histone H2A deubiquitinase activity

Definition

Target type: molecularfunction

A histone deubiquitinase that cleaves ubiquitin from a histone H2A protein to which it is conjugated. [PMID:18226187, PMID:20436459]

Histone H2A deubiquitinase activity refers to the enzymatic removal of ubiquitin moieties from histone H2A. Ubiquitination is a reversible post-translational modification that plays a critical role in regulating chromatin structure and function. The addition of ubiquitin to histone H2A, known as monoubiquitylation, is catalyzed by histone H2A ubiquitin ligases (E3 ligases) and can lead to the recruitment of various proteins involved in gene regulation and DNA repair. Histone H2A deubiquitinases, also known as histone H2A DUBs, are a class of enzymes that specifically target the ubiquitin moieties attached to histone H2A. They are involved in a wide range of cellular processes, including:
- **Chromatin remodeling:** Histone H2A deubiquitinases can reverse the effects of histone H2A ubiquitination, which can alter chromatin accessibility and regulate gene expression. By removing ubiquitin from histone H2A, these enzymes can promote chromatin relaxation and facilitate the binding of transcription factors.
- **DNA repair:** Ubiquitylation of histone H2A is associated with DNA damage responses. Histone H2A deubiquitinases can contribute to the repair process by removing ubiquitin from damaged chromatin, allowing for the recruitment of repair machinery.
- **Cell cycle regulation:** Histone H2A deubiquitinases are involved in the regulation of cell cycle progression. They can modulate the expression of genes involved in cell cycle control and ensure proper DNA replication.
- **Immune response:** Histone H2A deubiquitinases have been implicated in regulating the immune response. They can influence the expression of genes involved in immune cell activation and cytokine production.
The molecular mechanism of histone H2A deubiquitinase activity involves a catalytic cysteine residue that facilitates the hydrolysis of the isopeptide bond between ubiquitin and histone H2A. This results in the release of ubiquitin and the deubiquitylation of histone H2A. Histone H2A deubiquitinases typically possess specific substrate recognition domains that ensure their selective activity towards histone H2A. These enzymes play a crucial role in maintaining the dynamic state of chromatin and contribute to various cellular processes.'
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Proteins (1)

Compounds (3)