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J. Biol. Chem., Vol. 275, Issue 21, 16127-16133, May 26, 2000
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Determinants of Cytochrome c Pro-apoptotic Activity
THE ROLE OF LYSINE 72 TRIMETHYLATION*

Ruth M. KluckDagger , Lisa M. Ellerby§, H. Michael Ellerby§, Shahrouz Naiem§, Michael P. Yaffe, Emanuel Margoliash||, Dale Bredesen§, A. Grant Mauk**, Fred ShermanDagger Dagger , and Donald D. NewmeyerDagger §§

From the Dagger  Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121, the § Buck Center for Research in Aging, Novato, California 94945, the  Department of Biology, University of California, San Diego, La Jolla, California 92093-0347, the || Department of Biological Sciences, University of Illinois, Chicago, Illinois 60607, the ** Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada, and the Dagger Dagger  Department of Biochemistry and Biophysics, University of Rochester Medical School, Rochester, New York 14642

Cytochrome c released from vertebrate mitochondria engages apoptosis by triggering caspase activation. We previously reported that, whereas cytochromes c from higher eukaryotes can activate caspases in Xenopus egg and mammalian cytosols, iso-1 and iso-2 cytochromes c from the yeast Saccharomyces cerevisiae cannot. Here we examine whether the inactivity of the yeast isoforms is related to a post-translational modification of lysine 72, N-epsilon -trimethylation. This modification was found to abrogate pro-apoptotic activity of metazoan cytochrome c expressed in yeast. However, iso-1 cytochrome c lacking the trimethylation modification also was devoid of pro-apoptotic activity. Thus, both lysine 72 trimethylation and other features of the iso-1 sequence preclude pro-apoptotic activity. Competition studies suggest that the lack of pro-apoptotic activity was associated with a low affinity for Apaf-1. As cytochromes c that lack apoptotic function still support respiration, different mechanisms appear to be involved in the two activities.

* This work was supported by American Cancer Society Grant DB-97 (to D. D. N.); National Institutes of Health Grants GM50284 (to D. D. N.), AG12282 (to D. E. B.), NS40251 (to L. M. E.), GM12702 (to F. S.); and Medical Research Council of Canada Grant MT-14021 (to A. G. M.). This is publication 193 from the La Jolla Institute for Allergy and Immunology.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§§ To whom correspondence should be addressed: Div. of Cellular Immunology, La Jolla Inst. for Allergy and Immunology, 10355 Science Center Dr., San Diego, CA 92121. Tel.: 619-558-3539; Fax: 650-373-7424; E-mail: don_newmeyer@liai.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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