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Sister chromatid cohesion depends on a multiprotein cohesin complex containing two SMC subunits, Smc1 and Smc3, that dimerize to form V-shaped molecules with ABC-like ATPase heads at the tips of their two arms. Cohesin's Smc1 and Smc3 "heads" are connected by an alpha kleisin subunit called Scc1, forming a tripartite ring with a diameter around 40 nm. We show here that some cohesin remains tightly bound to circular minichromosomes after their purification from yeast cells and that cleavage either of cohesin's ring or of the minichromosome's DNA destroys their association. This suggests that the stable association between cohesin and chromatin detected here is topological rather than physical, which is consistent with the notion that DNA is trapped inside cohesin rings.

Original publication

DOI

10.1016/j.cell.2005.07.018

Type

Journal article

Journal

Cell

Publication Date

23/09/2005

Volume

122

Pages

849 - 860

Keywords

Cell Cycle Proteins, Chromatids, Chromosomal Proteins, Non-Histone, Chromosome Pairing, Chromosomes, Fungal, DNA, DNA, Circular, Fungal Proteins, Nuclear Proteins, Nucleosomes, Phosphoproteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins