Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions - Wikidata - wikimedia - TriplyDB

Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions

Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions

http://www.wikidata.org/entity/Q27653382

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Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1 Condensins: universal organizers of chromosomes with diverse functions Multistep assembly of DNA condensation clusters by SMC.Structural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 Complex The Crystal Structure of the Hinge Domain of the Escherichia coli Structural Maintenance of Chromosomes Protein MukB The Role of MukE in Assembling a Functional MukBEF Complex Structural basis for the MukB-topoisomerase IV interaction and its functional implicationsin vivo An asymmetric SMC-kleisin bridge in prokaryotic condensin Transient growth arrest in Escherichia coli induced by chromosome condensation Cohesin: a catenase with separate entry and exit gates?Structural mapping of the coiled-coil domain of a bacterial condensin and comparative analyses across all domains of life suggest conserved features of SMC proteins.Physical manipulation of the Escherichia coli chromosome reveals its soft nature In vivo architecture and action of bacterial structural maintenance of chromosome proteins.The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks.In Favor of Establishment: Regulation of Chromatid Cohesion in Plants A new family of bacterial condensins Maintenance of chromosome structure in Pseudomonas aeruginosa Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli.Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction.Association of condensin with chromosomes depends on DNA binding by its HEAT-repeat subunits.Molecular basis for SMC rod formation and its dissolution upon DNA binding A novel mechanism for the establishment of sister chromatid cohesion by the ECO1 acetyltransferase.Crystal structure of the Mre11-Rad50-ATPγS complex: understanding the interplay between Mre11 and Rad50 MukBEF, a chromosomal organizer.Mre11-Rad50 complex crystals suggest molecular calisthenics.An SMC ATPase mutant disrupts chromosome segregation in Caulobacter.An SMC-like protein binds and regulates Caenorhabditis elegans condensins.Sister chromatid cohesion The MukB-ParC interaction affects the intramolecular, not intermolecular, activities of topoisomerase IV.SMC condensation centers in Bacillus subtilis are dynamic structures In vitro topological loading of bacterial condensin MukB on DNA, preferentially single-stranded DNA rather than double-stranded DNA.Pseudomonas aeruginosa Condensins Support Opposite Differentiation States.The Localization and Action of Topoisomerase IV in Escherichia coli Chromosome Segregation Is Coordinated by the SMC Complex, MukBEF.Cohesin and related coiled-coil domain-containing complexes physically and functionally connect the dots across the genome.The SMC complexes, DNA and chromosome topology: right or knot?The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes.The SMC complex MukBEF recruits topoisomerase IV to the origin of replication region in live Escherichia coli.A new twist in the coil: functions of the coiled-coil domain of structural maintenance of chromosome (SMC) proteins.Mechanics of DNA bridging by bacterial condensin MukBEF in vitro and in singulo.

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P2860

Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions

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Min-Kang Suh

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