Results 11 to 20 of about 1,562 (148)
MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin
The Escherichia coli SMC complex, MukBEF, acts in chromosome segregation. MukBEF shares the distinctive architecture of other SMC complexes, with one prominent difference; unlike other kleisins, MukF forms dimers through its N-terminal domain.
Katarzyna Zawadzka +6 more
doaj +5 more sources
The MukB-topoisomerase IV interaction mutually suppresses their catalytic activities. [PDF]
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 ...
Kumar R, Bahng S, Marians KJ.
europepmc +4 more sources
The condensin II complex mutations R551P, R551S, and S556F cause genomic instability by causing DNA damage, anaphase defects, micronuclei, and chromosomal instability. DNA damage and anaphase defects are caused primarily by ataxia telangiectasia and Rad3‐related‐dependent telomere dysfunction.
Emily Weyburne, Giovanni Bosco
wiley +1 more source
Transient growth arrest in Escherichia coli induced by chromosome condensation. [PDF]
MukB is a bacterial SMC (structural maintenance of chromosome) protein that regulates the global folding of the Escherichia coli chromosome by bringing distant DNA segments together.
Andrea L Edwards +4 more
doaj +1 more source
DNA Reshaping by MukB RIGHT-HANDED KNOTTING, LEFT-HANDED SUPERCOILING [PDF]
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.
Zoya M, Petrushenko +3 more
openaire +2 more sources
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.
Zoya M, Petrushenko +2 more
openaire +2 more sources
MukB-mediated Catenation of DNA Is ATP and MukEF Independent [PDF]
Properly condensed chromosomes are necessary for accurate segregation of the sisters after DNA replication. The Escherichia coli condesin is MukB, a structural maintenance of chromosomes (SMC)-like protein, which forms a complex with MukE and the kleisin MukF. MukB is known to be able to mediate knotting of a DNA ring, an intramolecular reaction.
Soon, Bahng +2 more
openaire +2 more sources
Mutants Suppressing Novobiocin Hypersensitivity of amukBNull Mutation [PDF]
ABSTRACTThemukBgene is essential for the partitioning of sister chromosomes inEscherichia coli. AmukBnull mutant is hypersensitive to the DNA gyrase inhibitor novobiocin. In this work, we isolated mutants suppressing the novobiocin hypersensitivity of themukBnull mutation.
Shun, Adachi, Sota, Hiraga
openaire +2 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 +4 more
openaire +2 more sources
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.
Weifeng, She +3 more
openaire +2 more sources

