Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1
Open Access
- 1 October 2001
- journal article
- research article
- Published by Springer Nature in EMBO Reports
- Vol. 2 (10), 920-925
- https://doi.org/10.1093/embo-reports/kve199
Abstract
We have recently shown that heterochromatin protein 1 (HP1) interacts with the nuclear envelope in an acetylation‐dependent manner. Using purified components and in vitro assays, we now demonstrate that HP1 forms a quaternary complex with the inner nuclear membrane protein LBR and a sub‐set of core histones. This complex involves histone H3/H4 oligomers, which mediate binding of LBR to HP1 and cross‐link these two proteins that do not interact directly with each other. Consistent with previous observations, HP1 and LBR binding to core histones is strongly inhibited when H3/H4 are modified by recombinant CREB‐binding protein, revealing a new mechanism for anchoring domains of under‐acetylated chromatin to the inner nuclear membrane.Keywords
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