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J. Biol. Chem., Vol. 281, Issue 24, 16264-16271, June 16, 2006

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The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription^*

Erica Cavellán, Patrik Asp¹, Piergiorgio Percipalle, and Ann-Kristin Östlund Farrants²

From the Department of Cell Biology, The Wenner-Gren Institute, Stockholm University SE-106 91 Stockholm and Cell and Molecular Biology, Karolinska Institutet, SE-171 77 Stockholm, Sweden

The WSTF (Williams syndrome transcription factor) protein is involved in vitamin D-mediated transcription and replication as a component of two distinct ATP-dependent chromatin remodeling complexes, WINAC and WICH, respectively. We show here that the WICH complex (WSTF-SNF2h) interacts with several nuclear proteins as follows: Sf3b155/SAP155, RNA helicase II/Gu, Myb-binding protein 1a, CSB, the proto-oncogene Dek, and nuclear myosin 1 in a large 3-MDa assembly, B-WICH, during active transcription. B-WICH also contains RNAs, 45 S rRNA, 5 S rRNA, 7SL RNA, and traces of the U2 small nuclear RNA. The core proteins, WSTF, SNF2h, and nuclear myosin 1, are associated with the RNA polymerase III genes 5 S rRNA genes and 7SL, and post-transcriptional silencing of WSTF reduces the levels of these transcripts. Our results show that a WSTF-SNF2h assembly is involved in RNA polymerase III transcription, and we suggest that WSTF-SNF2h-NM1 forms a platform in transcription while providing chromatin remodeling.

Received for publication, January 10, 2006 , and in revised form, April 7, 2006.

^* The work was supported by The Swedish Natural Science Research Council, The Carl Trygger Foundation, The Magnus Bergvall Foundation, The Nilsson-Ehle Foundation, the Foundation for Lars Hiertas Minne, and The Marcus Borgström Foundation. 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.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1–S3 and additional Refs. 1–5.

¹ Present address: Dept. of Pathology, New York University School of Medicine, MSB 504, New York, NY 10016.

² To whom correspondence should be addressed: Dept. of Cell Biology, Wenner-Gren Institute, Arrhenius Laboratories E5, Stockholm University, SE-106 91 Stockholm, Sweden. Tel.: 468-164-097; Fax: 468-159-837; E-mail: anki.ostlund{at}cellbio.su.se.

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