ArticleThe Journal of biological chemistry2016
MukB-mediated Catenation of DNA Is ATP and MukEF Independent.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed.
- DNA sliding and loop formation byBiochemistry and biophysics reports · 2022Article
- Intersubunit and intrasubunit interactions driving the MukBEF ATPase.The Journal of biological chemistry · 2022Article
- The MukB-topoisomerase IV interaction mutually suppresses their catalytic activities.Nucleic acids research · 2022Article
- Condensin minimizes topoisomerase II-mediated entanglements of DNA in vivo.The EMBO journal · 2021Article
- Protease-deficient SOS constitutive cells have RecN-dependent cell division phenotypes.Molecular microbiology · 2019Article
- Dissecting DNA Compaction by the Bacterial Condensin MukB.Methods in molecular biology (Clifton, N.J.) · 2019Article
- MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin.eLife · 2018Article
- The MukB-topoisomerase IV interaction is required for proper chromosome compaction.The Journal of biological chemistry · 2017Article
- The bacterial condensin MukB compacts DNA by sequestering supercoils and stabilizing topologically isolated loops.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Properly condensed chromosomes are necessary for accurate segregation of the sisters after DNA replication. The Escherichia coli condesin is MukB, a structural maintenance of chromosomes (SMC)-like protein, which forms a complex with MukE and the kleisin MukF. MukB is known to be able to mediate knotting of a DNA ring, an intramolecular reaction. In our investigations of how MukB condenses DNA we discovered that it can also mediate catenation of two DNA rings, an intermolecular reaction. This activity of MukB requires DNA binding by the head domains of the protein but does not require either ATP or its partner proteins MukE or MukF. The ability of MukB to mediate DNA catenation underscores its potential for bringing distal regions of a chromosome together.
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Registered trials
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