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利用单分子荧光共振能量转移和纳米孔测序技术解析古菌RNA聚合酶开放复合物的完整结构

Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS.

作者信息

Nagy Julia, Grohmann Dina, Cheung Alan C M, Schulz Sarah, Smollett Katherine, Werner Finn, Michaelis Jens

机构信息

Biophysics Institute, Ulm University, Albert-Einstein-Allee 11, Ulm 89069, Germany.

Institut für Physikalische und Theoretische Chemie-NanoBioSciences, Technische Universität Braunschweig, Hans-Sommer-Straße 10, 38106 Braunschweig, Germany.

出版信息

Nat Commun. 2015 Jan 30;6:6161. doi: 10.1038/ncomms7161.

DOI:10.1038/ncomms7161
PMID:25635909
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6294288/
Abstract

The molecular architecture of RNAP II-like transcription initiation complexes remains opaque due to its conformational flexibility and size. Here we report the three-dimensional architecture of the complete open complex (OC) composed of the promoter DNA, TATA box-binding protein (TBP), transcription factor B (TFB), transcription factor E (TFE) and the 12-subunit RNA polymerase (RNAP) from Methanocaldococcus jannaschii. By combining single-molecule Förster resonance energy transfer and the Bayesian parameter estimation-based Nano-Positioning System analysis, we model the entire archaeal OC, which elucidates the path of the non-template DNA (ntDNA) strand and interaction sites of the transcription factors with the RNAP. Compared with models of the eukaryotic OC, the TATA DNA region with TBP and TFB is positioned closer to the surface of the RNAP, likely providing the mechanism by which DNA melting can occur in a minimal factor configuration, without the dedicated translocase/helicase encoding factor TFIIH.

摘要

由于其构象灵活性和大小，RNA聚合酶II样转录起始复合物的分子结构仍然不明确。在此，我们报告了由启动子DNA、TATA盒结合蛋白（TBP）、转录因子B（TFB）、转录因子E（TFE）和来自嗜热栖热菌的12亚基RNA聚合酶（RNAP）组成的完整开放复合物（OC）的三维结构。通过结合单分子Förster共振能量转移和基于贝叶斯参数估计的纳米定位系统分析，我们构建了整个古菌OC的模型，该模型阐明了非模板DNA（ntDNA）链的路径以及转录因子与RNAP的相互作用位点。与真核OC模型相比，带有TBP和TFB的TATA DNA区域更靠近RNAP表面，这可能提供了一种机制，使得DNA解链能够以最小的因子配置发生，而无需专门编码转位酶/解旋酶的因子TFIIH。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/a0c871bfac11/emss-80785-f007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/684b170e40f1/emss-80785-f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/d7ac5acaf598/emss-80785-f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/becdf51bc026/emss-80785-f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/17646209fd1a/emss-80785-f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/af78f0f32dee/emss-80785-f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/8bed073d763d/emss-80785-f006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/a0c871bfac11/emss-80785-f007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/684b170e40f1/emss-80785-f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/d7ac5acaf598/emss-80785-f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/becdf51bc026/emss-80785-f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/17646209fd1a/emss-80785-f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/af78f0f32dee/emss-80785-f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/8bed073d763d/emss-80785-f006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08ed/6294288/a0c871bfac11/emss-80785-f007.jpg

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