Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato

verfasst von

Jelle B. Bultema, Hans Peter Braun, Egbert J. Boekema, Roman Kouřil

Abstract

The individual protein complexes of the oxidative phosphorylation system (OXPHOS complexes I to V) specifically interact and form defined supramolecular structures, the so-called "respiratory supercomplexes". Some supercomplexes appear to associate into larger structures, or megacomplexes, such as a string of dimeric ATP synthase (complex V₂). A row-like organization of OXPHOS complexes I, III and IV into respiratory strings has also been proposed. These transient strings cannot be purified after detergent solubilization. Hence the shape and composition of the respiratory string was approached by an extensive structural characterization of all its possible building blocks, which are the supercomplexes. About 400,000 molecular projections of supercomplexes from potato mitochondria were processed by single particle electron microscopy. We obtained two-dimensional projection maps of at least five different supercomplexes, including the supercomplex I + III₂, III₂ + IV₁, V₂, I + III₂ + IV₁ and I₂ + III₂ in different types of position. From these maps the relative position of the individual complexes in the largest unit, the I₂ + III₂ + IV₂ supercomplex, could be determined in a coherent way. The maps also show that the I + III₂ + IV₁ supercomplex, or respirasome, differs from its counterpart in bovine mitochondria. The new structural features allow us to propose a consistent model of the respiratory string, composed of repeating I₂ + III₂ + IV₂ units, which is in agreement with dimensions observed in former freeze-fracture electron microscopy data.

Organisationseinheit(en)

Institut für Pflanzengenetik

Externe Organisation(en)

Reichsuniversität Groningen

Typ

Artikel

Journal

Biochimica et Biophysica Acta - Bioenergetics

Band

1787

Seiten

60-67

Anzahl der Seiten

8

ISSN

0005-2728

Publikationsdatum

13.11.2008

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Biophysik, Biochemie, Zellbiologie

Elektronische Version(en)

https://doi.org/10.1016/j.bbabio.2008.10.010 (Zugang: Offen)