Evolutionary history of the TBP-domain superfamily.

Evolutionary history of the TBP-domain superfamily.
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DOI:
10.1093/nar/gkt045
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发表时间:
2013-03-01
影响因子:
14.9
通讯作者:
Poole AM
Poole AM
中科院分区:
生物学2区
文献类型:
--
作者:
Brindefalk B;Dessailly BH;Yeats C;Orengo C;Werner F;Poole AM

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TATA结合蛋白(TBP)是真核生物和拟南芥中一个重要的转录起始因子。细菌缺乏TBP,而是使用σ因子进行转录起始。TBP具有包含两个重复的TBP结构域的对称结构。使用序列,结构和系统发育分析,我们研究的分布和进化历史的TBP域,螺旋抓折叠家族的成员。我们的分析揭示了一个更广泛的分布比TBP,TBP域存在于所有三个领域的生活。与TBP相反,TBP结构域的所有其他表征实例都以单拷贝存在,主要在多结构域蛋白中。普遍存在的DNA糖基化酶中TBP结构域的存在表明,这种折叠可以追溯到所有三个生命结构域的祖先。TBP结构域也存在于RNase HIII中,系统发育分析表明RNase HIII通过TBP结构域融合从细菌RNase HII进化而来。最后,我们的比较基因组筛选证实和扩展了早期的报告中的蛋白质组成的一个单一的TBP结构域之间的一些peptidea。这些单组分TBP结构域蛋白表明,该结构域本身具有功能,并且TBP结构域可能首先作为一个独立的蛋白质进化,随后在不同的环境中被招募。
The TATA binding protein (TBP) is an essential transcription initiation factor in Archaea and Eucarya. Bacteria lack TBP, and instead use sigma factors for transcription initiation. TBP has a symmetric structure comprising two repeated TBP domains. Using sequence, structural and phylogenetic analyses, we examine the distribution and evolutionary history of the TBP domain, a member of the helix-grip fold family. Our analyses reveal a broader distribution than for TBP, with TBP-domains being present across all three domains of life. In contrast to TBP, all other characterized examples of the TBP domain are present as single copies, primarily within multidomain proteins. The presence of the TBP domain in the ubiquitous DNA glycosylases suggests that this fold traces back to the ancestor of all three domains of life. The TBP domain is also found in RNase HIII, and phylogenetic analyses show that RNase HIII has evolved from bacterial RNase HII via TBP-domain fusion. Finally, our comparative genomic screens confirm and extend earlier reports of proteins consisting of a single TBP domain among some Archaea. These monopartite TBP-domain proteins suggest that this domain is functional in its own right, and that the TBP domain could have first evolved as an independent protein, which was later recruited in different contexts.
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