Premium
COQ9 Membrane Association and Its Role in Coenzyme Q Biosynthesis
Author(s) -
Von Bank Helaina C.,
Lohman Danielle C.,
Aydin Deniz,
Smith Robert,
Bingman Craig,
Peraro Matteo Dal,
Pagliarini David J.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.815.8
Subject(s) - cofactor , biochemistry , coenzyme q – cytochrome c reductase , inner mitochondrial membrane , coenzyme a , biosynthesis , membrane protein , biology , mitochondrion , membrane , chemistry , gene , enzyme , cytochrome c , reductase
Coenzyme Q is a ubiquitous and hydrophobic lipid essential in cellular respiration. The de novo eukaryotic synthesis of coenzyme Q involves at least nine different proteins (COQ1–9), several of which have undiscovered functions. Many of these proteins are peripherally associated with the inner mitochondrial membrane as part of the biosynthetic complex Q. How these proteins bind the membrane and interact with coenzyme Q lipid intermediates remains unresolved. Filling these gaps in knowledge provides potential for improving the treatment of diseases associated with Coenzyme Q deficiency, such as Parkinson's disease and cardiomyopathy. Recently, we discovered that one member of complex Q, COQ9, can associate with mitochondrial membrane lipids. Our biochemical, crystallographic, and computational data reveal that a structurally unique amphipathic helix of COQ9 drives membrane association. Collectively, this work provides mechanistic insight into how a lipid‐binding protein associates with biological membranes and has important implications toward understanding its role in coenzyme Q biosynthesis. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .