Identification and functional characterization of BTas transactivator as a DNA-binding protein.
Identification and functional characterization of BTas transactivator as a DNA-binding protein.
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DOI:
10.1016/j.virol.2010.05.037
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发表时间:
2010-09
期刊:
影响因子:
3.7
通讯作者:
Juan Tan;Peng Hao;R. Jia;Wei Yang;R. Liu;Jinzhong Wang;Zhen Xi;Y. Geng;W. Qiao
中科院分区:
文献类型:
--
作者:
Juan Tan;Peng Hao;R. Jia;Wei Yang;R. Liu;Jinzhong Wang;Zhen Xi;Y. Geng;W. Qiao
The genome of bovine foamy virus (BFV) encodes a transcriptional transactivator, namely BTas, that remarkably enhances gene expression by binding to the viral long-terminal repeat promoter (LTR) and internal promoter (IP). In this report, we characterized the functional domains of BFV BTas. BTas contains two major functional domains: the N-terminal DNA-binding domain (residues 1–133) and the C-terminal activation domain (residues 198–249). The complete BTas responsive regions were mapped to the positions −380/−140 of LTR and 9205/9276 of IP. Four BTas responsive elements were identified at the positions −368/−346, −327/−307, −306/−285 and −186/−165 of the BFV LTR, and one element was identified at the position 9243/9264 of the BFV IP. Unlike other foamy viruses, the five BTas responsive elements in BFV shared obvious sequence homology. These data suggest that among the complex retroviruses, BFV appears to have a unique transactivation mechanism.