DNA methyltransferases - role and function / / Albert Jeltsch and Renata Z. Jurkowska, editors

• Pubblicazione: Cham, Switzerland : , : Springer, , [2022]; ©2022
• Edizione: Second edition.
• Descrizione fisica: 1 online resource (562 pages)
• Disciplina: 572.86
• Soggetto topico: DNA; Methyltransferases
• Persona (resp. second.): JeltschAlbert; JurkowskaRenata Z.
• Nota di bibliografia: Includes bibliographical references.
• Nota di contenuto: Intro -- Preface -- Contents -- About the Editors -- 1: Mechanisms and Biological Roles of DNA Methyltransferases and DNA Methylation: From Past Achievements to Future Challenges -- 1.1 Discovery of DNA Methylation -- 1.2 Discovery and Early Work on DNA MTases -- 1.3 DNA MTases Contain Conserved Amino Acids Sequence Motifs -- 1.4 Structure and Mechanism of DNA MTases -- 1.5 Molecular Evolution of MTases -- 1.6 Early Views on the Biological Role of DNA Methylation -- 1.7 Genetic Studies on DNMTs in Mammals -- 1.8 Structure, Function, and Regulation of Mammalian DNA MTases -- 1.9 Discovery of TET Enzymes -- 1.10 Methods for Site-Specific Detection of DNA Methylation -- 1.11 DNA MTases and Bacterial Epigenetics -- 1.12 Role of DNA Methylation in Cancer -- 1.13 Application of MTases in Artificial Epigenetic Systems -- 1.14 Conclusions and Outlook -- References -- 2: DNA Methylation in Prokaryotes -- 2.1 Introduction -- 2.2 CcrM Methylation -- 2.3 Dam Methylation -- 2.3.1 Role of Dam Methylation in DNA Mismatch Repair -- 2.3.2 Control of Chromosome Replication by Dam Methylation -- 2.3.3 Transcriptional Control by Dam Methylation -- 2.3.3.1 Temporal Regulation of Gene Expression by Dam Methylation -- 2.3.3.2 Regulation of Bistability by Dam Methylation -- 2.4 Phase Variable DNA Adenine Methylation -- 2.5 Additional Examples of DNA Adenine Methylation -- 2.6 C5-Methylcytosine -- 2.7 N4-Methylcytosine -- 2.8 Biomedical and Biotechnological Applications of Dam Methylation -- References -- 3: Domain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases -- 3.1 DNA Methylation and Methyltransferases in Mammals -- 3.2 Enzymes Responsible for the Establishment of DNA Methylation Patterns -- 3.2.1 PWWP Domain -- 3.2.2 ADD Domain -- 3.2.3 Catalytic Domain -- 3.2.4 Functions of Other Regions. ; 3.2.5 Factors That Guide Dnmt3 to the Regions to Be Methylated -- 3.2.6 Correlation Between de novo DNA Methylation and Histone Modifications -- 3.3 Enzymes Responsible for the Maintenance of DNA Methylation Patterns -- 3.3.1 NTD -- 3.3.2 RFTS Domain -- 3.3.3 CXXC -- 3.3.4 Two BAH Domains -- 3.3.5 Catalytic Domain -- 3.4 Cross-Talk Between De Novo-Type and Maintenance-Type DNA Methyltransferases -- 3.5 Conclusions and Perspective -- References -- 4: Enzymology of Mammalian DNA Methyltransferases -- 4.1 Introduction -- 4.2 General Features of Mammalian DNMTs -- 4.2.1 Structure and Domain Composition of Mammalian DNMTs -- 4.2.2 Catalytic Mechanism of C5-MTases -- 4.2.3 Regulation and Targeting of DNMTs -- 4.3 Structure, Function, and Mechanism of DNMT1 -- 4.3.1 Domain Composition of DNMT1 -- 4.3.2 Structures of DNMT1 and Allosteric Regulation -- 4.3.3 Specificity of DNMT1 -- 4.3.4 Processivity of DNMT1 -- 4.3.5 Allosteric Regulation and Targeting of DNMT1 -- 4.3.5.1 The DNMT1-PCNA Interaction -- 4.3.5.2 The DNMT1-UHRF1 Interaction -- 4.3.5.3 Binding of the DNMT1-RFTD