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Volume 272, Number 8, Issue of February 21, 1997 pp. 5320-5325
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Mft52, an Acid-bristle Protein in the Cytosol That Delivers Precursor Proteins to Yeast Mitochondria

(Received for publication, August 20, 1996, and in revised form, December 5, 1996)

Peter Cartwright , Traude Beilharz , Per Hansen , Jinnie Garrett ^§ and Trevor Lithgow

From the  School of Biochemistry, La Trobe University, Bundoora 3083, Australia and ^§ Department of Biology, Hamilton College, Clinton, New York 13323

We have identified a novel protein, Mft52, in the cytosol of yeast cells. Mft52 has a two-domain structure that includes a receptor-like carboxyl-terminal "acid-bristle" domain, which binds basic, amphipathic mitochondrial targeting sequences. Native Mft52, purified from the cytosol of yeast cells, is found as a large particle eluting in the void volume of a Superose 6 gel filtration column. Fusion proteins, consisting of mitochondrial targeting sequences fused to nonmitochondrial passenger proteins, are targeted to mitochondria in wild-type yeast cells, but defects in the gene encoding Mft52 drastically reduce the delivery of these proteins to the mitochondria. We propose that Mft52 is a subunit of a particle that is part of a system of targeting factors and molecular chaperones mediating the earliest stages of protein targeting to the mitochondria.

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