Membrane protein turnover by the m-AAA protease in mitochondria depends on the 
transmembrane domains of its subunits

Korbel, D.; Wurth, S.; Kaser, M.; Langer, T.

doi:10.1038/sj.embor.7400186

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Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits

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Langer, T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/15205678
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Citation

Korbel, D., Wurth, S., Kaser, M., & Langer, T. (2004). Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits. EMBO Rep, 5(7), 698-703. doi:10.1038/sj.embor.7400186.

Cite as: https://hdl.handle.net/21.11116/0000-000B-71EF-9

Abstract

AAA proteases are membrane-bound ATP-dependent proteases that are present in eubacteria, mitochondria and chloroplasts and that can degrade membrane proteins. Recent evidence suggests dislocation of membrane-embedded substrates for proteolysis to occur in a hydrophilic environment; however, next to nothing is known about the mechanism of this process. Here, we have analysed the role of the membrane-spanning domains of Yta10 and Yta12, which are conserved subunits of the hetero-oligomeric m-AAA protease in the mitochondria of Saccharomyces cerevisiae. We demonstrate that the m-AAA protease retains proteolytic activity after deletion of the transmembrane segments of either Yta10 or Yta12. Although the mutant m-AAA protease is still capable of processing cytochrome c peroxidase and degrading a peripheral membrane protein, proteolysis of integral membrane proteins is impaired. We therefore propose that transmembrane segments of m-AAA protease subunits have a direct role in the dislocation of membrane-embedded substrates.