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• W2103131657 endingPage "1505" @default.
• W2103131657 startingPage "1499" @default.
• W2103131657 abstract "Recently, we fused a matrix-targeting signal to a large fragment of vesicular stomatitis virus G protein, which contains near its COOH-terminus a well-characterized endoplasmic reticulum (ER) stop-transfer sequence; the hybrid G protein was sorted to the inner mitochondrial membrane (Nguyen, M., and G. C. Shore. 1987. J. Biol. Chem. 262:3929-3931). Here, we show that the 19 amino acid G stop-transfer domain functions in an identical fashion when inserted toward the COOH-terminus of an otherwise normal matrix precursor protein, pre-ornithine carbamyl transferase; after import, the mutant protein was found anchored in the inner membrane via the stop-transfer sequence, with its NH2 terminus facing the matrix and its short COOH-terminal tail located in the intermembrane space. However, when the G stop-transfer sequence was placed near the NH2 terminus, the protein was inserted into the outer membrane, in the reverse orientation (NH2 terminus facing out, with a large COOH-terminal fragment located in the intermembrane space). These observations for mitochondrial topogenesis can be explained by a simple extension of existing models for ER sorting." @default.
• W2103131657 created "2016-06-24" @default.
• W2103131657 creator A5007821279 @default.
• W2103131657 creator A5017038349 @default.
• W2103131657 creator A5052520192 @default.
• W2103131657 date "1988-05-01" @default.
• W2103131657 modified "2023-09-24" @default.
• W2103131657 title "Protein sorting between mitochondrial membranes specified by position of the stop-transfer domain." @default.
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• W2103131657 doi "https://doi.org/10.1083/jcb.106.5.1499" @default.
• W2103131657 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2115062" @default.
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• W2103131657 hasPublicationYear "1988" @default.
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