Alkhaja AK, Jans DC, Nikolov M, Vukotic M, Lytovchenko O, Ludewig F, Schliebs W, Riedel D, Urlaub H, Jakobs S, Deckers M

The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane but rather ...

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organize into functionally distinct subcompartments. It is currently unknown how the organization of the inner membrane is achieved. We have identified MINOS1/MIO10 (C1orf151/YCL057C-A) a conserved mitochondrial inner membrane protein. mio10 mutant yeast cells are affected in growth on non-fermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1-complexes in human and yeast mitochondria. Thus, our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery.

Date: Nov. 23, 2011

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