TY - JOUR

T1 - Protein interaction patterns in Arabidopsis thaliana leaf mitochondria change in dependence to light

AU - Rugen, Nils

AU - Schaarschmidt, Frank

AU - Eirich, Jürgen

AU - Finkemeier, Iris

AU - Braun, Hans-Peter

AU - Eubel, Holger

N1 - Funding Information: We thank Marianne Langer for expert technical assistance and Michael Senkler for most helpful IT support. We also thank Mareike Schallenberg-Rüdinger and Etienne Meyer for critically reading and discussing the manuscript. This work is founded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) within the framework of PAK918 and the project numbers EU 54/4-1 for HE, and FI1655/3-1 for IF.

PY - 2021/8/1

Y1 - 2021/8/1

N2 - 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.

AB - 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.

KW - Diurnal cycle

KW - Oxidative phosphorylation

KW - Plant mitochondria

KW - Post-translational modifications

KW - Protein:Protein interactions

KW - TCA-cycle

UR - http://www.scopus.com/inward/record.url?scp=85106295151&partnerID=8YFLogxK

U2 - 10.1016/j.bbabio.2021.148443

DO - 10.1016/j.bbabio.2021.148443

M3 - Article

C2 - 33965424

VL - 1862

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 8

M1 - 148443

ER -