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Published online 13 November 2000. doi:10.1083/jcb.151.4.749
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© The Rockefeller University Press, 0021-9525/2000//749 $5.00
The Journal of Cell Biology, Volume 151, Number 4, , 2000 749-762

Original Article

Characterization of Vertebrate Cohesin Complexes and Their Regulation in Prophase



Izabela Sumaraa, Elisabeth Vorlaufera, Christian Gieffersa, Beate H. Petersa, and Jan-Michael Petersa

a Research Institute of Molecular Pathology (IMP), A-1030 Vienna, Austria
A-1030 Vienna, Austria.43-1-797-30-886; Fax: 43-1-798-7153; E-mail: peters@nt.imp.univie.ac.at

In eukaryotes, sister chromatids remain connected from the time of their synthesis until they are separated in anaphase. This cohesion depends on a complex of proteins called cohesins. In budding yeast, the anaphase-promoting complex (APC) pathway initiates anaphase by removing cohesins from chromosomes. In vertebrates, cohesins dissociate from chromosomes already in prophase. To study their mitotic regulation we have purified two 14S cohesin complexes from human cells. Both complexes contain SMC1, SMC3, SCC1, and either one of the yeast Scc3p orthologs SA1 and SA2. SA1 is also a subunit of 14S cohesin in Xenopus. These complexes interact with PDS5, a protein whose fungal orthologs have been implicated in chromosome cohesion, condensation, and recombination. The bulk of SA1- and SA2-containing complexes and PDS5 are chromatin-associated until they become soluble from prophase to telophase. Reconstitution of this process in mitotic Xenopus extracts shows that cohesin dissociation does neither depend on cyclin B proteolysis nor on the presence of the APC. Cohesins can also dissociate from chromatin in the absence of cyclin-dependent kinase 1 activity. These results suggest that vertebrate cohesins are regulated by a novel prophase pathway which is distinct from the APC pathway that controls cohesins in yeast.

Key Words: anaphase-promoting complex • cell cycle • chromosome • mitosis • sister chromatid cohesion

© 2000 The Rockefeller University Press

Abbreviations used in this paper: APC, anaphase-promoting complex; CDK1, cyclin-dependent kinase 1; DAPI, 4', 6'-diamidino-2-phenylindole.


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