Structural insights into NusG regulating transcription elongation.

Abstract:

:NusG is an essential transcription factor that plays multiple key regulatory roles in transcription elongation, termination and coupling translation and transcription. The core role of NusG is to enhance transcription elongation and RNA polymerase processivity. Here, we present the structure of Escherichia coli RNA polymerase complexed with NusG. The structure shows that the NusG N-terminal domain (NGN) binds at the central cleft of RNA polymerase surrounded by the β' clamp helices, the β protrusion, and the β lobe domains to close the promoter DNA binding channel and constrain the β' clamp domain, but with an orientation that is different from the one observed in the archaeal β' clamp-Spt4/5 complex. The structure also allows us to construct a reliable model of the complete NusG-associated transcription elongation complex, suggesting that the NGN domain binds at the upstream fork junction of the transcription elongation complex, similar to σ2 in the transcription initiation complex, to stabilize the junction, and therefore enhances transcription processivity.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Liu B,Steitz TA

doi

10.1093/nar/gkw1159

subject

Has Abstract

pub_date

2017-01-25 00:00:00

pages

968-974

issue

2

eissn

0305-1048

issn

1362-4962

pii

gkw1159

journal_volume

45

pub_type

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