Punga T, Akusjärvi G
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, 751 23, Uppsala, Sweden.
FEBS Lett. 2000 Jul 7;476(3):248-52. doi: 10.1016/s0014-5793(00)01739-7.
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.
腺病毒E1B - 55K蛋白是一种多功能磷蛋白，在病毒裂解生长过程中调节宿主细胞和病毒mRNA从细胞核到细胞质的输出。E1B - 55K还通过结合并功能性失活人肿瘤抑制蛋白p53来阻断细胞凋亡。在此，我们表明E1B - 55K在腺病毒转化的293细胞系以及腺病毒裂解感染期间，均与组蛋白去乙酰化酶1（HDAC1）和转录共抑制蛋白mSin3A相互作用。此外，我们表明E1B - 55K中的中央氨基酸156 - 261对于有效的HDAC1相互作用是必需的。重要的是，E1B - 55K/mSin3A/HDAC1复合物也具有酶活性，可催化组蛋白底物肽的去乙酰化。总体而言，我们的结果表明，E1B - 55K与含mSin3A/HDAC1的复合物之间的相互作用可能对于归因于该蛋白的多种活性中的一种或几种具有重要意义。
