期刊
MOLECULAR CELL
卷 64, 期 6, 页码 1135-1143出版社
CELL PRESS
DOI: 10.1016/j.molcel.2016.11.013
关键词
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资金
- ERC Advanced Grant [ERC-2013-AdG340964-POL1PIC]
- EMBL International PhD program
- EMBL Interdisciplinary Postdoc Program (EIPOD) under Marie Curie COFUND actions [PCOFUND-GA-2008-229597]
RNA polymerase I (Pol I) is a 14-subunit enzyme that solely synthesizes pre-ribosomal RNA. Recently, the crystal structure of apo Pol I gave unprecedented insight into its molecular architecture. Here, we present three cryo-EM structures of elongating Pol I, two at 4.0 angstrom and one at 4.6 angstrom resolution, and a Pol I open complex at 3.8 angstrom resolution. Two modules in Pol I mediate the narrowing of the DNA-binding cleft by closing the clamp domain. The DNA is bound by the clamp head and by the protrusion domain, allowing visualization of the upstream and downstream DNA duplexes in one of the elongation complexes. During formation of the Pol I elongation complex, the bridge helix progressively folds, while the A12.2 C-terminal domain is displaced from the active site. Our results reveal the conformational changes associated with elongation complex formation and provide additional insight into the Pol I transcription cycle.
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