統合TV 統合TVは、ライフサイエンス統合データベースセンター(DBCLS)が発信する生命科学分野の有用なデータベース(DB)やウェブツールの活用法を動画で紹介するウェブサイトです。くわしくは はじめての方へ をご覧ください。ご質問、ご要望は、お問い合わせ もしくは ライフサイエンスQA からお願いします。TogoTV beta ('togo' means 'integration' in Japanese) is an archive of tutorial videos expounding how to use biological databases and tools. Although most of contents are currently depicted in Japanese, you can find English contents in TogoTV international. Please post any comments, suggestions, and requests at each content page, e-mail to the address described at the bottom of each page or contact form. This site is provided by Database Center for Life Science (DBCLS) and funded by MEXT Integrated Database Project in Japan.

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2011-12-13

_ [presentation][English] ゲノムメチル化とエピジェネティクスI:Genome Methylation and Epigenetics I: Unity in Diversity - A Curious Case of DNA Methyltransferases

Unity in Diversity - A Curious Case of DNA Methyltransferases

本日の統合TVは、2011年度夏学期(4〜7月)に開講された、東京大学グローバルCOEプログラム「ゲノム情報ビッグバンから読み解く生命圏新領域創成科学特別講義IIから、Department of Biochemistry, Indian Institute of Science の Prof. Desirazu Narasimha Rao による「ゲノムメチル化とエピジェネティクスI: Unity in Diversity - A Curious Case of DNA Methyltransferases」をお送りします。

Youtube版はこちらです。

This lecture is talked by Prof. Desirazu Narasimha Rao from Department of Biochemistry, Indian Institute of Science entitled "Genome Methylation and Epigenetics I: Unity in Diversity - A Curious Case of DNA Methyltransferases". It is a part of "Frontier Sciences Special Lecture Series II" in The University of Tokyo Global COE Program: Deciphering Biosphere from Genome Big Bang.

Please note: For first 2 minutes, Prof. Ichizo Kobayashi who is an organizer of this lecture series introduced Prof. Rao in Japanese. After that, Prof Rao talked in English.

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Keywords: GCOE,genome big bang,methyltransferase

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Unity in Diversity - A Curious Case of DNA Methyltransferases Survival-Defense Mechanisms Action of R-M Enzymes Types of Restriction-Modification Enzymes Escherichia coli Methanococcus jannaschii Restriction-Modification (R-M) systems in Helicobacter pylori Conserved motifs in DNA methyltransferases Arranged of conserved motifs in the primary structure of exocyclic DNA MTases Sequencial kinetic mechanisms of observed with AdoMet-dependent DNA MTases Reaction mechanisms for exocyclic DNA methylation Proposed reaction mechanisms for C5-methylation Base flipping HhaI DNA methyltransferase - Structure/Base flipping HaelII DNA methyltransferase - Structure/Base flipping TaqI DNA methltransferase - Structure/Base flipping PvuII DNA methyltransferase Type III Restriction-Modification Enzymes Conserved Motifs in Type III R-M Enzymes EcoP15I DNA Methyltransferase Comparison of Restriction Digestion Patterns of Methylated and Unmethylated DNA Determination of Molecular Mass of EcoP15I MTase Binding of EcoP15I MTase to DNA Binding of EcoP15I MTase to DNA in Presence of ATP using EMSA Conserved Motifs in Type III R-M Enzymes Modification Phenotypes of Mutant mod Genes Photolabeling of Wild-type and Mutant EcoP15I MTases with methyl-3H-AdoMet Schematic Representation of Cysteine Residues of EcoP15I MTase Kinetic Parameters of Wild-type and Mutant EcoP15I MTases Schematic representation of cysteine residues of EcoP15I MTase In vivo methylation activity Characterization of M. EcoP15I H335A Duplex Substrates Steady State Fluorescence Emission Spectra of 2-AP Substituted DNA with EcoP15I MTase EcoP15I MTase Binding Results in Sensitivity of Thymine Base to Permangante Oxidation Effect of Divalent Metal Ions on Methylation Activity of EcoP15I MTase Time Dependence of Inactivation of EcoP15I MTase by Fe2+ Fe2+/Ascorbate Treatment of EcoP15I MTase Schematic Diagram Depicting the Putative Metal Binding Sites of EcoP15I MTase Digestion of pGEM3Zf(-) Plasmid DNA Encoding Wild-type or Mutant MTases with R.EcoP15I CD Spectra of Wild-type EcoP15I MTase Steady State Fluorescence Emission Spectra of 2AP Substituted DNA with EcoP15I MTase Steady State Fluorescence Emission Spectra of 2AP Substituted DNA with Mutant EcoP15I MTase Sequence Alignment Based Identification of Potential Mg2+ Binding Motif in Type III Methyltransferases Metal Ions and DNA NTases Schematic Diagram Depicting the Putative Metal Binding Sites of EcoP15I MTase Colonization ability of EcoP15I mutants Colonization ability of EcoP15I mutants Western Blot Analysis Methylation Activity of Wild-type and Mutant MTases Gel Filtration Chromatography CD spectroscopy of M357P MTase in Presence of Increasing Concentrations of MgCl2 Binding of Wild-type and Mutant MTases to DNA AdoMet Cross-linking - Wild-type and Mutant MTases Digestion of pUC18 DNA with Wild-type and Mutant M357P MTase Digestion of pUC18 DNA with Wild-type and Mutant MTases DNA cleavage is independent of orientation of CAGCAG site Kinetics of DNA Cleavage with different substrates Plasmid without CAGCAG sites Steady-State Kinetics of DNA Cleavage Mapping the cleavage site Mg2+nificent DNA Methyltransferase Organization of DNA MTases recognizing asymmetric target sequence Post-replicative base modifications by MTases recognizing asymmetric sequence Oligomerisation status Structures of MTases Oligomeric status of KpnI MTase KpnI MTase acts as dimer during methylation Fold-recognition alignment of M.KpnI and structurally characterized beta-class DNA MTases Modeled Dimer KpnI Methyltransferase Homology model of M.KpnI dimer Gel filtration analysis of I161 and I146 mutant MTases Acknowledgment


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