title: The planti-AAA protease controls the turnover of an essential mitochondrial protein import component.
abstract: Mitochondria are multifunctional organelles that play a central role in energy metabolism. Owing to the life-essential functions of these organelles, mitochondrial content, quality and dynamics are tightly controlled. Across the species, highly conserved ATP-dependent proteases prevent malfunction of mitochondria through versatile activities. This study focuses on a molecular function of the plant mitochondrial inner membrane-embedded AAA protease (denotedi-AAA) FTSH4, providing its first bona fide substrate. Here, we report that the abundance of the Tim17-2 protein, an essential component of the TIM17:23 translocase (Tim17-2 together with Tim50 and Tim23), is directly controlled by the proteolytic activity of FTSH4. Plants that are lacking functional FTSH4 protease are characterized by significantly enhanced capacity of preprotein import through the TIM17:23-dependent pathway. Taken together, with the observation that FTSH4 prevents accumulation of Tim17-2, our data point towards the role of thisi-AAA protease in the regulation of mitochondrial biogenesis in plants.
authors.affiliation: Faculty of Biotechnology, University of Wroclaw, F. Joliot-Curie 14A, Wroclaw 50-383, Poland magdalena.opalinska@uwr.edu.pl hanna.janska@uwr.edu.pl.
authors.forename: Magdalena
authors.identifier: 0000-0003-1449-4243
authors.initials: M
authors.lastname: Opalińska
authors.affiliation: Faculty of Biotechnology, University of Wroclaw, F. Joliot-Curie 14A, Wroclaw 50-383, Poland.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Parys
authors.affiliation: Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, 35 Stirling Highway, Crawley Western Australia 6009, Australia.|School of Molecular Sciences, University of Western Australia, 35 Stirling Highway, Crawley, Western Australia 6009, Australia.
authors.forename: Monika W
authors.initials: MW
authors.lastname: Murcha
authors.affiliation: Faculty of Biotechnology, University of Wroclaw, F. Joliot-Curie 14A, Wroclaw 50-383, Poland magdalena.opalinska@uwr.edu.pl hanna.janska@uwr.edu.pl.
authors.forename: Hanna
authors.initials: H
authors.lastname: Jańska
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities / Q000378:metabolism*; D017360:Arabidopsis / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D045726:Metalloproteases / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism; D033681:Mitochondrial Membrane Transport Proteins / Q000378:metabolism*; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; D008970:Molecular Weight; D009154:Mutation / Q000235:genetics; D021381:Protein Transport; D059748:Proteolysis
chemical_list: D029681:Arabidopsis Proteins; D026901:Membrane Transport Proteins; D033681:Mitochondrial Membrane Transport Proteins; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; C501430:TIM17 protein, Arabidopsis; C506771:FtsH4 protein, Arabidopsis; D045726:Metalloproteases; D000074183:ATPases Associated with Diverse Cellular Activities
keywords: AAA protease; ATP-dependent proteolysis; Mitochondrial protein import; TIM17:23 translocase