ArticleNucleic acids research2007
Escherichia coli RNA polymerase-associated SWI/SNF protein RapA: evidence for RNA-directed binding and remodeling activity.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- 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
- On the stability of stalled RNA polymerase and its removal by RapA.Nucleic acids research · 2022Article
- 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
- Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.Nucleic acids research · 2021Article
- 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 interplay of post-translational modification and gene therapy.Drug design, development and therapy · 2016Review
- Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.Nucleic acids research · 2014Article
- Defense islands in bacterial and archaeal genomes and prediction of novel defense systems.Journal of bacteriology · 2011Article
- Structure and function of RapA: a bacterial Swi2/Snf2 protein required for RNA polymerase recycling in transcription.Biochimica et biophysica acta · 2011Review
- Article
- RapA, the SWI/SNF subunit of Escherichia coli RNA polymerase, promotes the release of nascent RNA from transcription complexes.Biochemistry · 2009Article
- An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA.Nucleic acids research · 2009Article
- Structure of RapA, a Swi2/Snf2 protein that recycles RNA polymerase during transcription.Structure (London, England : 1993) · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Helicase-like SWI/SNF proteins are present in organisms belonging to distant kingdoms from bacteria to humans, indicating that they perform a very basic and ubiquitous form of nucleic acid management; current studies associate the activity of SWI/SNF proteins with remodeling of DNA and DNA-protein complexes. The bacterial SWI/SNF homolog RapA-an integral part of the Escherichia coli RNA polymerase complex-has been implicated in remodeling post-termination DNA-RNA polymerase-RNA ternary complexes (PTC), however its explicit nucleic acid substrates and mechanism remain elusive. Our work presents evidence indicating that RNA is a key substrate of RapA. Specifically, the formation of stable RapA-RNA intermediates in transcription and other, independent lines of evidence presented herein indicate that RapA binds and remodels RNA during transcription. Our results are consistent with RapA promoting RNA release from DNA-RNA polymerase-RNA ternary complexes; this process may be accompanied by the destabilization of non-canonical DNA-RNA complexes (putative DNA-RNA triplexes). Taken together, our data indicate a novel RNA remodeling activity for RapA, a representative of the SWI/SNF protein superfamily.
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