help button home button Genetics AJP: Advances PE
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Genetics, Vol. 178, 2361-2372, April 2008, Copyright © 2008
doi:10.1534/genetics.107.085308

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Data Supplement
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Baskerville, C.
Right arrow Articles by Reed, S. I.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Baskerville, C.
Right arrow Articles by Reed, S. I.

The Protease Activity of Yeast Separase (Esp1) Is Required for Anaphase Spindle Elongation Independently of Its Role In Cleavage of Cohesin

Chris Baskerville*, Marisa Segal{dagger} and Steven I. Reed*,1

* Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037 and {dagger} Department of Genetics, University of Cambridge, Cambridge CB2 3EH, United Kingdom

1 Corresponding author: The Scripps Research Institute, Department of Molecular Biology, MB-7, 10550 N. Torrey Pines Rd., La Jolla, CA 92007.
E-mail: sreed{at}scripps.edu

Separase is a caspase-family protease required for the metaphase–anaphase transition in eukaryotes. In budding yeast, the separase ortholog, Esp1, has been shown to cleave a subunit of cohesin, Mcd1 (Scc1), thereby releasing sister chromatids from cohesion and allowing anaphase. However, whether Esp1 has other substrates required for anaphase has been controversial. Whereas it has been reported that cleavage of Mcd1 is sufficient to trigger anaphase in the absence of Esp1 activation, another study using a temperature-sensitive esp1 mutant concluded that depletion of Mcd1 was not sufficient for anaphase in the absence of Esp1 function. Here we revisit the issue and demonstrate that neither depletion of Mcd1 nor ectopic cleavage of Mcd1 by Tev1 protease is sufficient to support anaphase in an esp1 temperature-sensitive mutant. Furthermore, we demonstrate that the catalytic activity of the Esp1 protease is required for this Mcd1-independent anaphase function. These data suggest that another protein, possibly a spindle-associated protein, is cleaved by Esp1 to allow anaphase. Such a function is consistent with the previous observation that Esp1 localizes to the mitotic spindle during anaphase.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2008 by the Genetics Society of America.