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Papers In Press, published online ahead of print September 5, 2003
J. Biol. Chem, 10.1074/jbc.M302344200
Submitted on March 6, 2003
Revised on August 21, 2003
Accepted on September 5, 2003

Folding of fumarase during mitochondrial import determines its dual targeting in yeast

Ehud Sass, Sharon Karniely, and Ophry Pines

Molecular Biology, Hebrew University - Hadassah Medical School, Jerusalem 91120

Corresponding Author: ophry{at}md.huji.ac.il

We have previously proposed that a single translation product of the FUM1 gene encoding fumarase is distributed between the cytosol and mitochondria of S. cerevisiae and that all fumarase translation products are targeted and processed in mitochondria before distribution. Thus, fumarase processed in mitochondria returns to the cytosol. In the current work we (i) have generated mutations throughout the coding sequence which result in fumarases with altered conformations that are targeted to mitochondria but have lost their ability to be distributed, (ii) show by employing mass spectrometry that mature cytosolic and mitochondrial fumarase isoenzymes are identical, and (iii) show that Hsp70 chaperones in the cytosol (Ssa) and mitochondria (Ssc1) can affect fumarase distribution. The results are discussed in light of our model of targeting and distribution, that suggests that rapid folding of fumarase into an import incompetent state, provides the driving force for retrograde movement of the processed protein back to the cytosol through the translocation pore.


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