Beyond the histone tail: acetylation at the nucleosome dyad commands transcription.
Post-translational modifications (PTMs) of histones have been implicated in cellular processes such as transcription, replication and DNA repair. These processes normally involve dynamic changes in chromatin structure and DNA accessibility. Most of the PTMs reported so far map on the histone tails and essentially affect chromatin structure indirectly by recruiting effector proteins. A recent study by Schneider and colleagues published in Cell (1) has uncovered the function of H3K122 acetylation found within the histone globular domain and specifically positioned on the DNA-bound surface of the nucleosome. Their findings demonstrate a direct effect of histone PTMs on chromatin dynamics, and propose that modifications located in different parts of the nucleosome employ distinct regulatory mechanisms.
Department of Biological Sciences; University of Cyprus; Nicosia, Cyprus.
Diego
D
Molina-Serrano
Antonis
A
Kirmizis
D000818:Animals; D005786:Gene Expression Regulation; D042421:Histone Code; D006657:Histones / Q000378:metabolism*; D006801:Humans; D015533:Transcriptional Activation
D006657:Histones
acetylation; chromatin; histone; lateral surface; nucleosome; post-translational modification; transcription