ArticleScientific reports2015
The Smc5-Smc6 heterodimer associates with DNA through several independent binding domains.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 17 citations in OpenAlex.
- Smc5/6 uses its head-NSE module to preferentially associate with ssDNA gaps and ss-dsDNA junctions.Nucleic acids research · 2026Article
- The Smc5/6 complex counteracts R-loop formation at highly transcribed genes in cooperation with RNase H2.eLife · 2024Article
- The SMC5/6 complex: folding chromosomes back into shape when genomes take a break.Nucleic acids research · 2024Review
- SMC5/6 Promotes Replication Fork Stability via Negative Regulation of the COP9 Signalosome.International journal of molecular sciences · 2024Article
- Stabilization of DNA fork junctions by Smc5/6 complexes revealed by single-molecule imaging.Cell reports · 2022Article
- KSHV RTA antagonizes SMC5/6 complex-induced viral chromatin compaction by hijacking the ubiquitin-proteasome system.PLoS pathogens · 2022Article
- Comprehensive Analysis of SMC Gene Family Prognostic Value and Immune Infiltration in Patients With Pancreatic Adenocarcinoma.Frontiers in medicine · 2022Article
- Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding.The EMBO journal · 2021Article
- The Smc5/6 Core Complex Is a Structure-Specific DNA Binding and Compacting Machine.Molecular cell · 2020Article
- Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction.Molecular cell · 2020Article
- Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin.Molecular cell · 2019Article
- DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex.The EMBO journal · 2018Article
- Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Incision of damaged DNA in the presence of an impaired Smc5/6 complex imperils genome stability.Nucleic acids research · 2016Article
- DNA Repair--A Double-Edged Sword in the Genomic Stability of Cancer Cells--The Case of Chronic Myeloid Leukemia.International journal of molecular sciences · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Smc5-6 complex is required for the maintenance of genome integrity through its functions in DNA repair and chromosome biogenesis. However, the specific mode of action of Smc5 and Smc6 in these processes remains largely unknown. We previously showed that individual components of the Smc5-Smc6 complex bind strongly to DNA as monomers, despite the absence of a canonical DNA-binding domain (DBD) in these proteins. How heterodimerization of Smc5-6 affects its binding to DNA, and which parts of the SMC molecules confer DNA-binding activity is not known at present. To address this knowledge gap, we characterized the functional domains of the Smc5-6 heterodimer and identify two DBDs in each SMC molecule. The first DBD is located within the SMC hinge region and its adjacent coiled-coil arms, while the second is found in the conserved ATPase head domain. These DBDs can independently recapitulate the substrate preference of the full-length Smc5 and Smc6 proteins. We also show that heterodimerization of full-length proteins specifically increases the affinity of the resulting complex for double-stranded DNA substrates. Collectively, our findings provide critical insights into the structural requirements for effective binding of the Smc5-6 complex to DNA repair substrates in vitro and in live cells.
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.