Structure, function and mechanism of exocyclic DNA methyltransferases.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Biochemical Journal

• Publication date

  2006-10-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1042/BJ20060854PMID 16987108PMCID PMC1609917
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase

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• REBASE—restriction enzymes and DNA methyltransferases

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• Functional Characterization of Escherichia coli DNA Adenine Methyltransferase, a Novel Target for Antibiotics*

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  2004cited by this paper
• Stopped-flow and mutational analysis of base flipping by the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase.

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• Simultaneous DNA Binding, Bending, and Base Flipping

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  2004cited by this paper
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  2003cited by this paper
• DNA (Cytosine-N 4-)- and -(Adenine-N 6-)-methyltransferases Have Different Kinetic Mechanisms but the Same Reaction Route

  2003cited by this paper
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  2003cited by this paper
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• Structures of Liganded and Unliganded RsrI N6-Adenine DNA Methyltransferase

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• Functional analysis of BamHI DNA cytosine-N4 methyltransferase.

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• Kinetic and Catalytic Properties of Dimeric KpnI DNA Methyltransferase*

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• Characterization of the LlaCI methyltransferase from Lactococcus lactis subsp. cremoris W15 provides new insights into the biology of type II restriction-modification systems.

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• Bacteriophage T4 Dam DNA-[N6-adenine]Methyltransferase

  2002cited by this paper
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  2002influential reference
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  2002cited by this paper
• Sequence permutations in the molecular evolution of DNA methyltransferases

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• A dual role for substrate S-adenosyl-L-methionine in the methylation reaction with bacteriophage T4 Dam DNA-[N6-adenine]-methyltransferase.

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• Identification of the Active Oligomeric State of an Essential Adenine DNA Methyltransferase from Caulobacter crescentus *

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• Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA.

  2001cited by this paper
• Structure of the N6-adenine DNA methyltransferase M•TaqI in complex with DNA and a cofactor analog

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• AdoMet-dependent methylation, DNA methyltransferases and base flipping.

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• Molecular enzymology of the EcoRV DNA-(Adenine-N (6))-methyltransferase: kinetics of DNA binding and bending, kinetic mechanism and linear diffusion of the enzyme on DNA.

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• Pre-steady state kinetics of bacteriophage T4 dam DNA-[N(6)-adenine] methyltransferase: interaction with native (GATC) or modified sites.

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• DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases.

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• Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase.

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• Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.

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• Binding of EcoP15I DNA methyltransferase to DNA reveals a large structural distortion within the recognition sequence.

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• BACTERIAL DNA METHYLTRANSFERASES

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• DNA Bending by EcoRI DNA Methyltransferase Accelerates Base Flipping but Compromises Specificity*

  1999cited by this paper
• Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin.

  1999cited by this paper
• 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.

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• On the Substrate Specificity of DNA Methyltransferases

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• Effect of base analog substitutions in the specific GATC site on binding and methylation of oligonucleotide duplexes by the bacteriophage T4 Dam DNA-[N6-adenine] methyltransferase.

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• M.TaqI: possible catalysis via cation-pi interactions in N-specific DNA methyltransferases.

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• Base flipping.

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• Functional Roles of Conserved Amino Acid Residues in DNA Methyltransferases Investigated by Site-directed Mutagenesis of theEcoRV Adenine-N 6-methyltransferase*

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• Kinetics of methylation and binding of DNA by the EcoRV adenine-N6 methyltransferase.

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• The DNA binding characteristics of the trimeric EcoKI methyltransferase and its partially assembled dimeric form determined by fluorescence polarisation and DNA footprinting.

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• The crystal structure of Haelll methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing

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• Structure and function of DNA methyltransferases.

  1995influential reference
• Dam methylase from Escherichia coli: kinetic studies using modified DNA oligomers: hemimethylated substrates.

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  1995cited by this paper
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  1994cited by this paper
• The DNA (cytosine-5) methyltransferases

  1994cited by this paper
• Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5'-CAGCAG-3'.

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• A mutational analysis of the two motifs common to adenine methyltransferases.

  1994cited by this paper
• Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine.

  1994cited by this paper
• Effects of modified bases in sequence recognition by ClaI endonuclease and ClaI methylase.

  1993cited by this paper
• The role of the preserved sequences of Dam methylase.

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• DNA recognition by the EcoK methyltransferase. The influence of DNA methylation and the cofactor S-adenosyl-L-methionine.

  1993cited by this paper
• Biology of DNA restriction.

  1993cited by this paper
• Presteady state kinetics of an S-adenosylmethionine-dependent enzyme. Evidence for a unique binding orientation requirement for EcoRI DNA methyltransferase.

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• Kinetic characterization of the EcaI methyltransferase.

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• Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli.

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• In vitro specificity of EcoRI DNA methyltransferase.

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• Purification and biochemical characterization of the EcaI DNA methyltransferase.

  1992cited by this paper
• Cofactor and DNA interactions in EcoRI DNA methyltransferase. Fluorescence spectroscopy and phenylalanine replacement for tryptophan 183.

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