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M.B. and L.C. contributed equally to this work.
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Involvement of the yeast metacaspase Yca1 in ubp10Δ-programmed cell death
Article first published online: 9 JAN 2006
DOI: 10.1016/j.femsyr.2004.07.005
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How to Cite
Bettiga, M., Calzari, L., Orlandi, I., Alberghina, L. and Vai, M. (2004), Involvement of the yeast metacaspase Yca1 in ubp10Δ-programmed cell death. FEMS Yeast Research, 5: 141–147. doi: 10.1016/j.femsyr.2004.07.005
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M.B. and L.C. contributed equally to this work.
Publication History
- Issue published online: 9 JAN 2006
- Article first published online: 9 JAN 2006
- Received 30 January 2004, Revised 14 July 2004, Accepted 16 July 2004
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Keywords:
- Apoptosis;
- Deubiquitinating enzyme;
- Metacaspase;
- Ascorbic acid
Abstract
UBP10 encodes a deubiquitinating enzyme of Saccharomyces cerevisiae. Its inactivation results in a complex phenotype characterized by a subpopulation of cells that exhibits the typical cellular markers of apoptosis. Here, we show that additional deletion of YCA1, coding for the yeast metacaspase, suppressed the ubp10 disruptant phenotype. Moreover, YCA1 overexpression, without any external stimulus, had a detrimental effect on growth and viability of ubp10 cells accompanied by an increase of apoptotic cells. This response was completely abrogated by ascorbic acid addition.
We also observed that cells lacking UBP10 had an endogenous caspase activity, revealed by incubation in vivo with FITC-labeled VAD-fmk. All these results argue in favour of an involvement of the yeast metacaspase in the active cell death triggered by loss of UBP10 function.