to Ubiquitinated H3 Tails -- 4.3.5.4 Binding of DNMT1 to Heterochromatic Chromatin Marks -- 4.3.5.5 Regulation of Activity and Specificity of DNMT1 by Nucleic Acid Binding -- 4.3.6 PTMs of DNMT1 -- 4.3.6.1 Phosphorylation of DNMT1 -- 4.3.6.2 Acetylation and Ubiquitination of DNMT1 -- 4.3.6.3 Lysine Methylation of DNMT1 -- 4.4 Structure, Function, and Mechanism of DNMT3 Enzymes -- 4.4.1 Domain Composition of DNMT3 Proteins -- 4.4.2 Structures of DNMT3A and DNMT3B -- 4.4.3 Allosteric Regulation of DNMT3A -- 4.4.4 Specificity of DNMT3 Enzymes -- 4.4.5 Kinetic Mechanism of DNMT3 Enzymes -- 4.4.6 Oligomerization of DNMT3 Enzymes -- 4.4.6.1 Protein Multimerization of DNMT3 Enzymes -- 4.4.6.2 Multimerization of DNMT3A and DNMT3A/DNMT3L on DNA -- 4.4.7 Direct Chromatin Interaction of DNMT3 Enzymes. ; 4.4.7.1 Binding of the DNMT3 ADD Domain to H3 Tails -- 4.4.7.2 Binding of DNMT3 PWWP Domain to H3 Methylated at K36 -- 4.4.7.3 H2AK119ub Binding of DNMT3A1 -- 4.4.8 Interaction Partners of DNMT3s -- 4.4.8.1 DNMT3A/DNMT3L Interaction -- 4.4.8.2 Interaction of DNMT3A with MeCP2 -- 4.4.8.3 Other DNMT3A Interacting Proteins -- 4.4.9 Phosphorylation of DNMT3A -- 4.4.10 Binding of Regulatory DNA and RNA to DNMT3 Enzymes -- 4.5 Outlook -- References -- 5: Genetic Studies on Mammalian DNA Methyltransferases -- 5.1 Distinct Roles of Dnmt1 and Dnmt3 Families in DNA Methylation -- 5.1.1 Dnmt1: The Maintenance DNA Methyltransferase -- 5.1.2 Dnmt3 Family: Key Components of De Novo Methylation Machinery -- 5.1.3 Uhrf1: A Major Regulator of Maintenance DNA Methylation -- 5.2 Dnmts in Embryonic Development and Cellular Differentiation -- 5.2.1 Roles of Dnmts in Embryonic Development -- 5.2.2 Roles of Dnmts in Cellular Differentiation and Maintenance of Cell Identity. -- 5.2.3 DNMT Mutations in Human Diseases -- 5.3 Dnmts in Genomic Imprinting -- 5.3.1 Establishment of DNA Methylation Imprints during Gametogenesis -- 5.3.2 Maintenance of DNA Methylation Imprints during Development -- 5.3.3 Erasure of DNA Methylation Imprints in Primordial Germ Cells -- 5.3.4 Noncanonical Genomic Imprinting -- 5.4 Concluding Remarks -- References -- 6: Structure and Mechanism of Plant DNA Methyltransferases -- 6.1 Introduction -- 6.2 Structure and Mechanism of Plant DNA MTases -- 6.2.1 Structural Mechanism of the Maintenance of CHG Methylation in Plants -- 6.2.1.1 Overview of Plant CHG DNA Methylation -- 6.2.1.2 Structure and Mechanism of CMT3 -- 6.2.1.3 Structure and Mechanism of KRYPTONITE -- 6.2.2 Mechanism of CMT2-Mediated CHH Methylation -- 6.2.3 RNA-Directed DNA Methylation (RdDM) -- 6.2.3.1 Overview of RdDM -- 6.2.3.2 Structure and Mechanism of DRM2. ; 6.2.4 Potential Mechanism of MET1 in CG Methylation Maintenance -- 6.3 Conclusion and Perspective -- References -- 7: DNA Methylation in Honey Bees and the Unresolved Questions in Insect Methylomics -- 7.1 Introduction -- 7.2 Genotype to Phenotype -- 7.3 The Epigenetic Control of Gene Expression -- 7.4 DNA Methylation -- 7.4.1 Conserved and Non-Conserved Features of DNA Methylation Enzymology in Animals -- 7.4.2 DNMTs and Establishing DNA Methylation Patterns in the Honey Bee -- 7.4.3 How do TET Enzymes Contribute to Gene Regulation in the Honey Bees and Other Insects? -- 7.4.4 DNA Methylation Patterns Across Invertebrates -- 7.4.5 Does Gene Body Methylation Direct Gene