A higher plant mitochondrial homologue of the yeast m-AAA protease. Molecular cloning, localization, and putative function.
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.
Kolodziejczak
Marta
M
Institute of Biochemistry and Molecular Biology, University of Wroclaw, Tamka 2, Poland.
Kolaczkowska
Anna
A
Szczesny
Bartosz
B
Urantowka
Adam
A
Knorpp
Carina
C
Kieleczawa
Jan
J
Janska
Hanna
H
D025181:ATP Synthetase Complexes / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D029681:Arabidopsis Proteins; D015153:Blotting, Western; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism; D018076:DNA, Complementary / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005816:Genetic Complementation Test; D005990:Glycerol / Q000494:pharmacology; D008666:Metalloendopeptidases / Q000096:biosynthesis* / Q000737:chemistry*; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000201:enzymology; D010940:Plant Proteins / Q000378:metabolism; D014176:Protein Biosynthesis; D017434:Protein Structure, Tertiary; D011510:Proteolipids / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D013997:Time Factors
C063668:ATP9 protein, Arabidopsis; D029681:Arabidopsis Proteins; D018076:DNA, Complementary; D010940:Plant Proteins; D011510:Proteolipids; D000255:Adenosine Triphosphate; D025181:ATP Synthetase Complexes; D008666:Metalloendopeptidases; C114583:m-AAA proteases; D025261:Mitochondrial Proton-Translocating ATPases; D005990:Glycerol