An Arabidopsis Stomatin-Like Protein Affects Mitochondrial Respiratory Supercomplex Organization      . Issue 3 (14th January 2014)

• Record Type: Journal Article
• Authors: Gehl, Bernadette; Lee, Chun Pong; Bota, Pedro; Blatt, Michael R.; Sweetlove, Lee J.
• Is Part Of: Plant physiology. Volume 164:Issue 3(2014)
• Page Start: 1389
• Page End: 1400
• Publication Date: 2014-01-14
• Subjects: Plant physiology -- Periodicals; Botany -- Periodicals; Periodicals; Electronic journals; 571.2
• DOI: 10.1104/pp.113.230383
• Languages: English
• ISSNs: 0032-0889

Abstract

Abstract : A mitochondrial membrane protein forms a large oligomeric complex that affects the abundance of complex I and respiratory supercomplexes . Abstract: 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 (SLP s; 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 SLP s 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.