The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria

authored by

Hans-Peter Braun, Udo Schmitz

Abstract

Cytochrome c reductase from potato has been extensively studied with respect to its catalytic activities, its subunit composition, and the biogenesis of individual subunits. Molecular characterization of all 10 subunits revealed that the high-molecular-weight subunits exhibit striking homologies with the components of the general mitochondrial processing peptidase (MPP) from fungi and mammals. Some of the other subunits show differences in the structure of their targeting signals or in their molecular composition when compared to their counterparts from heterotrophic organisms. The proteolytic activity of MPP was found in the cytochrome c reductase complexes from potato, spinach, and wheat, suggesting that the integration of the protease into this respiratory complex is a general feature of higher plants.

External Organisation(s)

Max Planck Institute of Molecular Plant Physiology (MPI-MP)

Type

Article

Journal

Journal of Bioenergetics and Biomembranes

Volume

27

Pages

423-436

No. of pages

14

ISSN

0145-479X

Publication date

08.1995

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Physiology, Cell Biology

Electronic version(s)

https://doi.org/10.1007/BF02110005 (Access: Unknown)