Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/101878
Title: Mitochondrial ferredoxin-like is essential for forming complex I-containing supercomplexes in Arabidopsis
Author(s): Röhricht, Helene
Przybyla-Toscano, Jonathan
Forner, JoachimLook up in the Integrated Authority File of the German National Library
Boussardon, Clément
Keech, Olivier
Rouhier, Nicolas
Meyer, Etienne H.
Issue Date: 2023
Type: Article
Language: English
Abstract: In eukaryotes, mitochondrial ATP is mainly produced by the oxidative phosphorylation (OXPHOS) system, which is composed of 5 multiprotein complexes (complexes I–V). Analyses of the OXPHOS system by native gel electrophoresis have revealed an organization of OXPHOS complexes into supercomplexes, but their roles and assembly pathways remain unclear. In this study, we characterized an atypical mitochondrial ferredoxin (mitochondrial ferredoxin-like, mFDX-like). This protein was previously found to be part of the bridge domain linking the matrix and membrane arms of the complex I. Phylogenetic analysis suggested that the Arabidopsis (Arabidopsis thaliana) mFDX-like evolved from classical mitochondrial ferredoxins (mFDXs) but lost one of the cysteines required for the coordination of the iron-sulfur (Fe-S) cluster, supposedly essential for the electron transfer function of FDXs. Accordingly, our biochemical study showed that AtmFDX-like does not bind an Fe-S cluster and is therefore unlikely to be involved in electron transfer reactions. To study the function of mFDX-like, we created deletion lines in Arabidopsis using a CRISPR/Cas9-based strategy. These lines did not show any abnormal phenotype under standard growth conditions. However, the characterization of the OXPHOS system demonstrated that mFDX-like is important for the assembly of complex I and essential for the formation of complex I-containing supercomplexes. We propose that mFDX-like and the bridge domain are required for the correct conformation of the membrane arm of complex I that is essential for the association of complex I with complex III2 to form supercomplexes.
URI: https://opendata.uni-halle.de//handle/1981185920/103829
http://dx.doi.org/10.25673/101878
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Journal Title: Plant physiology
Publisher: Oxford University Press
Publisher Place: Oxford
Volume: 191
Issue: 4
Original Publication: 10.1093/plphys/kiad040
Page Start: 2170
Page End: 2184
Appears in Collections:Open Access Publikationen der MLU

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