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RSS FeedsIJMS, Vol. 18, Pages 2455: Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach (International Journal of Molecular Sciences)

 
 

18 november 2017 12:50:55

 
IJMS, Vol. 18, Pages 2455: Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach (International Journal of Molecular Sciences)
 


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.


 
111 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
IJMS, Vol. 18, Pages 2458: Cellular Localization of Wheat High Molecular Weight Glutenin Subunits in Transgenic Rice Grain (International Journal of Molecular Sciences)
IJMS, Vol. 18, Pages 2453: In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom (International Journal of Molecular Sciences)
 
 
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