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Nucleic Acids Research Advance Access published online on September 18, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm650
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Acetylation increases access of remodelling complexes to their nucleosome targets to enhance initiation of V(D)J recombination

Karl P. Nightingale1, Matthias Baumann2, Anton Eberharter3, Adamantios Mamais2, Peter B. Becker3 and Joan Boyes2,4,*

1Institute of Biomedical Research, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK, 2Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK, 3Adolf Butenandt Institute for Molecular Biology, Schillerstrasse 44, D-80336 Munich, Germany and 4Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.

*To whom correspondence should be addressed. Tel: 44 113 343 3147; Fax: 44 113 343 3167; Email: J.M.Boyes{at}leeds.ac.uk

Received April 10, 2007. Revised July 17, 2007. Accepted August 7, 2007.

Targeted chromatin remodelling is essential for many nuclear processes, including the regulation of V(D)J recombination. ATP-dependent nucleosome remodelling complexes are important players in this process whose activity must be tightly regulated. We show here that histone acetylation regulates nucleosome remodelling complex activity to boost RAG cutting during the initiation of V(D)J recombination. RAG cutting requires nucleosome mobilization from recombination signal sequences. Histone acetylation does not stimulate nucleosome mobilization per se by CHRAC, ACF or their catalytic subunit, ISWI. Instead, we find the more open structure of acetylated chromatin regulates the ability of nucleosome remodelling complexes to access their nucleosome templates. We also find that bromodomain/acetylated histone tail interactions can contribute to this targeting at limited concentrations of remodelling complex. We therefore propose that the changes in higher order chromatin structure associated with histone acetylation contribute to the correct targeting of nucleosome remodelling complexes and this is a novel way in which histone acetylation can modulate remodelling complex activity.

Present address: Matthias Baumann, GPC Biotech AG, D-82152 Martinsried, Germany.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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