histone H2AK5 acetyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: acetyl-CoA + histone H2A L-lysine (position 5) = CoA + histone H2A N6-acetyl-L-lysine (position 5). [EC:2.3.1.48]

Histone H2AK5 acetyltransferase activity refers to the enzymatic activity of proteins that specifically acetylate lysine 5 on histone H2A. This modification plays a crucial role in regulating gene expression and chromatin structure. Acetylation of lysine 5 on histone H2A is generally associated with increased gene transcription. The addition of an acetyl group to lysine 5 neutralizes its positive charge, which weakens the interaction between the histone and DNA. This, in turn, allows for greater accessibility of the DNA to transcription factors and other regulatory proteins. The specific mechanisms by which H2AK5 acetylation influences gene expression are complex and depend on the context of the cellular environment. However, several studies have demonstrated that H2AK5 acetylation is involved in a wide range of cellular processes, including DNA replication, DNA repair, and cell differentiation. In addition to its role in gene expression, H2AK5 acetylation has also been implicated in other cellular processes, such as DNA replication and repair. For instance, H2AK5 acetylation has been shown to promote the recruitment of DNA repair proteins to sites of DNA damage, suggesting a role in the repair of damaged DNA. H2AK5 acetylation is a dynamic process that is regulated by the interplay of histone acetyltransferases (HATs) and histone deacetylases (HDACs). HATs, such as the p300/CBP and GCN5 families of enzymes, catalyze the addition of acetyl groups to lysine residues on histones, including H2AK5. Conversely, HDACs, such as the HDAC1/2 and SIRT1 families of enzymes, remove acetyl groups from histones, including H2AK5. The balance between HAT and HDAC activity determines the acetylation status of H2AK5 and ultimately contributes to the regulation of gene expression and other cellular processes.'
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Proteins (1)

Compounds (5)