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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The 2.1-A deg crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box
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The 2.1-A deg crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box

机译:古细菌预起始复合物的2.1-A deg晶体结构:TATA盒结合蛋白/转录因子(II)B核心/ TATA盒

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摘要

Archaea possess a basal transcriptional ap- paratus that resembles that of eukaryotes. Here we report the 2.1-A deg crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts.
机译:古细菌具有类似于真核生物的基础转录装置。在这里,我们报告了TATA盒结合蛋白(TBP),转录因子IIB同源物和DNA靶标形成的古细菌转录因子复合物的2.1-A deg晶体结构,它们全部来自嗜热嗜热球菌。这两个基础转录因子的整体折叠与它们的真核对应物的折叠基本相同。

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