ArticleNucleic acids research2019
Dynamic architecture of the Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF.
Article in Nucleic acids research, 2019. 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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14 citing papers in PubMed, 25 citations in OpenAlex.
- Involvement of the inner surface residues of bacterial SMC protein MukB in the ssDNA binding in vitro.Communications biology · 2025Article
- Loop-extrusion-mediated plasmid DNA cleavage by the bacterial SMC Wadjet complex.Molecular cell · 2025Article
- Loop extrusion-mediated plasmid DNA cleavage by the bacterial SMC Wadjet complex.bioRxiv : the preprint server for biology · 2024Article
- The SMC-family Wadjet complex protects bacteria from plasmid transformation by recognition and cleavage of closed-circular DNA.Molecular cell · 2022Article
- DNA sliding and loop formation byBiochemistry and biophysics reports · 2022Article
- DNA tension-modulated translocation and loop extrusion by SMC complexes revealed by molecular dynamics simulations.Nucleic acids research · 2022Article
- Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites.Molecular cell · 2021Article
- Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.Nature communications · 2021Article
- Article
- XerD unloads bacterial SMC complexes at the replication terminus.Molecular cell · 2021Article
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.Nucleic acids research · 2020Review
- SMC complexes organize the bacterial chromosome by lengthwise compaction.Current genetics · 2020Review
- Organization of the Escherichia coli Chromosome by a MukBEF Axial Core.Molecular cell · 2020Article
- Article
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12 authors at 1 institution in 1 country.
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Abstract
Ubiquitous Structural Maintenance of Chromosomes (SMC) complexes use a proteinaceous ring-shaped architecture to organize and individualize chromosomes, thereby facilitating chromosome segregation. They utilize cycles of adenosine triphosphate (ATP) binding and hydrolysis to transport themselves rapidly with respect to DNA, a process requiring protein conformational changes and multiple DNA contact sites. By analysing changes in the architecture and stoichiometry of the Escherichia coli SMC complex, MukBEF, as a function of nucleotide binding to MukB and subsequent ATP hydrolysis, we demonstrate directly the formation of dimer of MukBEF dimer complexes, dependent on dimeric MukF kleisin. Using truncated and full length MukB, in combination with MukEF, we show that engagement of the MukB ATPase heads on nucleotide binding directs the formation of dimers of heads-engaged dimer complexes. Complex formation requires functional interactions between the C- and N-terminal domains of MukF with the MukB head and neck, respectively, and MukE, which organizes the complexes by stabilizing binding of MukB heads to MukF. In the absence of head engagement, a MukF dimer bound by MukE forms complexes containing only a dimer of MukB. Finally, we demonstrate that cells expressing MukBEF complexes in which MukF is monomeric are Muk-, with the complexes failing to associate with chromosomes.
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