Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning [PDF]
The 170 kDa protein MukB has been implicated in ATP-dependent chromosome partitioning during cell division in Escherichia coli. MukB shares its dimeric structure and domain architecture with the ubiquitous family of SMC (structural maintenance of chromosomes) proteins that facilitate similar functions.
Jan Lowe +2 more
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Localization of replication forks in wild-type and mukB mutant cells of Escherichia coli
To examine the subcellular localization of the replication machinery in Escherichia coli, we have developed an immunofluorescence method that allows us to determine the subcellular location of newly synthesized DNA pulse-labeled with 5-bromo-2'-deoxyuridine (BrdU). Using this technique, we have analyzed growing cells.
Shun Adachi, Sota Hiraga
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Dissecting DNA Compaction by the Bacterial Condensin MukB
Condensins in bacteria are one of the most important factors involved in the organization of long threads of DNA into compact chromosomes. The organization of DNA by condensins is vital to many DNA transactions including DNA repair and chromosome segregation.
Rupesh Kumar +2 more
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MukEF Is Required for Stable Association of MukB with the Chromosome [PDF]
ABSTRACTMukB is a bacterial SMC(structural maintenance of chromosome) protein required for correct folding of theEscherichia colichromosome. MukB acts in complex with the two non-SMC proteins, MukE and MukF. The role of MukEF is unclear. MukEF disrupts MukB-DNA interactions in vitro.
Valentin V Rybenkov +2 more
exaly +3 more sources
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Nucleotide-Dependent Interaction of the N-Terminal Domain of MukB with Microtubules
Journal of Structural Biology, 1998The MukB protein from Escherichia coli has a domain structure that is reminiscent of the eukaryotic motor proteins kinesin and myosin: N-terminal globular domains, a region of coiled-coil, and a specialised C-terminal domain. Sequence alignment of the N-terminal domain of MukB with the kinesin motor domain indicated an approximately 22% sequence ...
John Kendrick-Jones, A Lockhart
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Antagonistic Interactions of Kleisins and DNA with Bacterial Condensin MukB [PDF]
MukBEF is a bacterial SMC (structural maintenance of chromosome) complex required for faithful chromosome segregation in Escherichia coli. The SMC subunit of the complex, MukB, promotes DNA condensation in vitro and in vivo; however, all three subunits are required for the function of MukBEF.
Valentin V Rybenkov, Zoya M Petrushenko
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Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity [PDF]
The purified MukB protein of Escherichia coli has DNA binding activity and nucleotide binding activity. We have isolated a mutation, mukB1013, causing a substitution of valine at position 1379 to leucine. This mutant MukB protein was defective for DNA binding, while the ATP binding activity remained unaffected. A truncated MukB protein that is short of
Hironori Niki +2 more
exaly +4 more sources
The MukB–topoisomerase IV interaction is required for proper chromosome compaction [PDF]
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.
Rupesh Kumar +2 more
exaly +3 more sources
Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli [PDF]
mukF, mukE and mukB genes are essential for the process of chromosome partitioning in Escherichia coli. We have studied protein-protein interactions among MukB, MukE and MukF proteins by co-immunoprecipitation and sucrose gradient sedimentation experiments, using mukFEB null cells harboring plasmids carrying the wild-type or mutant-type mukFEB operon ...
Hironori Niki +2 more
exaly +3 more sources
FtsZ rings in mukB mutants with or without the Min system
Biochimie, 2001The site of cell division in Escherichia coli is defined by formation of the Z ring between the two segregated daughter nucleoids. Positioning of the Z ring, composed of the highly conserved and tubulin-like FtsZ protein, appears to be negatively regulated by both the nucleoid and the oscillating MinCD inhibitor proteins.
William Margolin, X C Yu
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