Histone Demethylase
Histone Demethylase - Related Videos
07:02
Application of MassSQUIRM for Quantitative Measurements of Lysine Demethylase Activity
0 Views •
Cited by 1 •
2012
We present a method for using MALDI mass spectrometry and reductive methylation chemistry to quantify changes in lysine methylation.
02:32
Histone Modification
0 Views •
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,...
02:30
Histone Variants at the Centromere
0 Views •
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...
09:47
Analysis of Histone Antibody Specificity with Peptide Microarrays
0 Views •
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.
11:02
Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
0 Views •
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.
FAQs
The two enzyme groups remove methyl groups through different chemical routes. LSD1-family enzymes use flavin adenine dinucleotide during oxidative demethylation, whereas JmjC-domain enzymes require iron and 2-oxoglutarate to hydroxylate the methyl group before it is removed. These distinct cofactor requirements provide a mechanistic basis for distinguishing enzyme activities in studies of chromatin regulation.
Activity depends on the enzyme’s selectivity for particular methylated lysine residues and on the catalytic mechanism available to process them. Consequently, different demethylases can influence different chromatin states rather than producing a uniform change across all histones. This site-specific behavior helps connect individual enzymes with particular patterns of gene regulation.
Selective activity allows researchers to relate changes at defined histone sites to broader chromatin and gene-expression outcomes. Instead of treating histone methylation as a single, uniform signal, investigators can examine how particular demethylases reshape specific chromatin states. This precision is especially relevant for understanding differentiation, development, DNA repair, and disease-associated regulation.
By changing methylation patterns on histones, these enzymes can alter chromatin states, which affects how DNA is packaged and how readily genes are expressed. Their effects therefore extend beyond the modified protein itself: changes in histone marks can contribute to cellular programs such as differentiation and development, as well as responses involving DNA repair.
Research commonly connects these enzymes with cell differentiation, development, DNA repair, and regulation of genes associated with disease. Studying their activity in these settings helps explain how chromatin states change as cells acquire specialized functions or respond to genomic stress. It also provides biological context for investigating abnormal gene regulation in disorders.
Their selective effects on methylated lysine residues and gene-regulatory chromatin states make histone demethylases attractive subjects for therapeutic research. If disease-associated gene regulation depends on particular demethylase activities, those enzymes may offer points for intervention. The overview specifically identifies cancer and other disorders as contexts in which this possibility is being explored.