ArticleNucleic acids research2022
Mechanism of transcription modulation by the transcription-repair coupling factor.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Predicting theLife (Basel, Switzerland) · 2025Article
- The role of lncRNA SNHG15 in UV-induced DNA damage repair.PloS one · 2025Article
- Dynamics of transcription-coupled repair of cyclobutane pyrimidine dimers and (6-4) photoproducts inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Global genome and transcription-coupled nucleotide excision repair pathway in prokaryotes.Journal of biosciences · 2023Review
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Mfd - at the crossroads of bacterial DNA repair, transcriptional regulation and molecular evolvability.Transcription · 2021Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Elongation by RNA polymerase is dynamically modulated by accessory factors. The transcription-repair coupling factor (TRCF) recognizes paused/stalled RNAPs and either rescues transcription or initiates transcription termination. Precisely how TRCFs choose to execute either outcome remains unclear. With Escherichia coli as a model, we used single-molecule assays to study dynamic modulation of elongation by Mfd, the bacterial TRCF. We found that nucleotide-bound Mfd converts the elongation complex (EC) into a catalytically poised state, presenting the EC with an opportunity to restart transcription. After long-lived residence in this catalytically poised state, ATP hydrolysis by Mfd remodels the EC through an irreversible process leading to loss of the RNA transcript. Further, biophysical studies revealed that the motor domain of Mfd binds and partially melts DNA containing a template strand overhang. The results explain pathway choice determining the fate of the EC and provide a molecular mechanism for transcription modulation by TRCF.
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Registered trials
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