Summary information and primary citation
- PDB-id
-
6z9r;
DSSR-derived features in text and
JSON formats
- Class
- transcription
- Method
- cryo-EM (4.1 Å)
- Summary
- Transcription termination intermediate complex 3
- Reference
-
Said N, Hilal T, Sunday ND, Khatri A, Burger J, Mielke T,
Belogurov GA, Loll B, Sen R, Artsimovitch I, Wahl MC
(2021): "Steps
toward translocation-independent RNA polymerase
inactivation by terminator ATPase rho."
Science, 371. doi: 10.1126/science.abd1673.
- Abstract
- Factor-dependent transcription termination mechanisms
are poorly understood. We determined a series of
cryo-electron microscopy structures portraying the
hexameric adenosine triphosphatase (ATPase) ρ on a pathway
to terminating NusA/NusG-modified elongation complexes. An
open ρ ring contacts NusA, NusG, and multiple regions of
RNA polymerase, trapping and locally unwinding proximal
upstream DNA. NusA wedges into the ρ ring, initially
sequestering RNA. Upon deflection of distal upstream DNA
over the RNA polymerase zinc-binding domain, NusA rotates
underneath one capping ρ subunit, which subsequently
captures RNA. After detachment of NusG and clamp opening,
RNA polymerase loses its grip on the RNA:DNA hybrid and is
inactivated. Our structural and functional analyses suggest
that ρ, and other termination factors across life, may use
analogous strategies to allosterically trap transcription
complexes in a moribund state.
