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Nature:RNA聚合酶Pol II/TFIIB复合物的晶体结构

来源:EurekAlert! 2009-11-20 09:34

专题:Nature报道

RNA聚合酶-II(Pol II)是在基因转录中起中心作用的酶,在真核细胞中制造所有的信使RNA。蛋白编码基因的转录是由Pol II和包括TFIIB在内的一般性转录因子所形成的一个复合物启动的。

Kostrewa等人确定了Pol II/TFIIB复合物的完整晶体结构。该结构及互补功能数据表明,转录的启动有一个由6个步骤构成的机制,包括当转录开始点被定位后所触发的向RNA伸长的过渡。(生物谷Bioon.com)

生物谷推荐原始出处:

Nature 462, 323-330 (19 November 2009) | doi:10.1038/nature08548

RNA polymerase II–TFIIB structure and mechanism of transcription initiationnear-final version

Dirk Kostrewa1,3, Mirijam E. Zeller2,3, Karim-Jean Armache1,3,4, Martin Seizl1, Kristin Leike1, Michael Thomm2 & Patrick Cramer1

1 Gene Center Munich and Center for Integrated Protein Science Munich (CIPSM), Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universit?t München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
2 Institut für Biochemie, Genetik und Mikrobiologie, Universit?t Regensburg, Universit?tsstrasse 31, 93053 Regensburg, Germany
3 These authors contributed equally to this work.
4 Present address: Department of Molecular Biology, Massachusetts General Hospital and Department of Genetics, Harvard Medical School, Boston, Massachusetts 02114, USA.
5 Correspondence to: Patrick Cramer1 Correspondence and requests for materials should be addressed to P.C.

To initiate gene transcription, RNA polymerase II (Pol II) requires the transcription factor IIB (B). Here we present the crystal structure of the complete Pol II–B complex at 4.3 ? resolution, and complementary functional data. The results indicate the mechanism of transcription initiation, including the transition to RNA elongation. Promoter DNA is positioned over the Pol II active centre cleft with the 'B-core' domain that binds the wall at the end of the cleft. DNA is then opened with the help of the 'B-linker' that binds the Pol II rudder and clamp coiled-coil at the edge of the cleft. The DNA template strand slips into the cleft and is scanned for the transcription start site with the help of the 'B-reader' that approaches the active site. Synthesis of the RNA chain and rewinding of upstream DNA displace the B-reader and B-linker, respectively, to trigger B release and elongation complex formation.

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