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Histone Modification

Histone Modification

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...

Histone Modification

Histone Modification

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Regulated Protein Degradation

Regulated Protein Degradation

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

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Related Experiment Video

Updated: Jan 8, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

Sirtuin 2 Regulates Histone Glycation as a Semi-deglycase.

Huapeng Li^1,2, Yvonne Ritsema^1,2, Zeng Lin^1,2

¹Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, Indiana 47907, United States.

|December 19, 2025

Summary

This summary is machine-generated.

Sirtuin 2 (SIRT2) acts as a semi-deglycase, removing acids from modified histones. This enzyme, with DJ-1, helps prevent cell damage from methylglyoxal (MGO) and glyoxal (GO) in cancer.

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Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

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Last Updated: Jan 8, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

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Published on: May 5, 2022

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

Published on: October 18, 2024

Area of Science:

Biochemistry
Molecular Biology
Cancer Research

Background:

Methylglyoxal (MGO) and glyoxal (GO) are reactive carbonyl species implicated in cancer development.
MGO/GO-induced histone glycation affects chromatin structure and cancer progression.
Previous work identified DJ-1 and PAD4 as enzymes with glyoxalase/deglycase activities against MGO/GO-histone modifications.

Purpose of the Study:

To identify novel regulators of histone glycation.
To investigate the role of histone deacetylase SIRT2 in antagonizing MGO/GO-induced histone modifications.
To elucidate the mechanism by which SIRT2 modulates histone glycation.

Main Methods:

Biochemical assays to assess SIRT2's enzymatic activity on modified histone residues.
Investigating the interaction and combined function of SIRT2 and DJ-1.
Utilizing an enzymatically inactive DJ-1 mutant (DJ-1-C106A) in experiments.

Main Results:

SIRT2 identified as a "semi-deglycase" removing lactic and glycolic acids from specific histone adducts.
These adducts (ε-N-l-lactyllysine and hydroxyacetyllysine) are derived from MGO/GO-lysine modifications.
SIRT2, with DJ-1-C106A, converts MGO/GO into lactate and glycolate, mitigating cytotoxicity.

Conclusions:

SIRT2 is a newly discovered regulator of histone glycation.
SIRT2 plays a protective role against MGO and GO cytotoxicity.
The SIRT2-DJ-1 axis offers a potential therapeutic target for managing MGO/GO-related pathologies in cancer.