Set7/9 Histone Methyltransferase

Set7/9 histone methyltransferase is a lysine methyltransferase that regulates gene expression and chromatin function by adding methyl groups to histone and selected nonhistone proteins. Using S-adenosyl-L-methionine as the methyl donor, the SET7/9 catalytic domain transfers a methyl group to specific lysine residues, including histone H3 lysine 4, creating binding or regulatory signals without altering the DNA sequence. These modifications can influence chromatin accessibility, transcription, DNA repair, and cell-cycle control. Studying Set7/9 helps clarify how epigenetic information is established and interpreted in biology and supports research into development, cellular stress responses, and disease-associated gene regulation.

Set7/9 Histone Methyltransferase - Related Videos

Education

JoVE Core - Molecular Biology

Histone Modification

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2020

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression. Acetylation The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

Histone Variants at the Centromere

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2020

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...

Research

JoVE Journal - Biology

In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity

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Cited by 2 •

2016

The present report describes an in vitro enzymatic assay to measure phosphatidylethanolamine methyltransferase activity using Leishmania cell extracts. This assay is based on the transfer of a radioactive methyl group from S-[Methyl-3H]adenosyl-L-methionine onto endogenous phosphatidylethanolamine.

Analysis of Histone Antibody Specificity with Peptide Microarrays

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Cited by 22 •

2017

This manuscript describes methods for applying peptide microarray technology to specificity profiling of antibodies that recognize histones and their post-translational modifications.

Research

JoVE Journal - Biology
Free Sample

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Cited by 227 •

2016

This protocol outlines a fully integrated workflow for characterizing histone post-translational modifications using mass spectrometry (MS). The workflow includes histone purification from cell cultures or tissues, histone derivatization and digestion, MS analysis using nano-flow liquid chromatography and instructions for data analysis. The protocol is designed for completion within 2 - 3 days.

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