Mitochondria are multifunctional organelles that play a central role in energy metabolism. Due to 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 plant mitochondrial inner membrane-embedded i – AAA protease, FTSH4, providing its first bona fide substrate. Here, we report that the abundance of Tim17-2 protein, the essential component of the TIM17:23 translocase, 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. Together with the observation that FTSH4 prevents accumulation of Tim17-2, our data points towards the role of this i - AAA protease in the regulation of mitochondrial biogenesis in plants.
- Received December 15, 2016.
- Accepted March 1, 2017.
- © 2017. Published by The Company of Biologists Ltd