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

FEBS Letters

Punga, Tanel¹  Akusjärvi, Göran¹ 

[1] Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, 751 23 Uppsala, Sweden

关键词: Adenovirus;    E1B-55K;    Histone deacetylase 1;    mSin3A;   

DOI  :  10.1016/S0014-5793(00)01739-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown