A mitochondrial membrane protein forms a large oligomeric complex that affects the abundance of complex I and respiratory supercomplexes. Stomatins belong to the band-7 protein family, a diverse group of conserved eukaryotic and prokaryotic membrane proteins involved in the formation of large protein complexes as protein-lipid scaffolds. The Arabidopsis (Arabidopsis thaliana) genome contains two paralogous genes encoding stomatin-like proteins (SLPs; AtSLP1 and AtSLP2) that are phylogenetically related to human SLP2, a protein involved in mitochondrial fusion and protein complex formation in the mitochondrial inner membrane. We used reverse genetics in combination with biochemical methods to investigate the function of AtSLPs. We demonstrate that both SLPs localize to mitochondrial membranes. SLP1 migrates as a large (approximately 3 MDa) complex in blue-native gel electrophoresis. Remarkably, slp1 knockout mutants have reduced protein and activity levels of complex I and supercomplexes, indicating that SLP affects the assembly and/or stability of these complexes. These findings point to a role for SLP1 in the organization of respiratory supercomplexes in Arabidopsis.
An Arabidopsis Stomatin-Like Protein Affects Mitochondrial Respiratory Supercomplex Organization1[C][W][OPEN]
B. Gehl,Chun-Pong Lee,Pedro Bota,M. Blatt,L. Sweetlove
Published 2014 in Plant Physiology
ABSTRACT
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- Publication year
2014
- Venue
Plant Physiology
- Publication date
2014-01-14
- Fields of study
Biology, Medicine, Environmental Science
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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