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Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Bernecky C,Plitzko JM,Cramer P

doi

10.1038/nsmb.3465

subject

Has Abstract

pub_date

2017-10-01 00:00:00

pages

809-815

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb.3465

journal_volume

24

pub_type

杂志文章

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