ArticleNature structural & molecular biology2024
Early intermediates in bacterial RNA polymerase promoter melting visualized by time-resolved cryo-electron microscopy.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Structural basis for loading of transcription repair-coupling factor Mfd onto stalled elongation complexes.Nucleic acids research · 2026Article
- Structural basis for multi-subunit DNA-dependent RNA polymerase catalytic activity.Molecular cell · 2026Article
- Dynamic landscape of transcription initiation by yeast RNA polymerase I.Nucleic acids research · 2026Article
- The bacterial RNA polymerase-associated CarD protein couples promoter activity to DNA supercoiling.Nature communications · 2026Article
- Integrated experimental and AI innovations for RNA structure determination.Nature biotechnology · 2026Review
- Structural Insights into De Novo Promoter Escape by Mycobacterium tuberculosis RNA Polymerase.Nature communications · 2025Article
- Article
- Structural basis for loading of Transcription Repair-Coupling factor Mfd onto stalled elongation complexes.bioRxiv : the preprint server for biology · 2025Article
- A general RNA-templated RNA extension activity ofRNA (New York, N.Y.) · 2025Article
- Single-stranded DNA drives σ subunit loading onto mycobacterial RNA polymerase to unlock initiation-competent conformations.Nucleic acids research · 2025Article
- Targeting Bacterial RNA Polymerase: Harnessing Simulations and Machine Learning to Design Inhibitors for Drug-Resistant Pathogens.Biochemistry · 2025Review
- An extreme mutational hotspot in nlpD depends on transcriptional induction of rpoS.PLoS genetics · 2025Article
- RNA Polymerase II Activity Control of Gene Expression and Involvement in Disease.Journal of molecular biology · 2025Review
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Funding
Abstract
During formation of the transcription-competent open complex (RPo) by bacterial RNA polymerases (RNAPs), transient intermediates pile up before overcoming a rate-limiting step. Structural descriptions of these interconversions in real time are unavailable. To address this gap, here we use time-resolved cryogenic electron microscopy (cryo-EM) to capture four intermediates populated 120 ms or 500 ms after mixing Escherichia coli σ
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