An Arabidopsis Stomatin-Like Protein Affects Mitochondrial Respiratory Supercomplex Organization
Author(s) -
Bernadette Gehl,
Chun Pong Lee,
Pedro Bota,
Michael R. Blatt,
Lee Sweetlove
Publication year - 2014
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.113.230383
Subject(s) - arabidopsis , biology , arabidopsis thaliana , membrane protein , mitochondrion , mutant , inner mitochondrial membrane , respiratory chain , mitochondrial dna , microbiology and biotechnology , gene , biochemistry , protein family , mitochondrial membrane transport protein , membrane
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.
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