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Structural basis for transcription elongation by bacterial RNA polymerase.细菌RNA聚合酶转录延伸的结构基础。
Nature. 2007 Jul 12;448(7150):157-62. doi: 10.1038/nature05932. Epub 2007 Jun 20.
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Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis.转录的结构基础：触发环在底物特异性和催化作用中的作用。
Cell. 2006 Dec 1;127(5):941-54. doi: 10.1016/j.cell.2006.11.023.
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Elongation complexes of Thermus thermophilus RNA polymerase that possess distinct translocation conformations.嗜热栖热菌RNA聚合酶具有不同易位构象的延伸复合物。
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pH-dependent conformational switch activates the inhibitor of transcription elongation.pH 依赖性构象开关激活转录延伸抑制剂。
EMBO J. 2006 May 17;25(10):2131-41. doi: 10.1038/sj.emboj.7601094. Epub 2006 Apr 20.
6
Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS.完整的RNA聚合酶II延伸复合物结构及其与NTP和TFIIS的相互作用。
Mol Cell. 2004 Dec 22;16(6):955-65. doi: 10.1016/j.molcel.2004.11.040.
7
Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center.转录的结构基础：RNA聚合酶II活性中心通过旋转进行核苷酸选择。
Cell. 2004 Nov 12;119(4):481-9. doi: 10.1016/j.cell.2004.10.016.
8
Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme from Thermus thermophilus.嗜热栖热菌RNA聚合酶全酶的纯化、结晶及初步晶体学分析
Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1497-500. doi: 10.1107/S0907444902011770. Epub 2002 Aug 23.
9
Transcript cleavage by Thermus thermophilus RNA polymerase. Effects of GreA and anti-GreA factors.嗜热栖热菌RNA聚合酶的转录物切割。GreA和抗GreA因子的作用。
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10
Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution.转录的结构基础：分辨率为3.3埃的RNA聚合酶II延伸复合物
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嗜热栖热菌转录延伸复合物与Gfh1结合的结晶及初步X射线晶体学分析

Crystallization and preliminary X-ray crystallographic analysis of Thermus thermophilus transcription elongation complex bound to Gfh1.

作者信息

Tagami Shunsuke, Sekine Shun-ichi, Kumarevel Thirumananseri, Yamamoto Masaki, Yokoyama Shigeyuki

机构信息

Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):64-8. doi: 10.1107/S1744309109049215. Epub 2009 Dec 25.

DOI:10.1107/S1744309109049215
PMID:20057074
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2805540/
Abstract

RNA polymerase (RNAP) elongates RNA by iterative nucleotide-addition cycles (NAC). A specific structural state (or states) of RNAP may be the target of transcription elongation factors. Gfh1, a Thermus thermophilus Gre-family protein, inhibits NAC. To elucidate which RNAP structural state Gfh1 associates with, the T. thermophilus RNAP elongation complex (EC) was cocrystallized with Gfh1. Of the 70 DNA/RNA scaffolds tested, two (for EC1 and EC2) were successfully crystallized. In the presence of Gfh1, EC1 and EC2 yielded crystals belonging to space group P2(1) with similar unit-cell parameters (crystals 1 and 2, respectively). X-ray diffraction data sets were obtained at 3.6 and 3.8 A resolution, respectively.

摘要

RNA聚合酶（RNAP）通过迭代核苷酸添加循环（NAC）来延长RNA。RNAP的一种特定结构状态可能是转录延伸因子的作用靶点。嗜热栖热菌的Gre家族蛋白Gfh1可抑制NAC。为阐明Gfh1与RNAP的哪种结构状态相关联，将嗜热栖热菌RNAP延伸复合物（EC）与Gfh1进行了共结晶。在测试的70种DNA/RNA支架中，有两种（用于EC1和EC2）成功结晶。在Gfh1存在的情况下，EC1和EC2产生了属于空间群P2(1)且具有相似晶胞参数的晶体（分别为晶体1和晶体2）。分别在3.6 Å和3.8 Å分辨率下获得了X射线衍射数据集。