Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach
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 mit...
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2017-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/18/11/2455 |
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doaj-040648cff9c54133b4782d45211386ff2020-11-24T21:18:32ZengMDPI AGInternational Journal of Molecular Sciences1422-00672017-11-011811245510.3390/ijms18112455ijms18112455Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping ApproachMagdalena Opalińska0Katarzyna Parys1Hanna Jańska2Faculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14A, 50-383 Wroclaw, PolandFaculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14A, 50-383 Wroclaw, PolandFaculty of Biotechnology, University of Wroclaw, Fryderyka Joliot-Curie 14A, 50-383 Wroclaw, PolandMaintenance 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.https://www.mdpi.com/1422-0067/18/11/2455AAA proteaseATP-dependent proteolysismitochondriainner mitochondrial membrane proteostasiscarbonylated proteins |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Magdalena Opalińska Katarzyna Parys Hanna Jańska |
| spellingShingle |
Magdalena Opalińska Katarzyna Parys Hanna Jańska Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach International Journal of Molecular Sciences AAA protease ATP-dependent proteolysis mitochondria inner mitochondrial membrane proteostasis carbonylated proteins |
| author_facet |
Magdalena Opalińska Katarzyna Parys Hanna Jańska |
| author_sort |
Magdalena Opalińska |
| title |
Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach |
| title_short |
Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach |
| title_full |
Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach |
| title_fullStr |
Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach |
| title_full_unstemmed |
Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach |
| title_sort |
identification of physiological substrates and binding partners of the plant mitochondrial protease ftsh4 by the trapping approach |
| publisher |
MDPI AG |
| series |
International Journal of Molecular Sciences |
| issn |
1422-0067 |
| publishDate |
2017-11-01 |
| description |
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. |
| topic |
AAA protease ATP-dependent proteolysis mitochondria inner mitochondrial membrane proteostasis carbonylated proteins |
| url |
https://www.mdpi.com/1422-0067/18/11/2455 |
| work_keys_str_mv |
AT magdalenaopalinska identificationofphysiologicalsubstratesandbindingpartnersoftheplantmitochondrialproteaseftsh4bythetrappingapproach AT katarzynaparys identificationofphysiologicalsubstratesandbindingpartnersoftheplantmitochondrialproteaseftsh4bythetrappingapproach AT hannajanska identificationofphysiologicalsubstratesandbindingpartnersoftheplantmitochondrialproteaseftsh4bythetrappingapproach |
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1726008582097338368 |