ArticleBiochemistry2009
RapA, the SWI/SNF subunit of Escherichia coli RNA polymerase, promotes the release of nascent RNA from transcription complexes.
Article in Biochemistry, 2009. 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, 20 citations in OpenAlex.
- RapA opens the RNA polymerase clamp to disrupt post-termination complexes and prevent cytotoxic R-loop formation.Nature structural & molecular biology · 2025Article
- Recycling of bacterial RNA polymerase by the Swi2/Snf2 ATPase RapA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Recycling of Bacterial RNA Polymerase by the Swi2/Snf2 ATPase RapA.bioRxiv : the preprint server for biology · 2023Article
- The bacterial protein Hfq: Stable modifications and growth phase-dependent changes in SPAM profiles.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021Article
- Article
- Growth phase-specific changes in the composition of E. coli transcription complexes.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- The Mitochondrial DNA-Associated Protein SWIB5 Influences mtDNA Architecture and Homologous Recombination.The Plant cell · 2017Article
- Structural basis for transcription reactivation by RapA.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.Nucleic acids research · 2014Article
- Mechanisms for ATP-dependent chromatin remodelling: the means to the end.The FEBS journal · 2011Review
- Structure and function of RapA: a bacterial Swi2/Snf2 protein required for RNA polymerase recycling in transcription.Biochimica et biophysica acta · 2011Review
- Functions of the Snf2/Swi2 family Rad54 motor protein in homologous recombination.Biochimica et biophysica acta · 2011Review
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RapA, a prokaryotic member of the SWI/SNF protein superfamily, is an integral part of the RNA polymerase transcription complex. RapA's function and catalytic mechanism have been linked to nucleic acid remodeling. In this work, we show that mutations in the interface between RapA's SWI/SNF and double-stranded nucleic acid-binding domains significantly alter ATP hydrolysis in purified RapA. The effects of individual mutations on ATP hydrolysis loosely correlated with RapA's nucleic acid remodeling activity, indicating that the interaction between these domains may be important for the RapA-mediated remodeling of nonproductive transcription complexes. In this study, we introduced a model system for in vitro transcription of a full-length Escherichia coli gene (slyD). To study the function of RapA, we fractionated and identified in vitro transcription reaction intermediates in the presence or absence of RapA. These experiments demonstrated that RapA contributes to the formation of free RNA species during in vitro transcription. This work further refines our models for RapA function in vivo and establishes a new role in RNA management for a representative of the SWI/SNF protein superfamily.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.