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Reference: Folsch H, et al. (1996) Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria. EMBO J 15(3):479-87

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Abstract


The BCS1 protein is anchored in the mitochondrial inner membrane via a single transmembrane domain and has an N(out)-C(in) topology. Unlike the majority of nuclear encoded mitochondrial preproteins, the BCS1 protein does not contain an N-terminal targeting sequence. A positively charged segment of amino acids which is located immediately C-terminal to the transmembrane domain acts as an internal targeting signal. In order to function, we postulate that this sequence co-operates with the transmembrane domain to form a tight hairpin loop structure. This loop is translocated across the inner membrane via the MIM/mt-Hsp70 machinery in a membrane potential-dependent manner. This novel mechanism of import and sorting of the BCS1 protein is proposed to represent a more general mechanism used by a number of inner membrane proteins.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Folsch H, Guiard B, Neupert W, Stuart RA
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