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. 2001 Feb 19;152(4):683–692. doi: 10.1083/jcb.152.4.683

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© 2001 The Rockefeller University Press

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Insertion of a linker between the transmembrane segments of Fzo1 relieves its association with the inner membrane. (A) A mutant version of Fzo1, Fzo1-2, was constructed by insertion of a linker sequence between the transmembrane segments (TM). Depicted is the topology of the mutant protein and the amino acid sequence of the intermembrane space segment. (B) Topology of the Fzo1-2 protein. Mitochondria harboring the Fzo1-2 mutant protein were analyzed as in the legend to Fig. 1 B. (C) Complex assembly of the Fzo1-2 protein. A Triton X-100 extract of fzo1-2 mitochondria was loaded on a Superose-6 column. Fractions were collected and analyzed by immunoblotting and densitometry scanning. The elution peaks and molecular masses of marker proteins are indicated (Hsp60, 850 kD; apoferritin, 440 kD; ADH, 150 kD). (D) Submitochondrial localization of the Fzo1-2 protein. fzo1-2 mitochondria were subfractionated and analyzed as in the legend to Fig. 3 A.