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MBC in Press, published online ahead of print March 5, 2008
Mol. Biol. Cell 10.1091/mbc.E07-11-1113

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Submitted on November 6, 2007
Revised on January 29, 2008
Accepted on February 27, 2008

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

Hui Yang, Qun Ren, and Zhaojie Zhang

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

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 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.

Apoptosis; Cohesin; Mcd1; Esp1; S. cerevisiae; yeast

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






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