Summary information and primary citation
- PDB-id
-
6xlm;
DSSR-derived features in text and
JSON formats
- Class
- transcription, transferase-DNA
- Method
- cryo-EM (3.2 Å)
- Summary
- cryo-EM structure of e.coli rnap-DNA elongation complex
1 (rde1) in ecmrr-dependent transcription
- Reference
-
Yang Y, Liu C, Zhou W, Shi W, Chen M, Zhang B, Schatz DG,
Hu Y, Liu B (2021): "Structural
visualization of transcription activated by a
multidrug-sensing MerR family regulator." Nat
Commun, 12, 2702. doi: 10.1038/s41467-021-22990-8.
- Abstract
- Bacterial RNA polymerase (RNAP) holoenzyme initiates
transcription by recognizing the conserved -35 and -10
promoter elements that are optimally separated by a 17-bp
spacer. The MerR family of transcriptional regulators
activate suboptimal 19-20 bp spacer promoters in response
to myriad cellular signals, ranging from heavy metals to
drug-like compounds. The regulation of transcription by
MerR family regulators is not fully understood. Here we
report one crystal structure of a multidrug-sensing MerR
family regulator EcmrR and nine cryo-electron microscopy
structures that capture the EcmrR-dependent transcription
process from promoter opening to initial transcription to
RNA elongation. These structures reveal that EcmrR is a
dual ligand-binding factor that reshapes the suboptimal
19-bp spacer DNA to enable optimal promoter recognition,
sustains promoter remodeling to stabilize initial
transcribing complexes, and finally dissociates from the
promoter to reverse DNA remodeling and facilitate the
transition to elongation. Our findings yield a
comprehensive model for transcription regulation by MerR
family factors and provide insights into the transition
from transcription initiation to elongation.
