New insights into the co-evolution of cytochrome c reductase and the mitochondrial processing peptidase

authored by: Stefanie Brumme, Volker Kruft, Udo Schmitz, Hans-Peter Braun
Abstract: The mitochondrial processing peptidase (MPP) is a heterodimeric enzyme that forms part of the cytochrome c reductase complex from higher plants. Mitochondria from mammals and yeast contain two homologous enzymes: (i) an active MPP within the mitochondrial matrix and (ii) an inactive MPP within the cytochrome c reductase complex. To elucidate the evolution of MPP, the cytochrome c reductase complexes from lower plants were isolated and tested for processing activity. Mitochondria were prepared from the staghorn fern Platycerium bifurcatum, from the horsetail Equisetum arvense, and from the colorless algae Polytomella, and cytochrome c reductase complexes were purified by a micro-isolation procedure based on Blue-native polyacrylamide gel electrophoresis and electroelution. This is the first report on the subunit composition of a respiratory enzyme complex from a fern or a horsetail. The cytochrome c reductase complexes from P. bifurcatum and E. arvense are shown to efficiently process mitochondrial precursor proteins, whereas the enzyme complex from Polytomella lacks proteolytic activity. An evolutionary model is suggested that assumes a correlation between the presence of an active MPP within the cytochrome c reductase complex and the occurrence of chloroplasts.
Organisation(s): Section Plant Molecular Biology and Plant Proteomics
External Organisation(s): Applied Biosystems GmbH
Type: Article
Journal: Journal of Biological Chemistry
Volume: 273
Pages: 13143-13149
No. of pages: 7
ISSN: 0021-9258
Publication date: 22.05.1998
Publication status: Published
Peer reviewed: Yes
ASJC Scopus subject areas: Biochemistry, Molecular Biology, Cell Biology
Electronic version(s): https://doi.org/10.1074/jbc.273.21.13143 (Access: Open)
https://doi.org/10.15488/11694 (Access: Open)