ArticleNucleic acids research2021
Single-molecule visualization of human RECQ5 interactions with single-stranded DNA recombination intermediates.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 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
19 citing papers in PubMed, 26 citations in OpenAlex.
- FBH1 and RAD54L directly interact and cooperate to drive replication fork reversal.bioRxiv : the preprint server for biology · 2026Article
- Multifaceted roles of PDS5B in RAD51-dependent homology-directed DNA repair and replication fork protection.Nature communications · 2026Article
- Article
- High-throughput mapping of 6,888bioRxiv : the preprint server for biology · 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
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Biochemical Mechanisms of Genetic Recombination and DNA Repair.Annual review of biochemistry · 2025Review
- Characterization and organization of telomeric-linked helicase (tlh) gene families in Fusarium oxysporum.Current genetics · 2024Article
- Mechanisms and regulation of replication fork reversal.DNA repair · 2024Review
- DSS1 restrains BRCA2's engagement with dsDNA for homologous recombination, replication fork protection, and R-loop homeostasis.Nature communications · 2024Article
- RAD51 separation of function mutation disables replication fork maintenance but preserves DSB repair.iScience · 2024Article
- Review
- The role of bivalent ions in the regulation of D-loop extension mediated by DMC1 during meiotic recombination.iScience · 2022Article
- RAD51AP1 regulates ALT-HDR through chromatin-directed homeostasis of TERRA.Molecular cell · 2022Article
- Srs2 and Pif1 as Model Systems for Understanding Sf1a and Sf1b Helicase Structure and Function.Genes · 2021Review
- Editorial: Single-molecule studies of DNA-protein interactions collection 2021.Nucleic acids research · 2021Article
- Mechanistic Insights From Single-Molecule Studies of Repair of Double Strand Breaks.Frontiers in cell and developmental biology · 2021Review
- DNA bridges: A novel platform for single-molecule sequencing and other DNA-protein interaction applications.PloS one · 2021Article
Corrections and comments
- Erratum issuedCorrection.2024
Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
RECQ5 is one of five RecQ helicases found in humans and is thought to participate in homologous DNA recombination by acting as a negative regulator of the recombinase protein RAD51. Here, we use kinetic and single molecule imaging methods to monitor RECQ5 behavior on various nucleoprotein complexes. Our data demonstrate that RECQ5 can act as an ATP-dependent single-stranded DNA (ssDNA) motor protein and can translocate on ssDNA that is bound by replication protein A (RPA). RECQ5 can also translocate on RAD51-coated ssDNA and readily dismantles RAD51-ssDNA filaments. RECQ5 interacts with RAD51 through protein-protein contacts, and disruption of this interface through a RECQ5-F666A mutation reduces translocation velocity by ∼50%. However, RECQ5 readily removes the ATP hydrolysis-deficient mutant RAD51-K133R from ssDNA, suggesting that filament disruption is not coupled to the RAD51 ATP hydrolysis cycle. RECQ5 also readily removes RAD51-I287T, a RAD51 mutant with enhanced ssDNA-binding activity, from ssDNA. Surprisingly, RECQ5 can bind to double-stranded DNA (dsDNA), but it is unable to translocate. Similarly, RECQ5 cannot dismantle RAD51-bound heteroduplex joint molecules. Our results suggest that the roles of RECQ5 in genome maintenance may be regulated in part at the level of substrate specificity.
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.