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(Received for publication, July 11, 1995; and in revised form, August 23,
1995) Most mitochondrial precursor proteins are processed to the
mature form in one step by mitochondrial processing peptidase (MPP),
while a subset of precursors destined for the matrix or the inner
membrane are cleaved sequentially by MPP and mitochondrial intermediate
peptidase (MIP). We showed previously that yeast MIP (YMIP) is required
for mitochondrial function in Saccharomyces cerevisiae. To
further define the role played by two-step processing in mitochondrial
biogenesis, we have now characterized the natural substrates of YMIP. A
total of 133 known yeast mitochondrial precursors were collected from
the literature and analyzed for the presence of the motif
RX(
Volume 270,
Number 45,
Issue of November 10, 1995 pp. 27366-27373
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
)(F/L/I)XX(T/S/G)XXXX(
),
typical of precursors cleaved by MPP and MIP. We found characteristic
MIP cleavage sites in two distinct sets of proteins: respiratory
components, including subunits of the electron transport chain and
tricarboxylic acid cycle enzymes, and components of the mitochondrial
genetic machinery, including ribosomal proteins, translation factors,
and proteins required for mitochondrial DNA metabolism. Representative
precursors from both sets were cleaved to predominantly mature form by
mitochondrial matrix or intact mitochondria from wild-type yeast. In
contrast, intermediate-size forms were accumulated upon incubation of
the precursors with matrix from mip1
yeast or intact
mitochondria from mip1 yeast,
indicating that YMIP is necessary for maturation of these proteins.
Consistent with the fact that some of these substrates are essential
for the maintenance of mitochondrial protein synthesis and
mitochondrial DNA replication, mip1
yeast undergoes loss
of functional mitochondrial genomes.
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