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Molecular and Cellular Biology, January 2009, p. 342-356, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01213-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

DNA-Binding and -Bending Activities of SAP30L and SAP30 Are Mediated by a Zinc-Dependent Module and Monophosphoinositides ^,

Keijo M. Viiri,¹ Janne Jänis,² Trevor Siggers,³ Taisto Y. K. Heinonen,¹ Jarkko Valjakka,⁵ Martha L. Bulyk,^3,4,6 Markku Mäki,¹ and Olli Lohi^1*

Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, 33520 Tampere, Finland,¹ Department of Chemistry, University of Joensuu, FI-80101 Joensuu, Finland,² Division of Genetics, Department of Medicine, Brigham & Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115,³ Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115,⁴ Institute of Medical Technology and Tampere University Hospital, University of Tampere, FI-33014 Tampere, Finland,⁵ Harvard/MIT Division of Health Sciences and Technology, Harvard Medical School, Boston, Massachusetts 02115⁶

Received 1 August 2008/ Returned for modification 17 September 2008/ Accepted 6 November 2008

Deacetylation of histones is carried out by a corepressor complex in which Sin3A is an essential scaffold protein. Two proteins in this complex, the Sin3A-associated proteins SAP30L and SAP30, have previously been suggested to function as linker molecules between various corepressors. In this report, we demonstrate new functions for human SAP30L and SAP30 by showing that they can associate directly with core histones as well as naked DNA. A zinc-coordinating structure is necessary for DNA binding, one consequence of which is bending of the DNA. We provide evidence that a sequence motif previously shown to be a nuclear localization signal is also a phosphatidylinositol (PI)-binding element and that binding of specific nuclear monophosphoinositides regulates DNA binding and chromatin association of SAP30L. PI binding also decreases the repression activity of SAP30L and affects its translocation from the nucleus to the cytoplasm. Our results suggest that SAP30L and SAP30 play active roles in recruitment of deacetylating enzymes to nucleosomes, and mediate key protein-protein and protein-DNA interactions involved in chromatin remodeling and transcription.

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* Corresponding author. Mailing address: Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, 33520 Tampere, Finland. Phone: 358 3 35518405. Fax: 358 3 3551 8402. E-mail: olli.lohi{at}uta.fi

Published ahead of print on 17 November 2008.

Supplemental material for this article may be found at http://mcb.asm.org/.

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Molecular and Cellular Biology, January 2009, p. 342-356, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01213-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• He, Y., Imhoff, R., Sahu, A., Radhakrishnan, I. (2009). Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition. Nucleic Acids Res 37: 2142-2152 [Abstract] [Full Text]