Format

Send to

Choose Destination
Nucleus. 2013 Sep-Oct;4(5):343-8. doi: 10.4161/nucl.26051. Epub 2013 Aug 9.

Beyond the histone tail: acetylation at the nucleosome dyad commands transcription.

Author information

1
Department of Biological Sciences; University of Cyprus; Nicosia, Cyprus.

Abstract

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.

KEYWORDS:

acetylation; chromatin; histone; lateral surface; nucleosome; post-translational modification; transcription

PMID:
23941995
PMCID:
PMC3899122
DOI:
10.4161/nucl.26051
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center