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Evidence that loading of cohesin onto chromosomes involves opening of its SMC hinge.

Abstract:

Cohesin is a multisubunit complex that mediates sister-chromatid cohesion. Its Smc1 and Smc3 subunits possess ABC-like ATPases at one end of 50 nm long coiled coils. At the other ends are pseudosymmetrical hinge domains that interact to create V-shaped Smc1/Smc3 heterodimers. N- and C-terminal domains within cohesin's kleisin subunit Scc1 bind to Smc3 and Smc1 ATPase heads respectively, thereby creating a huge tripartite ring. It has been suggested that cohesin associates with chromosomes by ...

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Publication status:
Published

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Publisher copy:
10.1016/j.cell.2006.08.048

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Journal:
Cell More from this journal
Volume:
127
Issue:
3
Pages:
523-537
Publication date:
2006-11-01
DOI:
EISSN:
1097-4172
ISSN:
0092-8674

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