Histone Modifying Enzymes
Histone Modifying Enzymes - Related Videos
02:32
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,...
11:16
Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Cited by 23 •
2012
This article will describe the procedure for synthesizing a hydrophobically modified Nafion enzyme immobilization membrane and how to immobilize proteins and/or enzymes within the membrane and test their specific activity.
11:33
Investigating Interactions Between Histone Modifying Enzymes and Transcription Factors in vivo by Fluorescence Resonance Energy Transfer
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2022
Fluorescence resonance energy transfer (FRET) is an imaging technique for detecting protein interactions in living cells. Here, a FRET protocol is presented to study the association of histone-modifying enzymes with transcription factors that recruit them to the target promoters for epigenetic regulation of gene expression in plant tissues.
03:01
Detection of Target Enzyme Expression in Genetically Modified Bacterial Cells
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2025
Source: Kim, H. et. al., Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System. J. Vis. Exp. (2016)This video demonstrates a genetic screening method to detect enzyme expression using metagenomic fosmid libraries and chromogenic substrates. Flow cytometry identifies and isolates single cells producing colored products, enabling high-throughput selection of active enzyme-expressing cells.
09:34
Identification of Modified Histones as Binding Substrates of Human Spindlin Family Member 4 (SPIN4) by Peptide Arrays and Native Nucleosome Pulldown
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2026
Genetic variants in human Spindlin Family Member 4 (SPIN4) have recently been identified in patients with bone overgrowth, a novel developmental disorder. A protocol and new results describing the biochemical identification of modified histones in the context of nucleosomes as SPIN4 binding substrates are presented.
FAQs
Acetyltransferases and deacetylases act in opposite directions by adding or removing acetyl-related marks, while methyltransferases and demethylases add or remove methyl-related marks. These changes can alter DNA accessibility or influence which regulatory proteins bind histone tails. As a result, enzyme activity may support either transcriptional activation or repression, depending on the modification and cellular context.
Histone marks influence gene expression through chromatin behavior rather than by rewriting genetic information. A modification can change how accessible DNA is within chromatin, making regulatory regions more or less available. It can also recruit proteins that promote or repress transcription. This provides a mechanism for cells to adjust gene activity while preserving the underlying DNA sequence.
The effect of histone modifying enzymes depends on the biological program active in a cell. During development, their activity helps coordinate changing patterns of gene expression and cell identity. Environmental signals can also alter regulatory activity, allowing cells to respond without changing their DNA sequence. These context-dependent effects help explain why similar enzymes can contribute to different cellular outcomes.
By regulating the accessibility and transcriptional status of genes, these enzymes help establish which genetic programs remain active in a particular cell. Their activity contributes to developmental transitions and maintenance of cell identity, rather than simply controlling one isolated gene. Studying these regulatory patterns helps explain how cells acquire specialized functions as organisms develop.
Research commonly examines how these enzymes contribute to development, cell identity, DNA repair, and responses to environmental signals. The central question is how changes in histone-tail marks influence chromatin structure and gene regulation during each process. Comparing these contexts can reveal how cells coordinate genome use with changing physiological or developmental demands.
Abnormal histone modification can disrupt normal gene expression, making these enzymes relevant to disease research. In cancer and neurological disease studies, researchers examine whether altered enzyme activity contributes to inappropriate activation or repression of genes. This work also supports interest in epigenetic therapies, which aim to address disease-associated regulatory disturbances through mechanisms affecting histone modification.