Analysis of the varicella-zoster virus IE62 N-terminal acidic transactivating domain and its interaction with the human mediator complex.
Analysis of the varicella-zoster virus IE62 N-terminal acidic transactivating domain and its interaction with the human mediator complex.
复制标题
水痘带状疱疹病毒 IE62 N 末端酸性反式激活结构域及其与人类介质复合物相互作用的分析。
DOI：
10.1128/jvi.00054-09
复制
发表时间：
2009
影响因子：
5.4
通讯作者：
Ruyechan,WilliamT
中科院分区：
文献类型：
--
作者：
Yamamoto,Shinobu;Eletsky,Alexander;Szyperski,Thomas;Hay,John;Ruyechan,WilliamT
水痘-带状疱疹病毒主要反式激活因子IE62含有一个N-末端酸性转录激活结构域（acidic transcriptional activation domain，ACTA）。我们的实验表明，最小的IE62 β包括氨基酸（aa）19至67。我们发现，最小的神经元与人类中介复合体相互作用。位点特异性突变揭示了整个最小酶的残基，这些残基对激活和介体相互作用都很重要。直接与MED 25亚基的402至590位氨基酸相互作用，位点特异性突变消除了这种相互作用。二维核磁共振光谱显示，该化合物本质上是非结构化的。我们的研究表明，反式激活可能涉及的结合MED 25后，采用一个确定的结构。
The varicella-zoster virus major transactivator, IE62, contains a potent N-terminal acidic transcriptional activation domain (TAD). Our experiments revealed that the minimal IE62 TAD encompasses amino acids (aa) 19 to 67. We showed that the minimal TAD interacts with the human Mediator complex. Site-specific mutations revealed residues throughout the minimal TAD that are important for both activation and Mediator interaction. The TAD interacts directly with aa 402 to 590 of the MED25 subunit, and site-specific TAD mutations abolished this interaction. Two-dimensional nuclear magnetic resonance spectroscopy revealed that the TAD is intrinsically unstructured. Our studies suggest that transactivation may involve the TAD adopting a defined structure upon binding MED25.