ArticleThe Journal of biological chemistry2017
The MukB-topoisomerase IV interaction is required for proper chromosome compaction.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- 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
- Temporospatial control of topoisomerases by essential cellular processes.Current opinion in microbiology · 2024Review
- Single-nucleotide resolution detection of Topo IV cleavage activity in theFrontiers in microbiology · 2023Article
- MukBEF-dependent chromosomal organization in widenedFrontiers in microbiology · 2023Article
- Intersubunit and intrasubunit interactions driving the MukBEF ATPase.The Journal of biological chemistry · 2022Article
- Extended sister-chromosome catenation leads to massive reorganization of the E. coli genome.Nucleic acids research · 2022Article
- The MukB-topoisomerase IV interaction mutually suppresses their catalytic activities.Nucleic acids research · 2022Article
- Topoisomerase IV tracks behind the replication fork and the SeqA complex during DNA replication in Escherichia coli.Scientific reports · 2021Article
- Mechanisms for Chromosome Segregation in Bacteria.Frontiers in microbiology · 2021Review
- Alternating Dynamics ofmSphere · 2020Article
- Topoisomerase III Acts at the Replication Fork To Remove Precatenanes.Journal of bacteriology · 2019Article
- A Topology-Centric View on Mitotic Chromosome Architecture.International journal of molecular sciences · 2017Review
- 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
5 authors.
Funding
Abstract
The bacterial condensin MukB and the cellular decatenating enzyme topoisomerase IV interact. This interaction stimulates intramolecular reactions catalyzed by topoisomerase IV, supercoiled DNA relaxation, and DNA knotting but not intermolecular reactions such as decatenation of linked DNAs. We have demonstrated previously that MukB condenses DNA by sequestering negative supercoils and stabilizing topologically isolated loops in the DNA. We show here that the MukB-topoisomerase IV interaction stabilizes MukB on DNA, increasing the extent of DNA condensation without increasing the amount of MukB bound to the DNA. This effect does not require the catalytic activity of topoisomerase IV. Cells carrying a
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Registered trials
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