.png){kind=icon}
.png){kind=icon}
Return
Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein
.png){kind=icon}
OA
AI
DOI：10.1016/j.molcel.2018.07.014.png)
.png){kind=icon}
.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
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.
Keywords:
RNA-POLYMERASE-II
FACTOR-RHO
STRUCTURAL BASIS
NUSG
COMPLEX
HELICASE
TRANSLOCATION
ARCHITECTURE
SEQUENCE
DOMAIN
AI Summary
Key information extracted from the uploaded paper, including a brief overview, abstract, background, key highlights, visual analysis, and future outlook.
Journal
IF:
16.6
Papers:
1.0W
Citations:
8.5W
View more organizations