ArticleScientific reports2016
In vitro topological loading of bacterial condensin MukB on DNA, preferentially single-stranded DNA rather than double-stranded DNA.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- An Orc1 initiator-specific motif (ISM)-related region limits ORC-ssDNA binding and promotes replication origin specificity in budding yeast.Frontiers in microbiology · 2026Article
- Involvement of the inner surface residues of bacterial SMC protein MukB in the ssDNA binding in vitro.Communications biology · 2025Article
- Spatio-temporal organization of theEcoSal Plus · 2024Review
- MukBEF-dependent chromosomal organization in widenedFrontiers in microbiology · 2023Article
- Profiling a single-stranded DNA region within an rDNA segment that affects the loading of bacterial condensin.iScience · 2022Article
- SMC complexes: Lifting the lid on loop extrusion.Current opinion in cell biology · 2022Review
- Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites.Molecular cell · 2021Article
- Article
- MukB Is a Gene Necessary for Rapid Proliferation ofMicroorganisms · 2021Article
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- The Accidental Ally: Nucleosome Barriers Can Accelerate Cohesin-Mediated Loop Formation in Chromatin.Biophysical journal · 2020Article
- Topological DNA-binding of structural maintenance of chromosomes-like RecN promotes DNA double-strand break repair inCommunications biology · 2019Article
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- Article
- DNA entry, exit and second DNA capture by cohesin: insights from biochemical experiments.Nucleus (Austin, Tex.) · 2018Review
- The bacterial condensin MukB compacts DNA by sequestering supercoils and stabilizing topologically isolated loops.The Journal of biological chemistry · 2017Article
- The loading of condensin in the context of chromatin.Current genetics · 2017Review
- MukB-mediated Catenation of DNA Is ATP and MukEF Independent.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Condensin is the major driving force in the segregation of daughter chromosomes in prokaryotes. Core subunits of condensin belong to the SMC protein family, whose members are characterized by a unique ATPase activity and dimers with a V-shaped structure. The V-shaped dimers might close between head domains, forming a ring structure that can encircle DNA. Indeed, cohesin, which is a subfamily of SMC proteins, encircles double-stranded DNA to hold sister chromatids in eukaryotes. However, the question of whether or not condensin encircles the chromosomal DNA remains highly controversial. Here we report that MukB binds topologically to DNA in vitro, and this binding is preferentially single-stranded DNA (ssDNA) rather than double-stranded DNA. The binding of MukB to ssDNA does not require ATP. In fact, thermal energy enhances the binding. The non-SMC subunits MukF and MukE did stimulate the topological binding of MukB, although they hindered DNA-binding of MukB. Recent reports on the distribution of condensin in genomes reveal that actively transcribed genes in yeast and humans are enriched in condensin. In consideration of all these results, we propose that the binding specificity of condensin to chromosome is provided not by the DNA sequence but by the DNA structure, which is ssDNA.
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