Transcription factor IIB acetylates itself to regulate transcription
Transcription factor IIB acetylates itself to regulate transcription
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DOI：
10.1038/nature01899
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发表时间：
2003-08-21
期刊：
影响因子：
64.8
通讯作者：
Usheva, A
中科院分区：
文献类型：
--
作者：
Choi, CH;Hiromura, M;Usheva, A
乙酰化是众所周知的调节性翻译后修饰（1），但乙酰化在调节基础转录因子中的生物学功能尚未报道。在这里，我们表明，启动真核生物聚合酶II转录所需的一般转录因子TFIIB（2）是乙酰化的。TFIIB也是一种自身乙酰转移酶，尽管它与任何已知的乙酰转移酶没有序列同源性。在没有其他酶的情况下，它结合乙酰辅酶A（乙酰辅酶A），并催化乙酰基转移到特定的赖氨酸残基（K238）上。重组和细胞TFIIB都可以自动乙酰化，显著稳定TFIIB和转录因子TFIIF之间的相互作用，并在体外和细胞中激活转录。不能被自动乙酰化的K238A突变体不显示这种转录激活。我们的研究结果表明，有一个控制乙酰化TFIIB的调节途径，他们连接乙酰辅酶A与基础基因转录。
Acetylation is a well-known regulatory post-translational modification(1), but a biological function for acetylation in regulating basal transcription factors has not been reported. Here we show that the general transcription factor TFIIB, which is required for the initiation of eukaryotic polymerase II transcription(2), is acetylated. TFIIB is also an autoacetyltransferase, although it shares no sequence homology with any known acetyltransferases. In the absence of other enzymes, it binds acetyl-coenzyme A (acetyl-CoA), and catalyses the transfer of the acetyl group onto a specific lysine residue (K238). Both recombinant and cellular TFIIB can autoacetylate, markedly stabilizing the interaction between TFIIB and transcription factor TFIIF and activating transcription in vitro and in cells. A K238A mutant, which cannot be autoacetylated, does not show this activation of transcription. Our findings suggest that there is a regulatory pathway controlling acetylation of TFIIB, and they link acetyl-CoA with basal gene transcription.