Multiple proteins with essential mitochondrial functions have glycosylated isoforms.

Nucleocytosolic and secreted proteins are commonly glycosylated. However, reports of glycosylated mitochondrial proteins are rare. Using lectin chromatography on bovine heart, we detected low-abundance glycoforms of nuclear-encoded proteins with well-established mitochondrial function: pyruvate dehydrogenase E1α, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, ADP/ATP translocase, ATP synthase d and oligomycin sensitivity-conferring protein. Notably, the latter two have been previously detected at the plasma membrane. Our findings indicate that glycosylation of classic mitochondrial proteins may be more common than previously appreciated. We discuss the implication that glycosylation could represent an unexplored mechanism for regulating these proteins' functions within mitochondria or at extra-mitochondrial locations.