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  RNA polymerase I-Rrn3 complex at 4.8 Å resolution.

Engel, C., Plitzko, J., & Cramer, P. (2016). RNA polymerase I-Rrn3 complex at 4.8 Å resolution. Nature Communications, 7: 12129. doi:10.1038/ncomms12129.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-07DB-8 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-07F1-3
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 Creators:
Engel, C.1, Author           
Plitzko, J., Author
Cramer, P.1, Author           
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1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: Transcription of ribosomal DNA by RNA polymerase I (Pol I) requires the initiation factor Rrn3. Here we report the cryo-EM structure of the Pol I-Rrn3 complex at 4.8 Å resolution. The structure reveals how Rrn3 binding converts an inactive Pol I dimer into an initiation-competent monomeric complex and provides insights into the mechanisms of Pol I-specific initiation and regulation.

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Language(s): eng - English
 Dates: 2016-07-15
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms12129
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Title: Nature Communications
Source Genre: Journal
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Pages: 5 Volume / Issue: 7 Sequence Number: 12129 Start / End Page: - Identifier: -