English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Structure of transcribing mammalian RNA polymerase II.

Bernecky, C., Herzog, F., Baumeister, W., Plitzko, J. M., & Cramer, P. (2016). Structure of transcribing mammalian RNA polymerase II. Nature, 529(7587), 551-554. doi:10.1038/nature16482.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7D42-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3AFA-B
Genre: Journal Article

Files

show Files
hide Files
:
2247628.pdf (Publisher version), 12MB
 
File Permalink:
-
Name:
2247628.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), MBPC; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2247628_Suppl.pdf (Supplementary material), 47KB
Name:
2247628_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Bernecky, C.1, Author              
Herzog, F., Author
Baumeister, W., Author
Plitzko, J. M., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

Content

show
hide
Free keywords: -
 Abstract: RNA polymerase (Pol) II produces messenger RNA during transcription of protein-coding genes in all eukaryotic cells. The Pol II structure is known at high resolution from X-ray crystallography for two yeast species(1-3). Structural studies of mammalian Pol II, however, remain limited to low-resolution electron microscopy analysis of human Pol II and its complexes with various proteins(4-10). Here we report the 3.4 angstrom resolution cryo-electron microscopy structure of mammalian Pol II in the form of a transcribing complex comprising DNA template and RNA transcript. We use bovine Pol II, which is identical to the human enzyme except for seven amino-acid residues. The obtained atomic model closely resembles its yeast counterpart, but also reveals unknown features. Binding of nucleic acids to the polymerase involves 'induced fit' of the mobile Pol II clamp and active centre region. DNA downstream of the transcription bubble contacts a conserved 'TPSA motif' in the jaw domain of the Pol II subunit RPB5, an interaction that is apparently already established during transcription initiation(7). Upstream DNA emanates from the active centre cleft at an angle of approximately 105 degrees with respect to downstream DNA. This position of upstream DNA allows for binding of the general transcription elongation factor DSIF (SPT4-SPT5) that we localize over the active centre cleft in a conserved position on the clamp domain of Pol II. Our results define the structure of mammalian Pol II in its functional state, indicate that previous crystallographic analysis of yeast Pol II is relevant for understanding gene transcription in all eukaryotes, and provide a starting point for a mechanistic analysis of human transcription.

Details

show
hide
Language(s): eng - English
 Dates: 2016-01-202016-01-28
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nature16482
 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: 529 (7587) Sequence Number: - Start / End Page: 551 - 554 Identifier: -