Molecular cloning and characterization of dTAFII30 alpha and dTAFII30 beta: two small subunits of Drosophila TFIID.
Molecular cloning and characterization of dTAFII30 alpha and dTAFII30 beta: two small subunits of Drosophila TFIID.
复制标题
dTAFII30 α 和 dTAFII30 β 的分子克隆和表征：果蝇 TFIID 的两个小亚基。
作者：
K. Yokomori;J. Chen;A. Admon;S. Zhou;R. Tjian
多亚基转录因子TFIID是RNA聚合酶II起始装置的重要组成部分。最近的研究表明，TFIID亚基，或TAFs与TATA结合蛋白（TBP），在调节转录激活序列特异性DNA结合因子发挥关键作用。到目前为止，与果蝇TFIID相关的六个最大的TAF已被克隆和部分表征。在这里，我们报告的分子克隆，表达和亚基相互作用的特异性，两个小分子量TAFs。dTAFII 30 α和dTAFII 30 β均通过与其他TAF（包括dTAFII 250、dTAFII 150和dTAFII 110）的相互作用与TFIID相关。此外，dTAFII 30 α也与dTBP接触。发现dTAFII 110的羧基末端的一半与dTAFII 30 α的短的67个氨基酸区域接触，预测其形成两个潜在的α-螺旋，其中一个是两亲性的。有趣的是，dTAFII 30 α似乎也通过其羧基末端区域多聚化。尽管迄今为止尚未发现dTAFII 30 α和dTAFII 30 β与特异性激活剂相互作用，但有趣的是，两者都结合其他TAF，如dTAFII 110和dTAFII 150，它们是激活结构域的靶点。我们的研究表明，TFIID的两个小亚基在复合物的组装中发挥作用，并可能有助于多种TAF-TAF相互作用的稳定性。
The multisubunit transcription factor TFIID is an essential component of the RNA polymerase II initiation apparatus. Recent studies suggest that TFIID subunits, or TAFs associated with the TATA-binding protein (TBP), play a critical role in modulating transcriptional activation by sequence-specific DNA-binding factors. Thus far, six of the largest TAFs associated with Drosophila TFIID have been cloned and partially characterized. Here, we report the molecular cloning, expression, and subunit interaction specificities of two small molecular mass TAFs. Both dTAFII30 alpha and dTAFII30 beta are associated with TFIID via interactions with other TAFs, including dTAFII250, dTAFII150, and dTAFII110. In addition, dTAFII30 alpha also contacts dTBP. The carboxy-terminal half of dTAFII110 was found to contact a short 67-amino-acid region of dTAFII30 alpha, which is predicted to form two potential alpha-helices, one of which is amphipathic. Interestingly, dTAFII30 alpha also appears to multimerize through its carboxy-terminal region. Although neither dTAFII30 alpha nor dTAFII30 beta have been found to interact with specific activators thus far, it is intriguing that both bind other TAFs such as dTAFII110 and dTAFII150, which are the targets of activation domains. Our studies suggest that both of the small subunits of TFIID play a role in the assembly of the complex and may contribute to the stability of multiple TAF-TAF interactions.
影响因子：
10.5
作者：
DYNLACHT, BD;ATTARDI, LD;TJIAN, R
通讯作者：
TJIAN, R
影响因子：
10.5
作者：
KOKUBO, T;GONG, DW;NAKATANI, Y
通讯作者：
NAKATANI, Y