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DNA Reshaping by MukB RIGHT-HANDED KNOTTING, LEFT-HANDED SUPERCOILING [PDF]

open access: yesJournal of Biological Chemistry, 2006
MukB is a bacterial SMC (structural maintenance of chromosome) protein required for faithful chromosome segregation in Escherichia coli. We report here that purified MukB introduces right-handed knots into DNA in the presence of type-2 topoisomerase, indicating that the protein promotes intramolecular DNA condensation.
Valentin V Rybenkov, Zoya M Petrushenko
exaly   +3 more sources
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MukB acts as a macromolecular clamp in DNA condensation

Nature Structural & Molecular Biology, 2008
Correct folding of the chromosome into its highly ordered structure requires the action of condensins. The multisubunit condensins are highly conserved from bacteria to humans, and at their core they contain the characteristic V-shaped dimer of structural maintenance of chromosome proteins.
Yuanbo, Cui   +2 more
openaire   +2 more sources

A Repeated Coiled-Coil Interruption in the Escherichia coli Condensin MukB

Journal of Molecular Biology, 2011
MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosome segregation and condensation in Escherichia coli and other γ-proteobacteria. MukB and canonical SMC proteins share a common five-domain structure in which globular N- and C-terminal regions combine to form an ATP-binding-cassette-like ATPase domain.
Christopher S, Weitzel   +3 more
openaire   +2 more sources

The bacterial condensin MukB compacts DNA by sequestering supercoils and stabilizing topologically isolated loops [PDF]

open access: yesJournal of Biological Chemistry, 2017
MukB is a structural maintenance of chromosome-like protein required for DNA condensation. The complete condensin is a large tripartite complex of MukB, the kleisin, MukF, and an accessory protein, MukE. As found previously, MukB DNA condensation is a stepwise process. We have defined these steps topologically.
Rupesh Kumar   +2 more
exaly   +3 more sources

Cloning, sequencing, and characterization of multicopy suppressors of a mukB mutation in Escherichia coli

Molecular Microbiology, 1994
SummaryThe mukB gene codes for a 177kDa protein, which might be a candidate for a force‐generating enzyme in chromosome positioning in Escherichia coli. The mukB106 mutant produces normal‐sized, anucleate cells and shows a temperature‐sensitive colony formation.
K, Yamanaka   +4 more
openaire   +2 more sources

Amino acid residues for specific binding to ssDNA facilitate topological loading of bacterial condensin MukB

2023
ABSTRACT The bacterial condensin MukB facilitates proper chromosome segregation in Escherichia coli . A portion of the MukB proteins localize at a specific chromosome region, binding to DNA in a non-sequence-specific manner.
Koichiro Akiyama   +2 more
openaire   +1 more source

New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli

Molecular and General Genetics MGG, 1994
The nucleotide sequence was determined of the region upstream of the mukB gene of Escherichia coli. Two new genes were found, designated kicA and kicB (killing of cell); the gene order is kicB-kicA-mukB. Promoter activities were detected in the regions immediately upstream of kicB and kicA, but not in front of mukB. Gene disruption experiments revealed
J, Feng   +4 more
openaire   +2 more sources

Identification of Interacting Regions within the Coiled Coil of the Escherichia coli Structural Maintenance of Chromosomes Protein MukB

Journal of Molecular Biology, 2009
MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosome segregation and condensation in Escherichia coli and other gamma-proteobacteria. MukB and canonical SMC proteins share a common five-domain structure in which globular N- and C-terminal regions combine to form an ABC-like ATPase domain. This ATPase domain
Yinyin, Li   +3 more
openaire   +2 more sources

Comparison of MukB homodimer versus MukBEF complex molecular architectures by electron microscopy reveals a higher-order multimerization

Biochemical and Biophysical Research Communications, 2005
Kouta Mayanagi   +2 more
exaly  

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