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Fölsch, H, Guiard, B, Neupert, W and Stuart, RA (1996) Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria. EMBO J. 15:479-87
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.
Amino Acid Sequence; Base Sequence; Biological Transport, Active; Cloning, Molecular; DNA Primers/genetics; DNA, Fungal/genetics; Intracellular Membranes/metabolism; Membrane Proteins; Mitochondria/metabolism; Mitochondrial Proteins; Models, Biological; Molecular Chaperones; Molecular Sequence Data; Molecular Structure; Protein Sorting Signals/genetics; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins
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