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DNA methyltransferases - role and function / / Albert Jeltsch and Renata Z. Jurkowska, editors
| DNA methyltransferases - role and function / / Albert Jeltsch and Renata Z. Jurkowska, editors |
| Edizione | [Second edition.] |
| Pubbl/distr/stampa | Cham, Switzerland : , : Springer, , [2022] |
| Descrizione fisica | 1 online resource (562 pages) |
| Disciplina | 572.86 |
| Collana | Advances in experimental medicine and biology |
| Soggetto topico |
DNA
Methyltransferases |
| ISBN | 3-031-11454-X |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| 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. |
| Record Nr. | UNINA-9910629285803321 |
| Cham, Switzerland : , : Springer, , [2022] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
DNA Methyltransferases - Role and Function / / edited by Albert Jeltsch, Renata Z. Jurkowska
| DNA Methyltransferases - Role and Function / / edited by Albert Jeltsch, Renata Z. Jurkowska |
| Edizione | [1st ed. 2016.] |
| Pubbl/distr/stampa | Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 |
| Descrizione fisica | 1 online resource (VIII, 535 p. 61 illus., 57 illus. in color.) |
| Disciplina | 572.86 |
| Collana | Advances in Experimental Medicine and Biology |
| Soggetto topico |
Cell biology
Gene expression Cytogenetics Cell Biology Gene Expression |
| ISBN | 3-319-43624-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Mechanisms and biological roles of DNA methylation and DNA methyltransferases – from past achievements to future challenges -- DNA and RNA pyrimidine nucleobase alkylation at the carbon-5 position -- Bacterial DNA methylation and methylomes -- Domain structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA methyltransferases -- Enzymology of mammalian DNA methyltransferases -- Genetic studies on mammalian DNA methyltransferases -- The role of DNA methylation in cancer -- Structure and mechanism of plant DNA methyltransferases -- DNA methylation and gene regulation in honey bees: from genome-wide analyses to obligatory epi-alleles -- N6-methyladenine: a conserved and dynamic DNA mark -- Pathways of DNA demethylation -- Structure and function of TET enzymes -- Proteins that read DNA methylation -- DNA base flipping – a general mechanism for writing, reading, and erasing DNA modifications -- Current and emerging technologies for the analysis of the genome-wide and locus-specific DNA methylation patterns -- DNA methyltransferase inhibitors – development and applications -- Rewriting DNA methylation signatures at will: the curable genome within reach? -- Engineering and directed evolution of DNA methyltransferases -- DNA labeling using DNA methyltransferases. |
| Record Nr. | UNINA-9910150454903321 |
| Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Role of DNA Methyltransferases in the Epigenome / / edited by Albert Jeltsch, Humaira Gowher
| Role of DNA Methyltransferases in the Epigenome / / edited by Albert Jeltsch, Humaira Gowher |
| Pubbl/distr/stampa | Basel : , : MDPI - Multidisciplinary Digital Publishing Institute, , 2020 |
| Descrizione fisica | 1 online resource (150 pages) : illustrations |
| Disciplina | 574.1 |
| Soggetto topico | Enzymes |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910673902503321 |
| Basel : , : MDPI - Multidisciplinary Digital Publishing Institute, , 2020 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Structure, Activity, and Function of Protein Methyltransferases
| Structure, Activity, and Function of Protein Methyltransferases |
| Autore | Jeltsch Albert |
| Pubbl/distr/stampa | Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022 |
| Descrizione fisica | 1 electronic resource (292 p.) |
| Soggetto topico |
Research & information: general
Biology, life sciences Biochemistry |
| Soggetto non controllato |
protein lysine methylation
H3K9 methylation PKMT enzyme specificity enzyme regulation heterochromatin protein post-translational modification NSD3 WHSC1L1 structure and function protein arginine methylation PRMT7 epigenetics cancer immunity pluripotency SETDB1 methyltransferase schizophrenia Huntington's disease Rett syndrome Prader-Willi syndrome congenital heart diseases inflammatory bowel disease MLL2 structure H3K4me3 chromatin regulation disease dystonia NSD1 H3K36 SOTOS NUP98-NSD1 AML PRMT6 post-translational modification H3R2me2a SETD3 posttranslational modifications protein histidine methylation actin polymerization cytoskeleton enteroviruses oncogenesis PRMT5 cardiovascular disease neurodegenerative diseases diabetes inflammation G9a GLP EHMT2 EHMT1 post translational modification lysine methylation N-terminal methylation translation eEF1A METTL13 neuron synapse dendritic spine actin cytoskeleton GTPase PRMT1 arginine methylation H4R3 methylation transcriptional regulation cell signaling DNA damage repair PRMT2 SH3 SETMAR Metnase H3K36me2 Hsmar1 non-homologous end joining repair NHEJ transposase transposable elements histone SET7/9 SETD7 lysine-specific methyltransferase (PKMT) cell proliferation stress response post-translational protein modification |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910566479603321 |
Jeltsch Albert
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| Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||