EMD-4397
Cryo-EM structure of bacterial RNA polymerase-sigma54 holoenzyme initial transcribing complex
EMD-4397
Single-particle3.7 Å
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Map released: 04/07/2018
Last modified: 15/05/2024
Sample Organism:
Escherichia coli K-12,
Klebsiella pneumoniae
Sample: Cryo-EM structure of bacterial RNA polymerase-sigma54 holoenzyme initial transcribing complex
Fitted models: 6gfw (Avg. Q-score: 0.372)
Deposition Authors: Glyde R, Ye FZ
Sample: Cryo-EM structure of bacterial RNA polymerase-sigma54 holoenzyme initial transcribing complex
Fitted models: 6gfw (Avg. Q-score: 0.372)
Deposition Authors: Glyde R, Ye FZ
Structures of Bacterial RNA Polymerase Complexes Reveal the Mechanism of DNA Loading and Transcription Initiation.
Glyde R,
Ye F
,
Jovanovic M
,
Kotta-Loizou I
,
Buck M,
Zhang X
(2018) Mol Cell , 70 , 1111 - 1120.e3
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(2018) Mol Cell , 70 , 1111 - 1120.e3
Abstract:
Gene transcription is carried out by multi-subunit RNA polymerases (RNAPs). Transcription initiation is a dynamic multi-step process that involves the opening of the double-stranded DNA to form a transcription bubble and delivery of the template strand deep into the RNAP for RNA synthesis. Applying cryoelectron microscopy to a unique transcription system using σ54 (σN), the major bacterial variant sigma factor, we capture a new intermediate state at 4.1 Å where promoter DNA is caught at the entrance of the RNAP cleft. Combining with new structures of the open promoter complex and an initial de novo transcribing complex at 3.4 and 3.7 Å, respectively, our studies reveal the dynamics of DNA loading and mechanism of transcription bubble stabilization that involves coordinated, large-scale conformational changes of the universally conserved features within RNAP and DNA. In addition, our studies reveal a novel mechanism of strand separation by σ54.
Gene transcription is carried out by multi-subunit RNA polymerases (RNAPs). Transcription initiation is a dynamic multi-step process that involves the opening of the double-stranded DNA to form a transcription bubble and delivery of the template strand deep into the RNAP for RNA synthesis. Applying cryoelectron microscopy to a unique transcription system using σ54 (σN), the major bacterial variant sigma factor, we capture a new intermediate state at 4.1 Å where promoter DNA is caught at the entrance of the RNAP cleft. Combining with new structures of the open promoter complex and an initial de novo transcribing complex at 3.4 and 3.7 Å, respectively, our studies reveal the dynamics of DNA loading and mechanism of transcription bubble stabilization that involves coordinated, large-scale conformational changes of the universally conserved features within RNAP and DNA. In addition, our studies reveal a novel mechanism of strand separation by σ54.