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First published online 6 October 2009
doi: 10.1242/jcs.056887

Journal of Cell Science 122, 3931-3941 (2009)
Published by The Company of Biologists 2009
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Research Article

Nuclear localisation is crucial for the proapoptotic activity of the HtrA-like serine protease Nma111p

Kenneth D. Belanger1, David Walter2, Tracey A. Henderson1,*, Allison L. Yelton1,{ddagger}, Travis G. O'Brien1,*, Karyn G. Belanger1, Susan J. Geier1 and Birthe Fahrenkrog2,§

1 Department of Biology, Colgate University, 13 Oak Drive, Hamilton, NY 13346, USA
2 M. E. Muller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstr. 70, 4056 Basel, Switzerland

§ Author for correspondence (birthe.fahrenkrog{at}unibas.ch)

Accepted 21 August 2009

Programmed cell death is induced by the activation of a subset of intracellular proteins in response to specific extra- and intracellular signals. In the yeast Saccharomyces cerevisiae, Nma111p functions as a nuclear serine protease that is necessary for apoptosis under cellular stress conditions, such as elevated temperature or treatment of cells with hydrogen peroxide to induce cell death. We have examined the role of nuclear protein import in the function of Nma111p in apoptosis. Nma111p contains two small clusters of basic residues towards its N-terminus, both of which are necessary for efficient translocation into the nucleus. Nma111p does not shuttle between the nucleus and cytoplasm during either normal growth conditions or under environmental stresses that induce apoptosis. The N-terminal half of Nma111p is sufficient to provide the apoptosis-inducing activity of the protein, and the nuclear-localisation signal (NLS) sequences and catalytic serine 235 are both necessary for this function. We provide compelling evidence that intranuclear Nma111p activity is necessary for apoptosis in yeast.

Key words: Nma111p, HtrA, Serine protease, Yeast apoptosis, Nuclear-localisation signal


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