Published online 4 July 2006
© 2006 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-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.
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SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus
1 Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital Tampere, Finland 2 Molecular Pathology, University of Tartu Tartu, Estonia 3 Institute of Medical Technology and Tampere University Hospital Tampere, Finland 4 Department of Biology of Physical Activity, University of Jyväskylä Finland
To whom correspondence should be addressed. Tel: +358 3 355 184 05; Fax: +358 3 355 184 02; Email: olli.lohi{at}uta.fi
Received January 19, 2006. Revised March 24, 2006. Accepted May 11, 2006.
Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120–140 in the C-terminal part of the protein. We provide evidence that SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. Finally, we characterize a functional nucleolar localization signal in SAP30L and show that SAP30L and SAP30 are able to target Sin3A to the nucleolus.
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