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Biochemical Analysis of Histone Succinylation
Atsushi Yokoyama1,2, Shogo Katsura2, Akira Sugawara1
1Department of Molecular Endocrinology, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan.
Histone succinylation, a newly identified posttranslational modification (PTM), is now confirmed to be enzymatic. This study provides the first direct evidence of an enzyme catalyzing histone succinylation in the nucleus.
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- Posttranslational modifications (PTMs) regulate protein function and stability.
- Histone PTMs are crucial for gene expression via chromatin remodeling.
- Histone succinylation is a recently discovered PTM, but its enzymatic basis is unknown.
Purpose of the Study:
- To investigate whether histone succinylation is an enzymatic process.
- To identify the source of histone succinylation activity in cell nuclei.
Main Methods:
- In vitro assays using HepG2 cell nuclear extracts.
- Fractionation of nuclear extracts using 1.0 M KCl.
Main Results:
- Whole nuclear extracts showed no histone succinylation activity.
- A specific fraction (1.0 M KCl) of nuclear extracts exhibited histone succinylation activity.
- This indicates the presence of an enzyme responsible for histone succinylation.
Conclusions:
- Histone succinylation is an enzymatic posttranslational modification.
- This finding adds to the understanding of the histone code and gene regulation.
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