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Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69
journal contribution
posted on 2023-06-08, 08:42 authored by Caroline M S Ekblad, Gayatri B Chavali, Balaka P Basu, Stefan M V Freund, Dmitry Veprintsev, Luke Hughes-Davies, Tony Kouzarides, Aidan DohertyAidan Doherty, Laura S ItzhakiEMSY is a large nuclear protein that binds to the transactivation domain of BRCA2. EMSY contains an 100-residue segment at the amino terminus called the ENT (EMSY N-terminal) domain. Plant proteins containing ENT domains also contain members of the royal family of chromatin-remodelling domains. It has been proposed that EMSY may have a role in chromatin-related processes. This is supported by the observation that a number of chromatin-regulator proteins, including HP1 and BS69, bind directly to EMSY by means of a conserved motif adjacent to the ENT domain. Here, we report the crystal structure of residues 1¿108 of EMSY at 2.0 Å resolution. The structure contains both the ENT domain and the HP1/BS69-binding motif. This binding motif forms an extended peptide-like conformation that adopts distinct orientations in each subunit of the dimer. Biophysical and nuclear magnetic resonance analyses show that the main complex formed by EMSY and the chromoshadow domain of HP1 (HP1-CSD) consists of one EMSY dimer sandwiched between two HP1-CSD dimers. The HP1-binding motif is necessary and sufficient for EMSY to bind to the chromoshadow domain of HP1.
History
Publication status
- Published
Journal
EMBO ReportsISSN
1469-221XPublisher
Nature Publishing GroupExternal DOI
Issue
7Volume
6Page range
675-680Pages
6.0Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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