Expression in Insects? -- 7.5 Conclusion -- References -- 8: N6-methyladenine: A Rare and Dynamic DNA Mark -- 8.1 Introduction -- 8.2 Types of DNA Modifications -- 8.3 Discovery of 6mA in Various Eukaryotes -- 8.4 Abundance of 6mA -- 8.5 Methods of Detecting 6mA -- 8.6 6mA Regulating Enzymes -- 8.6.1 DNA Methyltransferases -- 8.6.2 Mechanism of 6mA Methyltransferases -- 8.7 DNA Adenine Demethylation -- 8.8 6mA Binding Proteins -- 8.9 Biological Functions of 6mA -- 8.9.1 Effects of Adenine Methylation on DNA Structure -- 8.9.2 Restriction-Modification Systems -- 8.9.3 DNA Damage Control -- 8.9.4 Effect on Transcription -- 8.9.5 Nucleosome Positioning -- 8.9.6 Cell Cycle Regulation -- 8.9.7 Transgenerational Inheritance -- 8.10 Conclusions and Future Directions -- References -- 9: Pathways of DNA Demethylation -- 9.1 DNA Methylation: One Building Block of the Epigenome -- 9.2 DNA Methylation Reprogramming: Setting the Epigenome Up for Success -- 9.3 Active DNA Demethylation: The Hunt for the `Demethylase´ -- 9.4 Direct DNA Demethylation -- 9.5 Indirect Loss of DNA Methylation -- 9.5.1 Role of Cytosine Deamination in DNA Demethylation. ; 9.5.2 Methylcytosine Oxidation-Based Demethylation Mechanisms -- 9.6 Chromatin Remodelling, DNA Replication, and Repair: The Epigenetic Triumvirate -- 9.7 Replication-Coupled Loss of DNA Methylation: Passive Demethylation -- 9.8 Resetting and Erasure of the Germline: A Barrier Against Transgenerational Inheritance -- 9.8.1 Demethylation During Preimplantation Development -- 9.9 Removing the Molecular Escapement Mechanism to Cell Fate and Aging by Modulation of DNA Methylation: How Cells Can Turn Ba... -- References -- 10: Structure and Function of TET Enzymes -- 10.1 Introduction -- 10.2 Discovery of TET-Mediated 5mC Oxidation -- 10.2.1 TET-Mediated Iterative Oxidation of 5mC -- 10.2.2 TET-Dependent DNA Demethylation -- 10.2.3 Mechanisms and Processivity for TET-Mediated Oxidation Reaction -- 10.2.4 Oxidation of 5mrC-RNA and 6mA-DNA -- 10.3 Function of TET Enzymes -- 10.3.1 Distribution of TET Enzymes and 5mC Oxidation Derivatives -- 10.3.2 TET in ESCs and Cell Differentiation -- 10.3.3 TETs Mediate Epigenetic Reprogramming in Early Embryogenesis and PGC Development -- 10.3.4 TET Enzymes in Somatic Cell Reprogramming -- 10.3.5 TET Enzymes and Cancer -- 10.3.6 TET Enzymes in Neural System -- 10.4 Structure of TET Enzymes -- 10.4.1 Domain Structure of Human TET Enzymes -- 10.4.2 Crystal Structure of the TET2-5mC-DNA Complex -- 10.4.3 Crystal Structure of the NgTet1-5mC-DNA Complex -- 10.4.4 Structural Basis for Substrate Preference in TET-Mediated Oxidation -- 10.4.5 Crystal Structure of Algal TET Homologue CMD1 in Complex with VC and 5mC-DNA -- 10.5 Regulation of TET Enzymes -- 10.5.1 Inhibitors -- 10.5.2 Activators -- 10.5.3 Interacting Proteins -- 10.6 Concluding Remarks -- References -- 11: Proteins That Read DNA Methylation -- 11.1 Introduction -- 11.2 The Methyl-CpG-Binding Domain Family -- 11.2.1 MeCP2 -- 11.2.2 MBD1 -- 11.2.3 MBD2. ; 11.2.4 MBD3.
• Titolo autorizzato: DNA Methyltransferases - Role and Function
• ISBN: 3-031-11454-X
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Lingua di pubblicazione: Inglese
• Record Nr.: 9910629285803321
• Lo trovi qui: Univ. Federico II
• Serie: Advances in experimental medicine and biology ; ; Volume 1389.