Journal of Biological Chemistry
Volume 286, Issue 5, 4 February 2011, Pages 3579-3586
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Cell Biology
A Conserved Motif at the C Terminus of Sororin Is Required for Sister Chromatid Cohesion*

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Sororin is a positive regulator of sister chromatid cohesion that interacts with the cohesin complex. Sororin is required for the increased stability of the cohesin complex on chromatin following DNA replication and sister chromatid cohesion during G2. The mechanism by which sororin ensures cohesion is currently unknown. Because the primary sequence of sororin does not contain any previously characterized structural or functional motifs, we have undertaken a structure-function analysis of the sororin protein. Using a series of mutant derivatives of sororin, we show that the ability of sororin to bind to chromatin is separable from both its role in sister chromatid cohesion and its interaction with the cohesin complex. We also show that derivatives of sororin with deletions or mutations in the conserved C terminus fail to rescue the loss-of-cohesion phenotype caused by sororin RNAi and that these mutations also abrogate the association of sororin with the cohesin complex. Our data suggest that the interaction of the highly conserved motif at the C terminus of sororin with the cohesin complex is critical to its ability to mediate sister chromatid cohesion.

Cell Division
Chromosomes
Mitosis
Protein Sequence
Protein-Protein Interactions
Cohesin Complex
Sister Chromatid Cohesion
Sororin
Structure-Function

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*

This work was supported, in whole or in part, by National Institutes of Health Grant RR016478 through the NCRR. This work was also supported by Oklahoma Center for the Advancement of Science and Technology Grant HR06-175S.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables 1 and 2 and Fig. 1.

1

Supported by a J. Donald Capra predoctoral fellowship.

2

Present address: Solomon H. Snyder Dept. of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.