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PLANT PHYSIOLOGY , Vol 104, Issue 4 1221-1229, Copyright © 1994 by American Society of Plant Biologists
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MOLECULAR BIOLOGY AND GENE REGULATION |
The Characterization of a Mitochondrial Acyl Carrier Protein Isoform Isolated from Arabidopsis thaliana
D. K. Shintani and J. B. Ohlrogge
Department of Botany and Plant Pathology, Michigan State University, East Lansing, Michigan 48824
A cDNA clone was isolated from an Arabidopsis leaf cDNA library that shared
a high degree of protein sequence identity with mitochondrial acyl carrier
proteins (mtACPs) isolated from Neurospora crassa and bovine heart muscle.
The cDNA encoded an 88-amino acid mature protein that was preceded by a
putative 35-amino acid presequence. In vitro protein import studies have
confirmed that the presequence specifically targets this protein into pea
mitochondria but not into chloroplasts. These studies indicated that pea
mitochondria were not only able to import and process the precursor protein
but also possessed the ability to acylate the mature protein. The
mitochondrial localization of this protein, mtACP-1, was confirmed by
western blot analysis. Arabidopsis mitochondrial protein extracts contained
two cross-reacting bands that comigrated with the mature mtACP-1 and
acylated mtACP-1 proteins. The acylated form of mtACP-1 was approximately 4
times more abundant than the unacylated form and appeared to be localized
predominantly in the mitochondrial membrane where the unacylated mtACP-1
was present mostly in the matrix fraction. A chloroplast fatty acid
synthase system was used, and mtACP-1 was able to function as a cofactor
for fatty acid synthesis. However, predominantly short- and medium-chain
fatty acids were produced in fatty acid synthase reactions supplemented
with mtACP-1, suggesting that mtACP-1 may be causing premature fatty acid
chain termination.
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