MukBEF-dependent chromosomal organization in widened Escherichia coli [PDF]
Frontiers in Microbiology, 2023 The bacterial chromosome is spatially organized through protein-mediated compaction, supercoiling, and cell-boundary confinement. Structural Maintenance of Chromosomes (SMC) complexes are a major class of chromosome-organizing proteins present throughout
Christos Gogou
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Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation [PDF]
Nature Communications, 2021 E. coli MukBEF is an SMC complex that plays key roles in chromosome organization-segregation. Here the authors show that the interaction between MukBEF and the Acyl Carrier Protein (AcpP) is essential for MukBEF activity in vitro (ATPase) and in vivo.
Josh P Prince +2 more
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DNA sliding and loop formation by E. coli SMC complex: MukBEF [PDF]
Biochemistry and Biophysics Reports, 2022 SMC (structural maintenance of chromosomes) complexes share conserved architectures and function in chromosome maintenance via an unknown mechanism. Here we have used single-molecule techniques to study MukBEF, the SMC complex in Escherichia coli.
Man Zhou
doaj +5 more sources
Competitive binding of MatP and topoisomerase IV to the MukB hinge domain [PDF]
eLife, 2021 Structural Maintenance of Chromosomes (SMC) complexes have ubiquitous roles in compacting DNA linearly, thereby promoting chromosome organization-segregation.
Gemma LM Fisher +10 more
doaj +5 more sources
Activity of MukBEF for chromosome management in E. coli and its inhibition by MatP [PDF]
eLife, 2023 Structural maintenance of chromosomes (SMC) complexes share conserved structures and serve a common role in maintaining chromosome architecture. In the bacterium Escherichia coli, the SMC complex MukBEF is necessary for rapid growth and the accurate ...
Mohammed Seba +2 more
doaj +5 more sources
MatP regulates the coordinated action of topoisomerase IV and MukBEF in chromosome segregation [PDF]
Nature Communications, 2016 MukBEF, the bacterial structural maintenance of chromosomes complex, is known to associate with origins of replication and topoisomerase IV. Here the authors show an association of MukBEF with MatP and replication termination regions, important for ...
Sophie Nolivos +2 more
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The Localization and Action of Topoisomerase IV in Escherichia coli Chromosome Segregation Is Coordinated by the SMC Complex, MukBEF [PDF]
Cell Reports, 2015 The type II topoisomerase TopoIV, which has an essential role in Escherichia coli chromosome decatenation, interacts with MukBEF, an SMC (structural maintenance of chromosomes) complex that acts in chromosome segregation.
Paweł Zawadzki +2 more
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Intersubunit and intrasubunit interactions driving the MukBEF ATPase [PDF]
Journal of Biological Chemistry, 2022 MukBEF, a structural maintenance of chromosome-like protein complex consisting of an ATPase, MukB, and two interacting subunits, MukE and MukF, functions as the bacterial condensin. It is likely that MukBEF compacts DNA via an ATP hydrolysis-dependent DNA loop-extrusion reaction similar to that demonstrated for the yeast structural maintenance of ...
Rupesh Kumar, Kenneth J Marians
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Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites [PDF]
Molecular Cell, 2021 SummaryThe ring-like structural maintenance of chromosomes (SMC) complex MukBEF folds the genome of Escherichia coli and related bacteria into large loops, presumably by active DNA loop extrusion. MukBEF activity within the replication terminus macrodomain is suppressed by the sequence specific unloader MatP.
Frank Bürmann +2 more
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Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic [PDF]
CellRing-like structural maintenance of chromosome (SMC) complexes are crucial for genome organization and operate through mechanisms of DNA entrapment and loop extrusion. Here, we explore the DNA loading process of the bacterial SMC complex MukBEF. Using cryoelectron microscopy (cryo-EM), we demonstrate that ATP binding opens one of MukBEF's three ...
Oliver Wilkinson +2 more
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