Protein interaction patterns in Arabidopsis thaliana leaf mitochondria change in dependence to light

authored by

Nils Rugen, Frank Schaarschmidt, Jürgen Eirich, Iris Finkemeier, Hans-Peter Braun, Holger Eubel

Abstract

Mitochondrial biology is underpinned by the presence and activity of large protein assemblies participating in the organelle-located steps of respiration, TCA-cycle, glycine oxidation, and oxidative phosphorylation. While the enzymatic roles of these complexes are undisputed, little is known about the interactions of the subunits beyond their presence in these protein complexes and their functions in regulating mitochondrial metabolism. By applying one of the most important regulatory cues for plant metabolism, the presence or absence of light, we here assess changes in the composition and molecular mass of protein assemblies involved in NADH-production in the mitochondrial matrix and in oxidative phosphorylation by employing a differential complexome profiling strategy. Covering a mass up to 25 MDa, we demonstrate dynamic associations of matrix enzymes and of components involved in oxidative phosphorylation. The data presented here form the basis for future studies aiming to advance our understanding of the role of protein:protein interactions in regulating plant mitochondrial functions.

Organisation(s)

Institute of Plant Genetics
Institute of Cell Biology and Biophysics

External Organisation(s)

University of Münster

Type

Article

Journal

Biochimica et Biophysica Acta - Bioenergetics

Volume

1862

ISSN

0005-2728

Publication date

01.08.2021

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Biophysics, Biochemistry, Cell Biology

Electronic version(s)

https://doi.org/10.1016/j.bbabio.2021.148443 (Access: Closed)