histone H4K12 acetyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: acetyl-CoA + histone H4 L-lysine (position 12) = CoA + histone H4 N6-acetyl-L-lysine (position 12). [EC:2.3.1.48]

Histone H4K12 acetyltransferase activity is a molecular function that describes the ability of an enzyme to catalyze the transfer of an acetyl group from acetyl-CoA to the lysine residue at position 12 (K12) of histone H4. This acetylation event is a crucial regulatory mechanism in eukaryotic cells, playing a significant role in chromatin remodeling and gene expression.

Histone H4 is a core histone protein that forms the nucleosome, the fundamental unit of chromatin structure. The N-terminal tail of histone H4 protrudes from the nucleosome and is subject to various post-translational modifications, including acetylation. Acetylation at lysine 12 of histone H4 (H4K12ac) is associated with increased gene expression.

Histone H4K12 acetyltransferases (HATs) are a family of enzymes that catalyze this acetylation reaction. These enzymes recognize specific sequence motifs within the histone H4 tail and utilize acetyl-CoA as a substrate. The acetylation of lysine 12 neutralizes the positive charge of the lysine residue, reducing the affinity of the histone tail for DNA. This weakening of the histone-DNA interaction allows for a more relaxed chromatin structure, making the DNA more accessible to transcription factors and other regulatory proteins.

The precise molecular mechanisms by which H4K12 acetylation regulates gene expression are still being elucidated. However, it is believed that this modification can:

- Recruit transcriptional coactivators: H4K12ac can act as a docking site for proteins that promote gene transcription, such as bromodomain-containing proteins.
- Alter chromatin structure: Acetylation can induce changes in nucleosome positioning and dynamics, facilitating the recruitment of transcription machinery.
- Modulate interactions with other histone modifications: H4K12ac can cooperate with other histone modifications to fine-tune gene expression.

Dysregulation of H4K12 acetyltransferase activity can contribute to various diseases, including cancer and developmental disorders. Therefore, understanding the molecular function of this activity is crucial for developing therapeutic strategies that target chromatin remodeling and gene expression pathways.'
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Proteins (4)

Compounds (8)