The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc₁-complex of the respiratory chain

verfasst von: Hans-Peter Braun, Michael Emmermann, Volker Kruft, Martin Bödicker, Udo Schmitz
Abstract: The bc₁-complex (EC 1.10.2.2.) from Triticum aestivum L. was purified by cytochrome-c affinity chromatography and gel filtration using either etiolated seedlings or wheat-germ extract as starting material. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the isolated enzyme revealed ten bands, which were analysed by immunoblotting and direct amino-acid sequencing. The enzyme from wheat is the first bc₁-complex that is reported to contain four core proteins (55.5, 55.0, 51.5 and 51.0 kDa). In addition, the wheat bc₁-complex comprises cytochrome b (35 kDa), cytochrome c₁ (33 kDa) the "Rieske" iron-sulphur protein (25 kDa) and three small subunits < 15 kDa. This composition differs from the one reported in fungi, mammals and potato. Partial sequence determination of the large subunits suggests that the 55.5 and 55.0-kDa-proteins represent the β-subunit of the general mitochondrial processing peptidase, and the 51.5 and 51.0-kDa proteins the α-subunit of this enzyme. The bc₁-complex from wheat efficiently processes mitochondrial precursor proteins as shown in an in-vitro processing assay. In control experiments the isolated bc₁-complexes from potato, yeast, Neurospora and beef, all purified by the same isolation procedure, were also tested for processing activity. Only the protein complexes from plants contain the general mitochondrial processing peptidase. The composition of the wheat bc₁-complex sheds new light on the co-evolution of the processing peptidase and the middle segment of the respiratory chain.
Externe Organisation(en): Applied Biosystems GmbH
Universitätsklinikum Düsseldorf
Max-Planck-Institut für molekulare Pflanzenphysiologie
Typ: Artikel
Journal: Planta
Band: 195
Seiten: 396-402
Anzahl der Seiten: 7
ISSN: 0032-0935
Publikationsdatum: 01.1995
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Genetik, Pflanzenkunde
Elektronische Version(en): https://doi.org/10.1007/BF00202597 (Zugang: Unbekannt)

BibTeX

@article{590702f7761e4ea0b0940083d09a7b35,
title = "The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain",
abstract = "The bc1-complex (EC 1.10.2.2.) from Triticum aestivum L. was purified by cytochrome-c affinity chromatography and gel filtration using either etiolated seedlings or wheat-germ extract as starting material. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the isolated enzyme revealed ten bands, which were analysed by immunoblotting and direct amino-acid sequencing. The enzyme from wheat is the first bc1-complex that is reported to contain four core proteins (55.5, 55.0, 51.5 and 51.0 kDa). In addition, the wheat bc1-complex comprises cytochrome b (35 kDa), cytochrome c1 (33 kDa) the {"}Rieske{"} iron-sulphur protein (25 kDa) and three small subunits < 15 kDa. This composition differs from the one reported in fungi, mammals and potato. Partial sequence determination of the large subunits suggests that the 55.5 and 55.0-kDa-proteins represent the β-subunit of the general mitochondrial processing peptidase, and the 51.5 and 51.0-kDa proteins the α-subunit of this enzyme. The bc1-complex from wheat efficiently processes mitochondrial precursor proteins as shown in an in-vitro processing assay. In control experiments the isolated bc1-complexes from potato, yeast, Neurospora and beef, all purified by the same isolation procedure, were also tested for processing activity. Only the protein complexes from plants contain the general mitochondrial processing peptidase. The composition of the wheat bc1-complex sheds new light on the co-evolution of the processing peptidase and the middle segment of the respiratory chain.",
keywords = "bc-Complex, Mitochondria, Mitochondrial processing peptidase, Protein import, Respiratory chain, Triticum",
author = "Hans-Peter Braun and Michael Emmermann and Volker Kruft and Martin B{\"o}dicker and Udo Schmitz",
year = "1995",
month = jan,
doi = "10.1007/BF00202597",
language = "English",
volume = "195",
pages = "396--402",
journal = "Planta",
issn = "0032-0935",
publisher = "Springer Verlag",
number = "3",
}

The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain

The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc₁-complex of the respiratory chain