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Vol. 19, Issue 5, 2127-2134, May 2008

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Cleavage of Mcd1 by Caspase-like Protease Esp1 Promotes Apoptosis in Budding Yeast

Department of Zoology and Physiology, University of Wyoming, Laramie, WY 82071

Submitted November 6, 2007; Revised January 29, 2008; Accepted February 27, 2008
Monitoring Editor: Thomas Fox

Over the last decade, yeast has been used successfully as a model system for studying the molecular mechanism of apoptotic cell death. Here, we report that Mcd1, the yeast homology of human cohesin Rad21, plays an important role in hydrogen peroxide-induced apoptosis in yeast. On induction of cell death, Mcd1 is cleaved and the C-terminal fragment is translocated from nucleus into mitochondria, causing the decrease of mitochondrial membrane potential and the amplification of cell death in a cytochrome c-dependent manner. We further demonstrate that the caspase-like protease Esp1 has dual functions and that it is responsible for the cleavage of Mcd1 during the hydrogen peroxide-induced apoptosis. When apoptosis is induced, Esp1 is released from the anaphase inhibitor Pds1. The activated Esp1 acts as caspase-like protease for the cleavage of Mcd1, which enhances the cell death via its translocation from nucleus to mitochondria.

Address correspondence to: Zhaojie Zhang (zzhang{at}uwyo.edu)

Abbreviations used: _M, mitochondrial membrane potential; APC/C, anaphase-promoting complex or cyclosome; DAPI, 4',6-diamidino-2-phenylindole; GFP, green fluorescent protein; ROS, reactive oxygen species, zVAD-fmk, N-benzoylcarbonyl-Val-Ala-Asp fluoromethyl ketone.