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First published online 11 April 2006
doi: 10.1242/jcs.02902

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The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S. cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2

David Walter^1,*, Silke Wissing^2,*, Frank Madeo^2,3 and Birthe Fahrenkrog^1,

¹ M. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
² Institute for Physiological Chemistry, University of Tübingen, 72076 Tübingen, Germany
³ IMB, Karl-Franzens University, Universitätsplatz 2, 8010 Graz, Austria

Author for correspondence (e-mail: birthe.fahrenkrog{at}unibas.ch)

Accepted 23 January 2006

Inhibitor-of-apoptosis proteins (IAPs) play a crucial role in the regulation of metazoan apoptosis. IAPs are typically characterized by the presence of one to three baculovirus IAP repeat (BIR) domains that are essential for their anti-apoptotic activity. Bir1p is the sole BIR-protein in yeast and has been shown to participate in chromosome segregation events. Here, we show that Bir1p is a substrate for Nma111p, which is the homologue of the human pro-apoptotic serine protease Omi/HtrA2 and which is known to mediate apoptosis in yeast. Bir1p is a cytoplasmic and nuclear protein, and yeast cells lacking bir1 are more sensitive to apoptosis induced by oxidative stress. Consistently, overexpression of Bir1p reduces apoptosis-like cell death, whereas this protective effect can be antagonized in vivo by simultaneous overexpression of Nma111p. Moreover, chronologically aged cells that constitutively overexpress Bir1p show a delayed onset of cell death. Therefore, Bir1p, like its closest metazoan homologues deterin and survivin, has dual functions: it participates in chromosome segregation events and cytokinesis and exhibits anti-apoptotic activity.

Key words: Bir1p, IAP, Nma111p, Omi/HtrA2, Yeast apoptosis

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