Molecular determinants underlying functional innovations of TBP and their impact on transcription initiation

Molecular determinants underlying functional innovations of TBP and their impact on transcription initiation
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TBP功能创新的分子决定因素及其对转录起始的影响

DOI:
10.1038/s41467-020-16182-z
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发表时间:
2020
影响因子:
16.6
通讯作者:
S. Balaji
S. Balaji
中科院分区:
综合性期刊1区
文献类型:
--
作者:
C. Ravarani;T. Flock;T. Flock;S. Chavali;S. Chavali;M. Anandapadamanaban;M. Babu;S. Balaji

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TATA盒结合蛋白(TBP)是古细菌和真核生物中每一个转录事件所必需的。它结合DNA,并含有两个具有内部结构对称性的重复序列,显示序列不对称性。在进化的不同时期,TBP已经获得了多个相互作用伙伴,并且不同的生物已经进化出具有额外蛋白质区域的TBP旁系同源物。总之,这些观察结果提出了什么样的分子决定因素(即关键残基)导致TBP获得新的相互作用的能力,从而导致在真核生物中越来越复杂的转录系统的问题。我们提出了一个全面的研究TBP的进化历史和它的相互作用伙伴在所有领域的生活,包括病毒。我们的分析揭示了TBP功能创新的分子决定因素,并提出了一个统一的多阶段进化模型。这些发现强调了保守结构支架上的协调化学变化如何允许在基本生物过程中出现复杂性。TATA盒结合蛋白(TBP)是古细菌和真核生物转录起始所必需的。在这里,作者描述了TBP的功能是如何通过与各种蛋白质伴侣的上下文依赖性相互作用进化出新的功能特征的。
TATA-box binding protein (TBP) is required for every single transcription event in archaea and eukaryotes. It binds DNA and harbors two repeats with an internal structural symmetry that show sequence asymmetry. At various times in evolution, TBP has acquired multiple interaction partners and different organisms have evolved TBP paralogs with additional protein regions. Together, these observations raise questions of what molecular determinants (i.e. key residues) led to the ability of TBP to acquire new interactions, resulting in an increasingly complex transcriptional system in eukaryotes. We present a comprehensive study of the evolutionary history of TBP and its interaction partners across all domains of life, including viruses. Our analysis reveals the molecular determinants and suggests a unified and multi-stage evolutionary model for the functional innovations of TBP. These findings highlight how concerted chemical changes on a conserved structural scaffold allow for the emergence of complexity in a fundamental biological process. The TATA-box binding protein (TBP) is required for transcription initiation in archaea and eukaryotes. Here the authors delineate how TBP’s function has evolved new functional features through context-dependent interactions with various protein partners.
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