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Journal Article

Functional architecture of RNA polymerase I

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Mielke,  Thorsten
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Kuhn, C.-D., Geiger, S. R., Baumli, S., Gartmann, M., Gerber, J., Jennebach, S., et al. (2007). Functional architecture of RNA polymerase I. Cell, 131(7), 1260-1272. doi:doi:10.1016/j.cell.2007.10.051.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-80F0-F
Abstract
Synthesis of ribosomal RNA (rRNA) by RNA polymerase (Pol) I is the first step in ribosome biogenesis and a regulatory switch in eukaryotic cell growth. Here we report the 12 Å cryo-electron microscopic structure for the complete 14-subunit yeast Pol I, a homology model for the core enzyme, and the crystal structure of the subcomplex A14/43. In the resulting hybrid structure of Pol I, A14/43, the clamp, and the dock domain contribute to a unique surface interacting with promoter-specific initiation factors. The Pol I-specific subunits A49 and A34.5 form a heterodimer near the enzyme funnel that acts as a built-in elongation factor and is related to the Pol II-associated factor TFIIF. In contrast to Pol II, Pol I has a strong intrinsic 3′-RNA cleavage activity, which requires the C-terminal domain of subunit A12.2 and, apparently, enables ribosomal RNA proofreading and 3′-end trimming.