Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor
- Tsukasa Shimojima1,2,5,
- Masahiro Okada1,5,6,
- Takahiro Nakayama1,
- Hitoshi Ueda1,
- Katsuya Okawa4,
- Akihiro Iwamatsu4,
- Hiroshi Handa3, and
- Susumu Hirose1,7
- 1 Department of Developmental Genetics, National Institute of Genetics, and Department of Developmental Genetics, Graduate University for Advanced Studies, Mishima, Shizuoka-ken 411-8540, Japan, 2 Faculty of Bioscience and Biotechnology, and 3 Frontier Collaborative Research Center, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan, 4 Central Laboratories for Key Technology, Kirin Brewery, Kanazawa-ku, Yokohama 236-0004, Japan
Abstract
Chromatin structure plays a critical role in the regulation of transcription. Drosophila GAGA factor directs chromatin remodeling to its binding sites. We show here that Drosophila FACT (facilitates chromatin transcription), a heterodimer of dSPT16 and dSSRP1, is associated with GAGA factor through its dSSRP1 subunit, binds to a nucleosome, and facilitates GAGA factor-directed chromatin remodeling. Moreover, genetic interactions between Trithorax-like encoding GAGA factor and spt16 implicate the GAGA factor–FACT complex in expression of Hox genes Ultrabithorax, Sex combs reduced, and Abdominal-B. Chromatin immunoprecipitation experiments indicated the presence of the GAGA factor–FACT complex in the regulatory regions of Ultrabithorax and Abdominal-B. These data illustrate a crucial role of FACT in the modulation of chromatin structure for the regulation of gene expression.
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Footnotes
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Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1086803.
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↵5 These authors contributed equally to this work.
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↵6 Present address: Laboratory of Molecular Genetics, RIKEN Tsukuba Institute, 3-1-1 Koyadai, Tsukuba, Ibaragi-ken 305-0074, Japan.
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Corresponding author.
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↵7 E-MAIL shirose{at}lab.nig.ac.jp; FAX 81-55-981-6776.
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- Accepted May 5, 2003.
- Received February 19, 2003.
- Cold Spring Harbor Laboratory Press











