title: Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing.
abstract: Nuclear encoded mitochondrial precursor proteins are cleaved to mature size products by the general mitochondrial processing peptidase (MPP). In contrast to non-plant sources where MPP is a matrix enzyme, the plant mitochondrial MPP is localised in the inner membrane and constitutes an integral part of the bc1 complex of the respiratory chain. Core proteins of the complex are immunologically related and show high sequence similarity to the MPP subunits from non-plant sources. The bc1 complex in plants is thus bifunctional, being involved both in respiration and in protein processing.
authors.affiliation: Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.
authors.forename: E
authors.initials: E
authors.lastname: Glaser
authors.forename: A
authors.initials: A
authors.lastname: Eriksson
authors.forename: S
authors.initials: S
authors.lastname: Sjöling
mesh_terms: D002384:Catalysis; D002462:Cell Membrane / Q000378:metabolism; D004579:Electron Transport; D014450:Electron Transport Complex III / Q000737:chemistry / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D000096122:Mitochondrial Processing Peptidase
chemical_list: D014450:Electron Transport Complex III; D008666:Metalloendopeptidases; D010940:Plant Proteins; D000096122:Mitochondrial Processing Peptidase