ArticleCurrent biology : CB2010
Both interaction surfaces within cohesin's hinge domain are essential for its stable chromosomal association.
Article in Current biology : CB, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Site-to-site mutational dissection of fission yeast cohesin reveals its dynamics.G3 (Bethesda, Md.) · 2025Article
- Folding of cohesin's coiled coil is important for Scc2/4-induced association with chromosomes.eLife · 2021Article
- A cohesin cancer mutation reveals a role for the hinge domain in genome organization and gene expression.PLoS genetics · 2021Article
- Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A role for the Smc3 hinge domain in the maintenance of sister chromatid cohesion.Molecular biology of the cell · 2018Article
- Specialized interfaces of Smc5/6 control hinge stability and DNA association.Nature communications · 2017Article
- A Cohesin-Based Partitioning Mechanism Revealed upon Transcriptional Inactivation of Centromere.PLoS genetics · 2016Article
- Cohesin's ATPase activity couples cohesin loading onto DNA with Smc3 acetylation.Current biology : CB · 2014Article
- ROCC, a conserved region in cohesin's Mcd1 subunit, is essential for the proper regulation of the maintenance of cohesion and establishment of condensation.Molecular biology of the cell · 2014Article
- Linking chromosome duplication and segregation via sister chromatid cohesion.Methods in molecular biology (Clifton, N.J.) · 2014Review
- Pds5 promotes and protects cohesin acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- DROMPA: easy-to-handle peak calling and visualization software for the computational analysis and validation of ChIP-seq data.Genes to cells : devoted to molecular & cellular mechanisms · 2013Article
- Pericentric chromatin loops function as a nonlinear spring in mitotic force balance.The Journal of cell biology · 2013Article
- Disengaging the Smc3/kleisin interface releases cohesin from Drosophila chromosomes during interphase and mitosis.The EMBO journal · 2013Article
- Article
- Sister chromatid cohesion.Cold Spring Harbor perspectives in biology · 2012Review
- Cohesin's DNA exit gate is distinct from its entrance gate and is regulated by acetylation.Cell · 2012Article
- Bub1 kinase and Sgo1 modulate pericentric chromatin in response to altered microtubule dynamics.Current biology : CB · 2012Article
- Cohesin: a catenase with separate entry and exit gates?Nature cell biology · 2011Review
- A positively charged channel within the Smc1/Smc3 hinge required for sister chromatid cohesion.The EMBO journal · 2011Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundThe cohesin complex that mediates sister chromatid cohesion contains three core subunits: Smc1, Smc3, and Scc1. Heterotypic interactions between Smc1 and Smc3 dimerization domains create stable V-shaped Smc1/Smc3 heterodimers with a hinge at the center and nucleotide-binding domains (NBDs) at the ends of each arm. Interconnection of each NBD through their association with the N- and C-terminal domains of Scc1 creates a tripartite ring, within which sister DNAs are thought to be entrapped (the ring model). Crystal structures show that the Smc1/Smc3 hinge has a toroidal shape, with independent "north" and "south" interaction surfaces on an axis of pseudosymmetry. The ring model predicts that sister chromatid cohesion would be lost by transient hinge opening.
resultsWe find that mutations within either interface weaken heterodimerization of isolated half hinges in vitro but do not greatly compromise formation of cohesin rings in vivo. They do, however, reduce the residence time of cohesin on chromosomes and cause lethal defects in sister chromatid cohesion. This demonstrates that mere formation of rings is insufficient for cohesin function. Stable cohesion requires cohesin rings that cannot easily open.
conclusionsEither the north or south hinge interaction surface is sufficient for the assembly of V-shaped Smc1/Smc3 heterodimers in vivo. Any tendency of Smc proteins with weakened hinges to dissociate will be suppressed by interconnection of their NBDs by Scc1. We suggest that transient hinge dissociation caused by the mutations described here is incompatible with stable sister chromatid cohesion because it permits chromatin fibers to escape from cohesin rings.
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