Lysine acetylation sites in bovine foamy virus transactivator BTas are important for its DNA binding activity
Lysine acetylation sites in bovine foamy virus transactivator BTas are important for its DNA binding activity
复制标题
牛泡沫病毒反式激活蛋白 BTa 中的赖氨酸乙酰化位点对其 DNA 结合活性很重要
DOI：
10.1016/j.virol.2011.07.003
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发表时间：
2011-09-15
期刊：
影响因子：
3.7
通讯作者：
Qiao, Wentao
中科院分区：
文献类型：
--
作者：
Chang, Rui;Tan, Juan;Qiao, Wentao
Cellular acetylation signaling is important for viral gene regulation, particularly during the transactivation of retroviruses. The regulatory protein of bovine foamy virus (BFV), BTas, is a transactivator that augments viral gene transcription from both the long terminal repeat (LTR) promoter and the internal promoter (IP). In this study, we report that the histone acetyltransferase (HAT), p300, specifically acetylates BTas both in vivo and in vitro. Further studies demonstrated that BTas acetylation markedly enhances its transactivation activity. Mutagenesis analysis identified three lysines at positions 66, 109 and 110 in Bias that are acetylated by p300. The K110R mutant lost its binding to BFV promoter as well as its ability to activate BFV promoter. The acetylation of K66 and K109 may contribute to increased Bias binding ability. These results suggest that the p300-acetylated lysines of BTas are important for transactivation of BFV promoters and therefore have an important role in BFV replication. (C) 2011 Elsevier Inc. All rights reserved.
