (N6-adenine) DNA methyltransferase. Nucleic Acids Res., 28, 3962-3971.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3962-3971
    • Szegedi, S.1    Reich, N.2    Gumport, R.3
  • 18
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino-acid sequence data
    • Gill,S. and vonHippel,P. (1989) Calculation of protein extinction coefficients from amino-acid sequence data. Anal. Biochem., 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.1    vonHippel, P.2
  • 19
    • 0033514427 scopus 로고    scopus 로고
    • Functional roles of the conserved aromatic amino acid residues at position 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus
    • Pues,H., Bleimling,N., Holz,B., Wolcke,J. and Weinhold,E. (1999) Functional roles of the conserved aromatic amino acid residues at position 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus. Biochemistry, 38, 1426-1434.
    • (1999) Biochemistry , vol.38 , pp. 1426-1434
    • Pues, H.1    Bleimling, N.2    Holz, B.3    Wolcke, J.4    Weinhold, E.5
  • 20
    • 0033591248 scopus 로고    scopus 로고
    • Kinetic mechanism of cytosine DNA methyltransferase MspI
    • Bhattacharya,S. and Dubey,A. (1999) Kinetic mechanism of cytosine DNA methyltransferase MspI. J. Biol. Chem., 274, 14743-14749.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14743-14749
    • Bhattacharya, S.1    Dubey, A.2
  • 21
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic,P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase. Anal. Biochem., 237, 260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 22
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson,J., Higgins,D. and Gibson,T. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 25
    • 0030768931 scopus 로고    scopus 로고
    • The Hill equation revisited: Uses and misuses
    • Weiss,J. (1997) The Hill equation revisited: Uses and misuses. FASEB J., 11, 835-841.
    • (1997) FASEB J. , vol.11 , pp. 835-841
    • Weiss, J.1
  • 26
    • 0003043542 scopus 로고
    • The possible effects of aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill,A. (1910) The possible effects of aggregation of the molecules of haemoglobin on its dissociation curves. J. Physiol., 40, iv-vii.
    • (1910) J. Physiol. , vol.40
    • Hill, A.1
  • 27
    • 0018861067 scopus 로고
    • Cooperativity in enzyme function: Equilibrium and kinetic aspects
    • Neet,K. (1980) Cooperativity in enzyme function: Equilibrium and kinetic aspects. Methods Enzymol., 64, 139-192.
    • (1980) Methods Enzymol. , vol.64 , pp. 139-192
    • Neet, K.1
  • 28
    • 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. 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.2    Cheng, X.3
  • 29
    • 0034668039 scopus 로고    scopus 로고
    • DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases
    • Szegedi,S. and Gumport,R. (2000) DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases. Nucleic Acids Res., 28, 3972-3981.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3972-3981
    • Szegedi, S.1    Gumport, R.2
  • 30
    • 0020491202 scopus 로고
    • Purification and properties of the HpaI methylase
    • Yoo,O., Dwyer-Hallquist,P. and Agarwal,K. (1982) Purification and properties of the HpaI methylase. Nucleic Acids Res., 10, 6511-6519.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 6511-6519
    • Yoo, O.1    Dwyer-Hallquist, P.2    Agarwal, K.3
  • 31
    • 0034746572 scopus 로고    scopus 로고
    • Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog
    • Goedecke,K., Pignot,M., Goody,R., Scheidig,A. and Weinhold,E. (2001) Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog. Nature Struct. Biol., 8, 121-125.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 121-125
    • Goedecke, K.1    Pignot, M.2    Goody, R.3    Scheidig, A.4    Weinhold, E.5
  • 32
    • 0037007175 scopus 로고    scopus 로고
    • Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA mediyltransferases
    • Jeltsch,A. (2002) Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA mediyltransferases. ChemBioChem, 3, 274-293.
    • (2002) Chem Bio Chem , vol.3 , pp. 274-293
    • Jeltsch, A.1
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
    • Guex,N. and Peitsch,M. (1997) SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2
  • 35
  • 36
    • 33644915621 scopus 로고    scopus 로고
    • (ed.) Merck & Co., Inc., Whitehouse Station, NJ, USA, 13th edn
    • O'Neil,M., (ed.) (2001) The Merck Index, Merck & Co., Inc., Whitehouse Station, NJ, USA, 13th edn., p. 29.
    • (2001) The Merck Index , pp. 29
    • O'Neil, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.