Functional architecture of RNA polymerase I.

Kuhn, C. D.; Geiger, S. R.; Baumli, S.; Gartmann, M.; Gerber, J.; Jennebach, S.; Mielke, T.; Tschochner, H.; Beckmann, R.; Cramer, P.

doi:10.1016/j.cell.2007.10.051

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Functional architecture of RNA polymerase I.

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Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S0092867407014146/pdfft?md5=1b302321d24ac55aa393a58113d5f209&pid=1-s2.0-S0092867407014146-main.pdf
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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:10.1016/j.cell.2007.10.051.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-7F26-7

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.