Viiri K M, Korkeamäki H, Kukkonen M K, Nieminen L K, Lindfors K, Peterson P, Mäki M, Kainulainen H, Lohi O
Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, Tampere, Finland.
Nucleic Acids Res. 2006 Jul 4;34(11):3288-98. doi: 10.1093/nar/gkl401. Print 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.
组蛋白乙酰化在基因表达调控中起关键作用。染色质结构以及基因对转录因子的可及性由使组蛋白乙酰化和去乙酰化的酶来调控。Sin3A共抑制复合物招募组蛋白去乙酰化酶，并且在许多情况下抑制转录。在此，我们报道Sin3相关蛋白30（SAP30）的紧密同源物SAP30L与Sin3A共抑制复合物的几个组分相互作用。我们表明它与小鼠Sin3A的PAH3/HID（配对双性螺旋3/组蛋白去乙酰化酶相互作用结构域）区域结合，结合位点在该蛋白C末端部分的第120至140位残基处。我们提供的证据表明，SAP30L可能通过招募Sin3A和组蛋白去乙酰化酶来诱导转录抑制。最后，我们鉴定了SAP30L中一个功能性核仁定位信号，并表明SAP30L和SAP30能够将Sin3A靶向至核仁。
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