internal protein amino acid acetylation

Definition

Target type: biologicalprocess

The addition of an acetyl group to a non-terminal amino acid in a protein. [GOC:mah]

Internal protein amino acid acetylation is a fundamental post-translational modification where acetyl groups (CH3CO) are added to amino acid residues within a protein molecule. This process plays a vital role in regulating a diverse range of cellular processes, including protein stability, localization, interactions with other proteins, and enzymatic activity. The most commonly acetylated amino acid residues are lysine (Lys) and, to a lesser extent, arginine (Arg) and histidine (His).

The acetylation reaction is catalyzed by a family of enzymes known as lysine acetyltransferases (KATs), which utilize acetyl-CoA as a donor of the acetyl group. Acetyl-CoA is a key metabolic intermediate that carries acetyl groups derived from the breakdown of carbohydrates, fatty acids, and amino acids. KATs exhibit substrate specificity and are often associated with specific cellular compartments and pathways.

Internal protein acetylation occurs in a variety of contexts and can be influenced by a range of factors. Some key aspects include:

- **N-terminal acetylation:** The N-terminal amino acid of many proteins undergoes acetylation shortly after translation. This modification is typically catalyzed by N-terminal acetyltransferases (NATs) and is often essential for protein stability and folding.
- **Lysine acetylation:** Lysine residues within the protein sequence can be acetylated by specific KATs. This modification can alter the electrostatic properties of the protein, affecting its interactions with other molecules, including DNA, RNA, and other proteins.
- **Regulatory acetylation:** Acetylation can be dynamically regulated in response to cellular signals, such as stress, nutrient availability, and developmental cues. These changes in acetylation patterns can alter protein function and contribute to the adaptation of cells to different environmental conditions.
- **Crosstalk with other modifications:** Acetylation often interacts with other post-translational modifications, such as phosphorylation and ubiquitination, creating complex regulatory networks.

The functional consequences of internal protein acetylation are diverse and encompass a wide range of cellular processes:

- **Protein stability:** Acetylation can influence protein stability by altering its conformation and susceptibility to proteolytic degradation.
- **Protein localization:** Acetylation can affect protein localization by altering its affinity for specific cellular compartments or by modulating interactions with transport machinery.
- **Protein-protein interactions:** Acetylation can create or disrupt protein-protein interactions by altering the electrostatic surface properties of proteins.
- **Enzyme activity:** Acetylation can regulate enzyme activity by influencing substrate binding, catalytic efficiency, or protein conformation.

Understanding the mechanisms and functional consequences of internal protein acetylation is crucial for unraveling the intricate regulatory networks that govern cellular processes. This knowledge has implications for understanding human health and disease, as dysregulation of acetylation has been implicated in various pathologies, including cancer, neurodegenerative disorders, and metabolic diseases.'
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Proteins (2)

Compounds (41)