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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-9F1F-D Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-9F26-C
Genre: Journal Article

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 Creators:
Engel, C., Author
Plitzko, Jürgen1, Author           
Cramer, P., Author
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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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
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms12129
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: 5 Volume / Issue: 7 Sequence Number: 12129 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723