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THE PLANT CELL, Vol 2, Issue 12 1249-1260, Copyright © 1990 by American Society of Plant Biologists
A Yeast Mitochondrial Leader Peptide Functions in Vivo as a Dual Targeting Signal for Both Chloroplasts and Mitochondria
J. Huang, E. Hack, R. W. Thornburg and A. M. Myers
Department of Genetics, Iowa State University, Ames, Iowa 50011
A fusion protein was expressed in transgenic tobacco and yeast cells to
examine the functional conservation of mechanisms for importing precursor
proteins from the cytosol into mitochondria and chloroplasts. The test
protein consisted of the mitochondrial leader peptide from the yeast
precursor to cytochrome oxidase subunit Va (prC5) fused to the reporter
protein chloramphenicol acetyltransferase. This protein, denoted prC5/CAT,
was transported into the mitochondrial interior in yeast and tobacco cells.
In both organisms, the mitochondrial form of prC5/CAT was smaller than the
primary translation product, suggesting that proteolytic processing
occurred during the transport process. prC5/CAT also was translocated into
chloroplasts in vivo, accumulating to approximately the same levels as in
plant mitochondria. However, accumulation of prC5/CAT in chloroplasts
relative to mitochondria varied with the conditions under which plants were
grown. The chloroplast form of prC5/CAT also appeared to have been
proteolytically processed, yielding a mature protein of the same apparent
size as that seen in mitochondria of either tobacco or yeast.
Chloramphenicol acetyltransferase lacking a mitochondrial targeting peptide
did not associate with either chloroplasts or mitochondria. The results
demonstrated that in plant cells a single leader peptide can interact
functionally with the protein translocation systems of both chloroplasts
and mitochondria, and raised the possibility that certain native proteins
might be shared between these two organelles.
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