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Nucleic Acids Research Advance Access originally published online on August 20, 2009
Nucleic Acids Research 2009 37(18):5993-6007; doi:10.1093/nar/gkp660
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Nucleic Acids Research, 2009, Vol. 37, No. 18 5993-6007
© The Author 2009. Published by Oxford University Press.
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.

Gene Regulation, Chromatin and Epigenetics

Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A

Jongkyu Choi, Kyu Heo and Woojin An*

Department of Biochemistry and Molecular Biology, University of Southern California, Norris Comprehensive Cancer Center, Los Angeles, CA 90033, USA

*To whom correspondence should be addressed. Tel: +1 323 442 4398; Fax: +1 323 442 4433; Email: woojinan{at}usc.edu

Received May 28, 2009. Revised July 21, 2009. Accepted July 24, 2009.

H2A.Z is an evolutionarily conserved H2A variant that plays a key role in the regulation of chromatin transcription. To understand the molecular mechanism of H2A.Z exchange, we purified two distinct H2A.Z-interacting complexes termed the small and big complexes from a human cell line. The big complex contains most components of the SRCAP chromatin remodeling and TIP60 HAT complexes, whereas the small complex possesses only a subset of SRCAP and TIP60 subunits. Our exchange analysis revealed that both small and big complexes enhance the incorporation of H2A.Z-H2B dimer into the nucleosome. In addition, TIP60-mediated acetylation of nucleosomal H2A specifically facilitates the action of the small complex in the H2A.Z exchange reaction. Among factors present in the small complex, we determined that TIP48 and TIP49 play a major role in catalyzing H2A acetylation-induced H2A.Z exchange via their ATPase activities. Overall, our work uncovers the previously-unrecognized role of TIP48 and TIP49 in H2A.Z exchange and a novel epigenetic mechanism controlling this process.


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