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Nucleic Acids Research 2006 34(2):397-406; doi:10.1093/nar/gkj437
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Published online 13 January 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

p66{alpha} and p66ß of the Mi-2/NuRD complex mediate MBD2 and histone interaction

Marc Brackertz, Zihua Gong, Jörg Leers and Rainer Renkawitz*

Institute for Genetics, Justus-Liebig-University Giessen and Heinrich-Buff-Ring 58-62 D-35392 Giessen, Germany

*To whom correspondence should be addressed. Tel: +49 641 99 35460; Fax: +49 641 99 35469; Email: Rainer.Renkawitz{at}gen.bio.uni-giessen.de

Received November 16, 2005. Revised December 22, 2005. Accepted December 22, 2005.

The Mi-2/NuRD complex is a multi-subunit protein complex with enzymatic activities involving chromatin remodeling and histone deacetylation. Targeting of Mi-2/NuRD to methylated CpG sequences mediates gene repression. The function of p66{alpha} and of p66ß within the multiple subunits has not been addressed. Here, we analyzed the in vivo function and binding of both p66-paralogs. Both factors function in synergy, since knocking-down p66{alpha} affects the repressive function of p66ß and vice versa. Both proteins interact with MBD2 functionally and biochemically. Mutation of a single amino acid of p66{alpha} abolishes in vivo binding to MBD2 and interferes with MBD2-mediated repression. This loss of binding results in a diffuse nuclear localization in contrast to wild-type p66{alpha} that shows a speckled nuclear distribution. Furthermore, wild-type subnuclear distribution of p66{alpha} and p66ß depends on the presence of MBD2. Both proteins interact with the tails of all octamer histones in vitro, and acetylation of histone tails interferes with p66 binding. The conserved region 2 of p66{alpha} is required for histone tail interaction as well as for wild-type subnuclear distribution. These results suggest a two-interaction forward feedback binding mode, with a stable chromatin association only after deacetylation of the histones has occurred.


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