Show simple item record

dc.contributor.authorSchalbetter, Stephanie Andrea
dc.contributor.authorGoloborodko, Anton
dc.contributor.authorFudenberg, Geoffrey
dc.contributor.authorBelton, Jon-Matthew
dc.contributor.authorMiles, Catrina
dc.contributor.authorYu, Miao
dc.contributor.authorDekker, Job
dc.contributor.authorMirny, Leonid
dc.contributor.authorBaxter, Jonathan
dc.date2022-08-11T08:10:59.000
dc.date.accessioned2022-08-23T17:27:21Z
dc.date.available2022-08-23T17:27:21Z
dc.date.issued2017-09-01
dc.date.submitted2017-11-30
dc.identifier.citation<p>Nat Cell Biol. 2017 Sep;19(9):1071-1080. doi: 10.1038/ncb3594. Epub 2017 Aug 21. <a href="https://doi.org/10.1038/ncb3594">Link to article on publisher's site</a></p>
dc.identifier.issn1465-7392 (Linking)
dc.identifier.doi10.1038/ncb3594
dc.identifier.pmid28825700
dc.identifier.urihttp://hdl.handle.net/20.500.14038/49843
dc.description.abstractStructural maintenance of chromosomes (SMC) protein complexes are key determinants of chromosome conformation. Using Hi-C and polymer modelling, we study how cohesin and condensin, two deeply conserved SMC complexes, organize chromosomes in the budding yeast Saccharomyces cerevisiae. The canonical role of cohesin is to co-align sister chromatids, while condensin generally compacts mitotic chromosomes. We find strikingly different roles for the two complexes in budding yeast mitosis. First, cohesin is responsible for compacting mitotic chromosome arms, independently of sister chromatid cohesion. Polymer simulations demonstrate that this role can be fully accounted for through cis-looping of chromatin. Second, condensin is generally dispensable for compaction along chromosome arms. Instead, it plays a targeted role compacting the rDNA proximal regions and promoting resolution of peri-centromeric regions. Our results argue that the conserved mechanism of SMC complexes is to form chromatin loops and that distinct SMC-dependent looping activities are selectively deployed to appropriately compact chromosomes.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=28825700&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5640152/
dc.subjectChromosome condensation
dc.subjectChromosome conformation capture-based methods
dc.subjectCohesion
dc.subjectDNA sequencing
dc.subjectMitosis
dc.subjectComputational Biology
dc.subjectGenomics
dc.subjectStructural Biology
dc.subjectSystems Biology
dc.titleSMC complexes differentially compact mitotic chromosomes according to genomic context
dc.typeJournal Article
dc.source.journaltitleNature cell biology
dc.source.volume19
dc.source.issue9
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/sysbio_pubs/117
dc.identifier.contextkey11176473
html.description.abstract<p>Structural maintenance of chromosomes (SMC) protein complexes are key determinants of chromosome conformation. Using Hi-C and polymer modelling, we study how cohesin and condensin, two deeply conserved SMC complexes, organize chromosomes in the budding yeast Saccharomyces cerevisiae. The canonical role of cohesin is to co-align sister chromatids, while condensin generally compacts mitotic chromosomes. We find strikingly different roles for the two complexes in budding yeast mitosis. First, cohesin is responsible for compacting mitotic chromosome arms, independently of sister chromatid cohesion. Polymer simulations demonstrate that this role can be fully accounted for through cis-looping of chromatin. Second, condensin is generally dispensable for compaction along chromosome arms. Instead, it plays a targeted role compacting the rDNA proximal regions and promoting resolution of peri-centromeric regions. Our results argue that the conserved mechanism of SMC complexes is to form chromatin loops and that distinct SMC-dependent looping activities are selectively deployed to appropriately compact chromosomes.</p>
dc.identifier.submissionpathsysbio_pubs/117
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentProgram in Systems Biology
dc.source.pages1071-1080


This item appears in the following Collection(s)

Show simple item record