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- W2890981602 abstract "Cohesin is a ring-shaped, multi-subunit ATPase assembly that is fundamental to the spatiotemporal organization of chromosomes. The ring establishes a variety of chromosomal structures including sister chromatid cohesion and chromatin loops. At the core of the ring is a pair of highly conserved SMC (Structural Maintenance of Chromosomes) proteins, which are closed by the flexible kleisin subunit. In common with other essential SMC complexes including condensin and the SMC5-6 complex, cohesin encircles DNA inside its cavity, with the aid of HEAT (Huntingtin, elongation factor 3, protein phosphatase 2A and TOR) repeat auxiliary proteins. Through this topological embrace, cohesin is thought to establish a series of intra- and interchromosomal interactions by tethering more than one DNA molecule. Recent progress in biochemical reconstitution of cohesin provides molecular insights into how this ring complex topologically binds and mediates DNA-DNA interactions. Here, I review these studies and discuss how cohesin mediates such chromosome interactions." @default.
- W2890981602 created "2018-09-27" @default.
- W2890981602 creator A5019824906 @default.
- W2890981602 date "2018-10-20" @default.
- W2890981602 modified "2023-10-15" @default.
- W2890981602 title "DNA entry, exit and second DNA capture by cohesin: insights from biochemical experiments" @default.
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- W2890981602 doi "https://doi.org/10.1080/19491034.2018.1516486" @default.
- W2890981602 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6244732" @default.
- W2890981602 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30205748" @default.
- W2890981602 hasPublicationYear "2018" @default.
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