SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus
Viiri, K., Korkeamäki, H., Kukkonen, M., Nieminen, L., Lindfors, K., Peterson, P., Mäki, M., Kainulainen, H., & Lohi, O. (2006). SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus. Nucleic Acids Research, 34(11), 3288-3298. https://doi.org/10.1093/nar/gkl401
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Nucleic Acids ResearchAuthors
Date
2006Copyright
© 2006 The Author(s).
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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Oxford University PressISSN Search the Publication Forum
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This work was supported by the Academy of Finland Research Council for Health (funding decision number 201361), the Foundation for Paediatric Research in Finland, the Medical Research Fund of Pirkanmaa Hospital District, Maud Kuistila Memorial Foundation, and Nona and Kullervo Väre Foundation. Funding to pay the Open Access publication charges for this article was provided by Medical Research Fund of Pirkanmaa Hospital District. ...License
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