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Originally published In Press as doi:10.1074/jbc.M001891200 on May 1, 2000

J. Biol. Chem., Vol. 275, Issue 27, 20508-20513, July 7, 2000
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Cytochrome c Methyltransferase, Ctm1p, of Yeast*

Bogdan Polevoda, Mark R. Martzen, Biswadip Das, Eric M. Phizicky, and Fred ShermanDagger

From the Department of Biochemistry and Biophysics, University of Rochester Medical School, Rochester, New York 14642

Cytochromes c from plants and fungi, but not higher animals, contain methylated lysine residues at specific positions, including for example, the trimethylated lysine at position 72 in iso-1-cytochrome c of the yeast Saccharomyces cerevisiae. Testing of 6,144 strains of S. cerevisiae, each overproducing a different open reading frame fused to glutathione S-transferase, previously revealed that YHR109w was associated with an activity that methylated horse cytochrome c. We show here that this open reading frame, denoted Ctm1p, is specifically responsible for trimethylating lysine 72 of iso-1-cytochrome c. Unmethylated forms of cytochrome c but not other proteins or nucleic acids are methylated in vitro by Ctm1p produced in S. cerevisiae or Escherichia coli. Iso-1-cytochrome c purified from a ctm1-Delta strain is not trimethylated in vivo, whereas the K72R mutant form, or the trimethylated Lys-72 form of iso-1-cytochrome c, are not significantly methylated by Ctm1p in vitro. Like apocytochrome c, but in contrast to holocytochrome c, Ctm lp is located in the cytosol, consistent with the view that the natural substrate is apocytochrome c. The ctm1-Delta strain lacking the methyltransferase did not exhibit any growth defect on a variety of media and growth conditions, and the unmethylated iso-1-cytochrome c was produced at the normal level and exhibited the normal activity in vivo. Ctm1p and cytochrome c were coordinately regulated during anaerobic to aerobic transition, a finding consistent with the view that this methyltransferase evolved to act on cytochrome c.

* This work was supported by National Institutes of Health Research Grant GM12702 (to F. S.) and by Merck Genome Research Institute Grant 196 (to E. M. P.).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.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, Box 712, University of Rochester Medical School, Rochester, NY 14642. Tel.: 716-275-6647; Fax: 716-275-6007; E-mail: Fred_Sherman@urmc.rochester.edu.

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