The adenovirus-2 E1B-55K protein interacts with a mSin3A/histone deacetylase 1 complex

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• 作者：Punga ; Tanel ; Akusj&auml ; rvi ; Gö ; ran
• 关键词：Adenovirus ; E1B-55K ; Histone deacetylase 1 ; mSin3A
• 刊名：FEBS Letters
• 出版年：2000
• 出版时间：July 7, 2000
• 年：2000
• 卷：476
• 期：3
• 页码：248-252
• 全文大小：219 K

文摘

The adenovirus E1B-55K protein is a multifunctional phosphoprotein that regulates nuclear to cytoplasmic export of host cell and viral mRNAs during lytic viral growth. E1B-55K also blocks apoptosis by binding and functionally inactivating the human tumor suppressor protein p53. Here, we show that E1B-55K interacts with histone deacetylase 1 (HDAC1) and the transcriptional corepressor protein mSin3A, both in the adenovirus-transformed 293 cell line and during a lytic adenovirus infection. Furthermore, we show that the central amino acids 156–261 in E1B-55K are necessary for efficient HDAC1 interaction. Importantly, the E1B-55K/mSin3A/HDAC1 complex is also enzymatically active, catalyzing deacetylation of a histone substrate peptide. Collectively, our results suggest that E1B-55K interaction with mSin3A/HDAC1 containing complexes may be significant for one or several of the multiple activities ascribed to this protein.