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J. Biol. Chem., Vol. 277, Issue 46, 43792-43798, November 15, 2002

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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^**

From the  Institute of Biochemistry and Molecular Biology, University of Wroclaw, Tamka 2, Wroclaw 50-137, Poland, the ^§ Department of Plant Biology, Swedish University of Agricultural Sciences, Box 7080, Uppsala S-750 07, Sweden, and the ^¶ Department of Biology, Brookhaven National Laboratory, Upton, New York 11973

Mitochondrial AAA metalloproteases play a fundamental role in 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 matrix AAA (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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