Titlebook: Histone Methyltransferases; Methods and Protocol Raphaël Margueron,Daniel Holoch Book 2022 The Editor(s) (if applicable) and The Author(s),

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Determination of Histone Methyltransferase Structures in Complex with the Nucleosome by Cryogenic Elplex structures. Histone methyltransferases are a group of enzymes that posttranslationally methylate histone lysine and arginine residues on the nucleosome, providing important epigenetic signals that regulate gene expression. Here we describe a protocol to solve the structure of histone lysine met

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Genetic, Genomic, and Imaging Approaches to Dissect the Role of Polycomb Group Epigenetic Regulatorsct as part of a highly conserved set of chromatin regulators called Polycomb Group (PcG) proteins. Reaching a precise understanding of the roles of PcG proteins in the orchestration of differentiation and the maintenance of cell identity requires a variety of genetic and molecular approaches. Here,

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Profiling Histone Methylation in Low Numbers of Cellsod allows the generation of genome-wide profiles of the distribution of specific proteins in a given cellular context. Typical ChIP-seq experiments require millions of cells as input material and thus are not ideal to study many in vivo cell populations. Here, we describe an ultra-low-input native C

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Automated CUT & RUN Using the KingFisher Duo Primeable alternative to chromatin immunoprecipitation for the mapping of histone methylation patterns, generally producing results of equivalent quality while requiring less sequencing depth, less starting material and less effort. Automated CUT&RUN procedures have been developed to further facilitate c

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Bioinformatics Methods for ChIP-seq Histone Analysis by the emergence of the next-generation sequencing technologies. Among the different biological applications supported by recent sequencing technologies, ChIP-seq (Chromatin ImmunoPrecipitation followed by Sequencing) is one of the most powerful techniques which has dramatically changed our view of

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https://doi.org/10.1007/978-1-0716-2481-4chromatin compaction; automethylation; substrate interaction; X-ray crystallography; peptide probes

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