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EMBO Rep. 2001 Oct;2(10):920-5. Epub 2001 Sep 24.

Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1.

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Department of Basic Sciences, The University of Crete, School of Medicine, 71 110 Heraklion, Crete, Greece.


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.

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