Histone acetylation at lysine residues is an important epigenetic marker and can be measured with the use of histone lysine acetylation antibodies. Acetylation of histones reduces the interaction of histone N-termini with the phosphate groups of DNA, thereby loosening chromatin and opening it up for increased gene transcription. Acetylation of H3K14, for instance, has been linked to transcriptional activation and specifically DNA repair.
The addition of acetyl groups to histones, a process catalyzed by HAT enzymes (histone acetyltransferases), causes chromatin to relax and become more open (a state called euchromatin). HATs are therefore responsible for promoting euchromatin formation and gene expression. Conversely, deacetylation can cause chromatin to condense and become more closed (a state called heterochromatin), which represses the transcription of genes.
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