EMD-3819

Single-particle
3.8 Å
EMD-3819 Deposition: 18/07/2017
Map released: 13/09/2017
Last modified: 06/11/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-3819

Structure of an RNA polymerase II-DSIF transcription elongation complex, DSIF-EC5

EMD-3819

Single-particle
3.8 Å
EMD-3819 Deposition: 18/07/2017
Map released: 13/09/2017
Last modified: 06/11/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Bos taurus, Homo sapiens, synthetic construct
Sample: RNA polymerase II-DSIF elongation complex

Deposition Authors: Bernecky C, Plitzko JM, Cramer P
Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.
Bernecky C , Plitzko JM , Cramer P
(2017) Nat. Struct. Mol. Biol. , 24 , 809 - 815
PUBMED: 28892040
DOI: doi:10.1038/nsmb.3465
ISSN: 1545-9985
Abstract:
During transcription, RNA polymerase II (Pol II) associates with the conserved elongation factor DSIF. DSIF renders the elongation complex stable and functions during Pol II pausing and RNA processing. We combined cryo-EM and X-ray crystallography to determine the structure of the mammalian Pol II-DSIF elongation complex at a nominal resolution of 3.4 Å. Human DSIF has a modular structure with two domains forming a DNA clamp, two domains forming an RNA clamp, and one domain buttressing the RNA clamp. The clamps maintain the transcription bubble, position upstream DNA, and retain the RNA transcript in the exit tunnel. The mobile C-terminal region of DSIF is located near exiting RNA, where it can recruit factors for RNA processing. The structure provides insight into the roles of DSIF during mRNA synthesis.