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Originally published In Press as doi:10.1074/jbc.M509917200 on October 3, 2005
J. Biol. Chem., Vol. 280, Issue 51, 42252-42262, December 23, 2005
Binding of Barrier to Autointegration Factor (BAF) to Histone H3 and Selected Linker Histones Including H1.1*
Rocío Montes de Oca,
Kenneth K. Lee1, and
Katherine L. Wilson2
From the
Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Barrier to autointegration factor (BAF) is an essential conserved double-stranded DNA-binding protein in metazoans. BAF binds directly to LEM domain nuclear proteins (e.g. LAP2, Emerin, and MAN1), lamin A, homeodomain transcription factors, and human immunodeficiency virus type 1-encoded proteins. BAF influences higher order chromatin structure and is required to assemble nuclei. BAF also facilitates retroviral preintegration complex insertion into target DNA in vitro, through unknown mechanisms. We report that BAF binds directly and selectively to linker histone H1.1 (among three subtypes tested) and core histone H3 with affinities of 700 nM and 100-200 nM, respectively, in vitro and in vivo. Mutations at the bottom and top surfaces of the BAF dimer disrupted or enhanced, respectively, this binding and affected H1 and H3 similarly. Biochemical studies showed that C-terminal residues 108-215 of histone H1.1 and the N-terminal tail plus helix N in the core of histone H3.1 were each necessary and sufficient to bind BAF. Based on its interactions with histones and DNA, we propose BAF might bind nucleosomes in vivo.
Received for publication, September 8, 2005
, and in revised form, September 21, 2005.
* This work was funded by National Institutes of Health Grant RO1 GM48646 (to K. L. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 Present address: Stowers Institute for Medical Research, Kansas City, MO 64110.
2 To whom correspondence should be addressed: Dept. of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205. Tel.: 410-955-1801; Fax: 410-955-4129; E-mail: klwilson{at}jhmi.edu.

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Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
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