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. Author manuscript; available in PMC: 2018 Jul 19.
Published in final edited form as: Science. 2018 Jan 19;359(6373):eaah6834. doi: 10.1126/science.aah6834

Fig. 4. Interaction of Sam50 with the N-terminal β-strand of precursor proteins.

Fig. 4

(A) [35S]Por1(β14-19) precursors containing a single cysteine residue as indicated were imported into mitochondria isolated from yeast strains expressing the indicated Sam50 cysteine variants, followed by oxidation with 4-DPS, non-reducing SDS-PAGE and autoradiography. Black and white arrowheads, cysteine-specific disulfide-bonded Por1(β14-19) adducts to the C-terminal and N-terminal β-strand of Sam50, respectively. Right, schematic models. (B) [35S]Por1(β14-19)C206 and [35S]Por1(β14-19)C204 were treated as described in (A). (C) [35S]Por1(β14-19) single and double cysteine variants were incubated with isolated mitochondria from yeast strains expressing Sam50Cfree or the double cysteine variant Sam50C126/C480, followed by oxidation with 4-DPS. Samples were analyzed as described in (A).