ArticleNature structural & molecular biology2013
Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- Structure and function of IWS1 in transcription elongation.Nucleic acids research · 2026Article
- Distinct roles of RECQL5 in RAD51-mediated fork reversal and transcription elongation.Nucleic acids research · 2025Article
- Structural insights into transcriptional regulation by the helicase RECQL5.Nature structural & molecular biology · 2025Article
- Structural basis of RECQL5-induced RNA polymerase II transcription braking and subsequent reactivation.Nature structural & molecular biology · 2025Article
- Article
- Expression of human RECQL5 in Saccharomyces cerevisiae causes transcription defects and transcription-associated genome instability.Molecular genetics and genomics : MGG · 2024Article
- Review
- Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling.ACS chemical biology · 2021Article
- The comprehensive interactomes of human adenosine RNA methyltransferases and demethylases reveal distinct functional and regulatory features.Nucleic acids research · 2021Article
- A Dual-Site Inhibitor of CBP/p300 KIX is a Selective and Effective Modulator of Myb.Journal of the American Chemical Society · 2021Article
- Checkpoint functions of RecQ helicases at perturbed DNA replication fork.Current genetics · 2021Review
- RecQ helicases in DNA repair and cancer targets.Essays in biochemistry · 2020Review
- History of DNA Helicases.Genes · 2020Review
- Review
- Increased levels of RECQ5 shift DNA repair from canonical to alternative pathways.Nucleic acids research · 2018Article
- Covalent Chemical Cochaperones of the p300/CBP GACKIX Domain.Chembiochem : a European journal of chemical biology · 2018Article
- RecQ and Fe-S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions.Biochemical Society transactions · 2018Review
- KIXBASE: A comprehensive web resource for identification and exploration of KIX domains.Scientific reports · 2017Article
- Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.Nucleic acids research · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
RECQL5 is a member of the highly conserved RecQ family of DNA helicases involved in DNA repair. RECQL5 interacts with RNA polymerase II (Pol II) and inhibits transcription of protein-encoding genes by an unknown mechanism. We show that RECQL5 contacts the Rpb1 jaw domain of Pol II at a site that overlaps with the binding site for the transcription elongation factor TFIIS. Our cryo-EM structure of elongating Pol II arrested in complex with RECQL5 shows that the RECQL5 helicase domain is positioned to sterically block elongation. The crystal structure of the RECQL5 KIX domain reveals similarities with TFIIS, and binding of RECQL5 to Pol II interferes with the ability of TFIIS to promote transcriptional read-through in vitro. Together, our findings reveal a dual mode of transcriptional repression by RECQL5 that includes structural mimicry of the Pol II-TFIIS interaction.
Indexed as
Identifiers
What OpenQuestion holds
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.