Crystal structure of Methanococcus jannaschii TATA box-binding protein
Crystal structure of Methanococcus jannaschii TATA box-binding protein
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DOI：
10.1111/j.1365-2443.2008.01233.x
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发表时间：
2008-11-01
期刊：
影响因子：
2.1
通讯作者：
Horikoshi, Masami
中科院分区：
文献类型：
--
作者：
Adachi, Naruhiko;Senda, Miki;Horikoshi, Masami
由于古细菌转录系统由真核型转录装置和细菌型转录调控因子组成，因此分析转录装置和调控转录因子之间的分子界面对于揭示转录系统的进化变化至关重要。 TATA 盒结合蛋白 (TBP) 是转录装置的核心成分，分为三类：真核 TBP、古细菌 I 型和古细菌 II 型 TBP。因此，这三组TBP的功能比较分析对于研究转录系统的进化具有重要意义。在这里，我们展示了来自詹氏甲烷球菌的古菌-II TBP 的第一个晶体结构。 TBP 的高度保守和组特异性保守表面分别与 DNA 和 TFIIB/TFB 结合。 TBP 和 TFIIB/TFB 的系统发育树表明它们以耦合方式进化。古菌-II TBP 中的 TBP 多样化表面带负电，这与真核和古菌-I TBP 的情况完全不同，真核和古菌-I TBP 分别带正电和双相。这种差异导致了 TBP 在进化过程中调节功能的多样化。
As the archaeal transcription system consists of a eukaryotic-type transcription apparatus and bacterial-type regulatory transcription factors, analyses of the molecular interface between the transcription apparatus and regulatory transcription factors are critical to reveal the evolutionary change of the transcription system. TATA box-binding protein (TBP), the central components of the transcription apparatus are classified into three groups: eukaryotic, archaeal-I and archaeal-II TBPs. Thus, comparative functional analysis of these three groups of TBP is important for the study of the evolution of the transcription system. Here, we present the first crystal structure of an archaeal-II TBP from Methanococcus jannaschii. The highly conserved and group-specific conserved surfaces of TBP bind to DNA and TFIIB/TFB, respectively. The phylogenetic trees of TBP and TFIIB/TFB revealed that they evolved in a coupled manner. The diversified surface of TBP is negatively charged in the archaeal-II TBP, which is completely different from the case of eukaryotic and archaeal-I TBPs, which are positively charged and biphasic, respectively. This difference is responsible for the diversification of the regulatory functions of TBP during evolution.