ArticleNucleic acids research2022
The MukB-topoisomerase IV interaction mutually suppresses their catalytic activities.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Spatio-temporal organization of theEcoSal Plus · 2024Review
- Temporospatial control of topoisomerases by essential cellular processes.Current opinion in microbiology · 2024Review
- Bacterial chromatin proteins, transcription, and DNA topology: Inseparable partners in the control of gene expression.Molecular microbiology · 2024Review
- Activity of MukBEF for chromosome management ineLife · 2024Article
- DNA Segregation in Enterobacteria.EcoSal Plus · 2023Review
- The MksG nuclease is the executing part of the bacterial plasmid defense system MksBEFG.Nucleic acids research · 2023Article
- 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
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial condensin MukB and the cellular chromosomal decatenase, topoisomerase IV interact and this interaction is required for proper condensation and topological ordering of the chromosome. Here, we show that Topo IV stimulates MukB DNA condensation by stabilizing loops in DNA: MukB alone can condense nicked plasmid DNA into a protein-DNA complex that has greater electrophoretic mobility than that of the DNA alone, but both MukB and Topo IV are required for a similar condensation of a linear DNA representing long stretches of the chromosome. Remarkably, we show that rather than MukB stimulating the decatenase activity of Topo IV, as has been argued previously, in stoichiometric complexes of the two enzymes each inhibits the activity of the other: the ParC subunit of Topo IV inhibits the MukF-stimulated ATPase activity of MukB and MukB inhibits both DNA crossover trapping and DNA cleavage by Topo IV. These observations suggest that when in complex on the DNA, Topo IV inhibits the motor function of MukB and the two proteins provide a stable scaffold for chromosomal DNA condensation.
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