Details
| Original language | English |
|---|---|
| Article number | 148443 |
| Journal | Biochimica et Biophysica Acta - Bioenergetics |
| Volume | 1862 |
| Issue number | 8 |
| Early online date | 6 May 2021 |
| Publication status | Published - 1 Aug 2021 |
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.
Keywords
- Diurnal cycle, Oxidative phosphorylation, Plant mitochondria, Post-translational modifications, Protein:Protein interactions, TCA-cycle
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1862, No. 8, 148443, 01.08.2021.
Research output: Contribution to journal › Article › Research › peer review
}
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 -