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Structure of RNA polymerase I transcribing ribosomal DNA genes

November 2016. RNA polymerase is a central enzyme for the cellular function that transcribes DNA to RNA. In their new publication in the research journal Nature, researchers from the BMLS at the Goethe University Frankfurt and the Max Planck Institute for Biophysical Chemistry in Göttingen have visualized the RNA Polymerase I (Pol I) while it is actively transcribing ribosome genes in a cellular environment and have solved its structure with and without nucleic acids at 3.8 Å resolution by cryo-electron microscopy. The structures explain the regulation of transcription elongation in which contracted and expanded polymerase conformations are associated with active and inactive states, respectively. More ...

Figure: On the left a three-dimensional surface rendering of a cryo-electron tomogram showing several successive Pol I enzymes (yellow) transcribing on the DNA (blue), while the emanating RNA (red) with RNA-modifying complexes (cyan) can be seen ending in terminal knobs resembling preribosomal complexes. The DNA and Pol I are zoomed almost a hundred times to reveal the atomic model of the structure of the Pol I shown in a top view on the right. All subunits of the Pol I could be resolved at atomic resolution and are coloured according the standard Pol I subunit colouring: A190, grey; A135, wheat; A49, light blue; A43, slate; AC40, red; A34.5, pink; Rpb5, magenta; Rpb6, silver-blue; AC19, yellow; Rpb8, green; A14, hot pink; A12.2, orange;  Rpb10, blue; Rpb12, lemon. Template DNA, non-template DNA and RNA are depicted in medium blue, sky blue and red, respectively.

Achilleas Frangakis
Buchmann Institute for Molecular Life Sciences & Institute for Biophysics
Goethe University Frankfurt, Germany

Simon Neyer*, Michael Kunz*, Christian Geiss, Merle Hantsche, Victor-Valentin Hodirnau, Anja Seybert, Christoph Engel, Margot P. Scheffer, Patrick Cramer§, Achilleas S. Frangakis§ (2016). Structure of RNA polymerase I transcribing ribosomal DNA genes. Nature, advance online publication 14 November 2016, DOI 10.1038/nature20561, Link
* - equal contribution, § - shared corresponding authors