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Int. J. Mol. Sci. 2017, 18(11), 2455; https://doi.org/10.3390/ijms18112455

Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach

1
Faculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14A, 50-383 Wroclaw, Poland
2
Present address: Gregor Mendel Institute, Austrian Academy of Sciences, Vienna Biocenter, A-1030 Vienna, Austria
*
Authors to whom correspondence should be addressed.
Received: 25 October 2017 / Revised: 14 November 2017 / Accepted: 16 November 2017 / Published: 18 November 2017
(This article belongs to the Special Issue Plant Mitochondria)
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Abstract

Maintenance of functional mitochondria is vital for optimal cell performance and survival. This is accomplished by distinct mechanisms, of which preservation of mitochondrial protein homeostasis fulfills a pivotal role. In plants, inner membrane-embedded i-AAA protease, FTSH4, contributes to the mitochondrial proteome surveillance. Owing to the limited knowledge of FTSH4’s in vivo substrates, very little is known about the pathways and mechanisms directly controlled by this protease. Here, we applied substrate trapping coupled with mass spectrometry-based peptide identification in order to extend the list of FTSH4’s physiological substrates and interaction partners. Our analyses revealed, among several putative targets of FTSH4, novel (mitochondrial pyruvate carrier 4 (MPC4) and Pam18-2) and known (Tim17-2) substrates of this protease. Furthermore, we demonstrate that FTSH4 degrades oxidatively damaged proteins in mitochondria. Our report provides new insights into the function of FTSH4 in the maintenance of plant mitochondrial proteome. View Full-Text
Keywords: AAA protease; ATP-dependent proteolysis; mitochondria; inner mitochondrial membrane proteostasis; carbonylated proteins AAA protease; ATP-dependent proteolysis; mitochondria; inner mitochondrial membrane proteostasis; carbonylated proteins
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Opalińska, M.; Parys, K.; Jańska, H. Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach. Int. J. Mol. Sci. 2017, 18, 2455.

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