A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
J. Clin. Invest. Isla Ogilvie, et al. 115:2784 doi:10.1172/JCI26020 [
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Figure 2Mitochondrial localization and tissue-specific expression of B17.2L. (
A) HEK293 cells were transfected with a vector expressing a B17.2L-GFP fusion protein, stained with MitoTracker red (a mitochondrial marker), and viewed on a fluorescence microscope. The overlay of the 2 images shows complete superposition of the 2 markers, demonstrating the mitochondrial localization of B17.2L. (
B) Immunoblot analysis of B17.2L in human tissues. An anti-B17.2L antibody was used to measure the steady-state levels of B17.2L in normal human fibroblasts (F), heart (H), skeletal muscle (M), and liver (L) by immunoblot analysis. Porin, an outer mitochondrial membrane protein, and the 49-kDa structural subunit of complex I are shown for comparison.
