Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain.
Mitochondrial maintenance crucially depends on the quality control of proteins by various chaperones, proteases and repair enzymes. While most of the involved components have been studied in some detail, little is known on the biological role of the CLPXP protease complex located in the mitochondrial matrix. Here we show that deletion of PaClpP, encoding the CLP protease proteolytic subunit CLPP, leads to an unexpected healthy phenotype and increased lifespan of the fungal ageing model organism Podospora anserina. This phenotype can be reverted by expression of human ClpP in the fungal deletion background, demonstrating functional conservation of human and fungal CLPP. Our results show that the biological role of eukaryotic CLP proteases can be studied in an experimentally accessible model organism.
Johann Wolfgang Goethe University, Faculty for Biosciences & Cluster of Excellence, Macromolecular Complexes Frankfurt, Institute of Molecular Biosciences, Max-von-Laue-Straße 9, 60438 Frankfurt, Germany.
Fabian
F
Fischer
Andrea
A
Weil
Andrea
A
Hamann
Heinz D
HD
Osiewacz
D015153:Blotting, Western; D019295:Computational Biology; D049071:Endopeptidase Clp / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins; D017353:Gene Deletion; D005816:Genetic Complementation Test; D006801:Humans; D024101:Mitochondrial Proteins / Q000378:metabolism; D010641:Phenotype; D048468:Podospora / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development*; D049070:Protease La / Q000378:metabolism; D013696:Temperature
D005656:Fungal Proteins; D024101:Mitochondrial Proteins; D049070:Protease La; C568646:ClpP protein, human; D049071:Endopeptidase Clp