 |
PDBsum entry 6duq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription/RNA
|
PDB id
|
|
|
|
6duq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 6 more)
409 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 6 more)
43 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Mechanism for the regulated control of bacterial transcription termination by a universal adaptor protein.
|
|
|
Authors
|
|
M.R.Lawson,
W.Ma,
M.J.Bellecourt,
I.Artsimovitch,
A.Martin,
R.Landick,
K.Schulten,
J.M.Berger.
|
|
|
Ref.
|
|
Mol Cell, 2018,
71,
911.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
NusG/Spt5 proteins are the only transcription factors utilized by all cellular
organisms. In enterobacteria, NusG antagonizes the transcription termination
activity of Rho, a hexameric helicase, during the synthesis of ribosomal and
actively translated mRNAs. Paradoxically, NusG helps Rho act on untranslated
transcripts, including non-canonical antisense RNAs and those arising from
translational stress; how NusG fulfills these disparate functions is unknown.
Here, we demonstrate that NusG activates Rho by assisting helicase isomerization
from an open-ring, RNA-loading state to a closed-ring, catalytically active
translocase. A crystal structure of closed-ring Rho in complex with NusG reveals
the physical basis for this activation and further explains how Rho is excluded
from translationally competent RNAs. This study demonstrates how a universally
conserved transcription factor acts to modulate the activity of a ring-shaped
ATPase motor and establishes how the innate sequence bias of a termination
factor can be modulated to silence pervasive, aberrant transcription.
|
|
|
|
|
|
|
