English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure of RNA polymerase I transcribing ribosomal DNA genes.

Neyer, S., Kunz, M., Geiss, C., Hantsche, M., Hodirnau, V. V., Seybert, A., et al. (2016). Structure of RNA polymerase I transcribing ribosomal DNA genes. Nature, 540(7634), 607-610. doi:10.1038/nature20561.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-0150-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-078E-4
Genre: Journal Article

Files

show Files
hide Files
:
2364556.pdf (Publisher version), 13MB
 
File Permalink:
-
Name:
2364556.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2364556_Suppl.html (Supplementary material), 88KB
Name:
2364556_Suppl.html
Description:
-
Visibility:
Public
MIME-Type / Checksum:
text/html / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Neyer, S.1, Author              
Kunz, M., Author
Geiss, C., Author
Hantsche, M.1, Author              
Hodirnau, V. V., Author
Seybert, A., Author
Engel, C.1, Author              
Scheffer, M. P., Author
Cramer, P.1, Author              
Frangakis, A. S., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

Content

show
hide
Free keywords: Cryoelectron microscopy; Cryoelectron tomography
 Abstract: RNA polymerase I (Pol I) is a highly processive enzyme that transcribes ribosomal DNA (rDNA) and regulates growth of eukaryotic cells. Crystal structures of free Pol I from the yeast Saccharomyces cerevisiae have revealed dimers of the enzyme stabilized by a 'connector' element and an expanded cleft containing the active centre in an inactive conformation. The central bridge helix was unfolded and a Pol-I-specific 'expander' element occupied the DNA-template-binding site. The structure of Pol I in its active transcribing conformation has yet to be determined, whereas structures of Pol II and Pol III have been solved with bound DNA template and RNA transcript. Here we report structures of active transcribing Pol I from yeast solved by two different cryo-electron microscopy approaches. A single-particle structure at 3.8 Å resolution reveals a contracted active centre cleft with bound DNA and RNA, and a narrowed pore beneath the active site that no longer holds the RNA-cleavage-stimulating domain of subunit A12.2. A structure at 29 Å resolution that was determined from cryo-electron tomograms of Pol I enzymes transcribing cellular rDNA confirms contraction of the cleft and reveals that incoming and exiting rDNA enclose an angle of around 150°. The structures suggest a model for the regulation of transcription elongation in which contracted and expanded polymerase conformations are associated with active and inactive states, respectively.

Details

show
hide
Language(s): eng - English
 Dates: 2016-11-142016-12-22
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nature20561
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 540 (7634) Sequence Number: - Start / End Page: 607 - 610 Identifier: -