is the protein
complex responsible for binding the sister chromatids
through the G2 phase
and into mitosis phase. It is a multi-subunit complex called which contains four core subunits: Smc1 and Smc3, which are members of the structural maintenance of chromosomes (SMC) protein family, and two non-SMC subunits, Scc1 (also called Mcd1) which is a member of the kleisin family, and Scc3. At metaphase
, most cohesin is removed, except for some at the centromere
. At Anaphase
, an inhibitory subunit of separase
, is hydrolyzed. Separase hydrolyzes the remaining cohesin. In a classical experiment by covalently linking Cohesin's subunits which form a tripartite ring structure, Scc1, Smc1 and Smc3, it was demonstrated that that cohesin rings concatenate individual sister minichromosome DNA molecules.
- Michaelis C, Ciosk R, Nasmyth K (1997). "Cohesins: chromosomal proteins that prevent premature separation of sister chromatids". Cell 91 (1): 35–45.
- Guacci V, Koshland D, Strunnikov A (1997). "A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae". Cell 91 (1): 47–57.
- Tóth A, Ciosk R, Uhlmann F, Galova M, Schleiffer A, Nasmyth K (1999). "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication". Genes Dev. 13 (3): 320–33.
- Uhlmann F, Lottspeich F, Nasmyth K (1999). "Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1". Nature 400 (6739): 37–42.