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A more recent version of this article appeared on November 8, 2002
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M203831200v1
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Papers In Press, published online ahead of print September 11, 2002
J. Biol. Chem, 10.1074/jbc.M203831200
Submitted on April 19, 2002
Revised on September 9, 2002
Accepted on September 11, 2002

A higher plant mitochondrial homologue of the yeast m-AAA protease: molecular cloning, localization and putative function

Marta Kolodziejczak, Anna Kolaczkowska, Bartosz Szczesny, Adam Urantowka, Carina Knorpp, Jan Kieleczawa, and Hanna Janska

Institute of Biochemistry and Molecular Biology, University of Wroclaw, Wroclaw 50-137

Corresponding Author: janska{at}bf.uni.wroc.pl

Mitochondrial AAA metalloproteases play a fundamental role in the mitochondrial biogenesis and function. They have been identified in yeast and animals, but not yet in plants. This work describes the isolation and sequence analysis of the full-length cDNA from the pea (Pisum sativum) with significant homology to the yeast m-AAA protease. The product of this clone was imported into isolated pea mitochondria where it was processed to its mature form (PsFtsH). We have shown that the central region of PsFtsH containing the chaperone domain is exposed to the matrix space. Furthermore, we have demonstrated that the pea protease can complement respiration deficiency in the yta10 and/or yta12 null yeast mutants, indicating that the plant protein can compensate for the loss of at least some of the important m-AAA functions in yeast. Based on biochemical experiments using isolated pea mitochondria, we propose that PsFtsH like m-AAA is involved in the accumulation of the subunit 9 of the ATP synthase in the mitochondrial membrane.


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