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Histone acetylation leads to a relaxation of DNA, facilitating access for transcription machinery and allowing for active gene expression. The addition of acetyl groups to lysine residues on histone proteins neutralizes their positive charge, reducing the histones' affinity for the negatively charged DNA. This relaxed structure enables easier access for RNA polymerase and various transcription factors to bind to DNA, promoting transcription.

This process is a key mechanism in the regulation of gene expression and is associated with euchromatin formation, which is the less condensed form of chromatin. By contrast, other factors such as heterochromatin formation, transcription inhibition, or increased DNA binding would not be the direct outcomes of histone acetylation. Instead, histone acetylation is primarily linked to the enhancement of transcriptional activity through a more open chromatin structure.