Acetyltilstander

Acetyltilstander, or acetylation states, describe the pattern and degree of acetyl modification on biomolecules, most often proteins. The term covers which sites are acetylated and how extensively, including the fraction of molecules carrying the modification in a given sample.

Chemically, acetylation adds an acetyl group to nucleophilic sites, most commonly lysine residues and protein N-termini. In cells, acetyltransferases transfer the acetyl group from acetyl-CoA, while deacetylases remove it. This modification changes charge, conformation, and interaction properties of the target.

In histones, acetylation reduces positive charge, decreases histone-DNA interaction, and promotes chromatin accessibility and transcription. In non-histone proteins, acetylation can alter enzymatic activity, subcellular localization, stability, and protein-protein interactions.

Detecting acetyltilstander combines mass spectrometry to identify sites and estimate site occupancy with antibody-based methods (anti-acetyl-lysine) for enrichment and profiling. Quantitative approaches aim to determine the stoichiometry of acetylation at individual sites.

Biological and medical relevance: acetylation states are dynamic and responsive to metabolism and signaling. Dysregulation is linked to cancer, neurodegenerative disease, and metabolic disorders. Therapeutic strategies include inhibitors of histone deacetylases and other regulators of acetylation.