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

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

Externe Organisationen

  • Applied Biosystems GmbH
  • Universitätsklinikum Düsseldorf
  • Max-Planck-Institut für molekulare Pflanzenphysiologie
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)396-402
Seitenumfang7
FachzeitschriftPlanta
Jahrgang195
Ausgabenummer3
PublikationsstatusVeröffentlicht - Jan. 1995
Extern publiziertJa

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.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde

Zitieren

The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain. / Braun, Hans-Peter; Emmermann, Michael; Kruft, Volker et al.
in: Planta, Jahrgang 195, Nr. 3, 01.1995, S. 396-402.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Braun HP, Emmermann M, Kruft V, Bödicker M, Schmitz U. The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain. Planta. 1995 Jan;195(3):396-402. doi: 10.1007/BF00202597
Download
@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",

}

Download

TY - JOUR

T1 - The general mitochondrial processing peptidase from wheat is integrated into the cytochrome bc1-complex of the respiratory chain

AU - Braun, Hans-Peter

AU - Emmermann, Michael

AU - Kruft, Volker

AU - Bödicker, Martin

AU - Schmitz, Udo

PY - 1995/1

Y1 - 1995/1

N2 - 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.

AB - 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.

KW - bc-Complex

KW - Mitochondria

KW - Mitochondrial processing peptidase

KW - Protein import

KW - Respiratory chain

KW - Triticum

UR - http://www.scopus.com/inward/record.url?scp=0029158755&partnerID=8YFLogxK

U2 - 10.1007/BF00202597

DO - 10.1007/BF00202597

M3 - Article

C2 - 7766045

AN - SCOPUS:0029158755

VL - 195

SP - 396

EP - 402

JO - Planta

JF - Planta

SN - 0032-0935

IS - 3

ER -

Von denselben Autoren