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J. Biol. Chem., Vol. 276, Issue 49, 46111-46117, December 7, 2001
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From the Department of Molecular Biology, Hebrew University Medical
School, Jerusalem 91120, Israel
We have previously proposed that a single
translation product of the FUM1 gene encoding fumarase is
distributed between the cytosol and mitochondria of Saccharomyces
cerevisiae and that all fumarase translation products are
targeted and processed in mitochondria before distribution. Alternative
models for fumarase distribution have been proposed that require more
than one translation product. In the current work (i) we show by using
sequential Edman degradation and mass spectrometry that fumarase
cytosolic and mitochondrial isoenzymes have an identical amino terminus
that is formed by cleavage by the mitochondrial processing
peptidase, (ii) we have generated fumarase mutants in which the
second potential translation initiation codon (Met-24) has been
substituted, yet the protein is processed efficiently and retains its
ability to be distributed between the cytosol and mitochondria, and
(iii) we show that although a signal peptide is required for fumarase targeting to mitochondria the specific fumarase signal peptide and the
sequence immediately downstream to the cleavage site are not required
for the dual distribution phenomenon. Our results are discussed in
light of our model of fumarase targeting and distribution that suggests
rapid folding into an import-incompetent state and retrograde movement
of the processed protein back to the cytosol through the translocation pore.
Mitochondrial and Cytosolic Isoforms of Yeast Fumarase Are
Derivatives of a Single Translation Product and Have Identical Amino
Termini*
*
This research was supported by the German-Israeli Foundation
for Scientific Research and Development (GIF) (to W. Neupert and
O. 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.
To whom correspondence should be addressed. Tel.: 972-2-6757203;
Fax: 972-2-6758918; E-mail: ophry@md.huji.ac.il.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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