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• W2072694199 abstract "Many biological processes require proteins to undergo conformational changes at the surface of membranes. For example, some precursor proteins unfold at the surface of mitochondria and chloroplasts before translocation into the organelles, and toxins such as colicin A unfold to the molten globule state at bacterial surfaces before inserting into the cell membrane. It is commonly thought that the membrane surfaces and the associated protein machinery destabilize the substrate proteins and that this effect is required for membrane insertion or translocation. One of the best characterized translocation processes is protein import into mitochondria. By measuring the contributions of individual interactions within a model protein to its stability at the mitochondrial surface and in free solution, we show here that the mitochondrial surface neither induces the molten globule state in this protein nor preferentially destabilizes any type of interaction (e.g., hydrogen bonds, nonpolar, etc.) within the protein. Because it is not possible to measure absolute protein stability at the surface of mitochondria, we determined the stability of a tightly associated protein–protein complex at the mitochondrial import site as a model of the stability of a protein. We found the binding constants of the protein–protein complex at the mitochondrial surface and in free solution to be identical. Our results demonstrate that the mitochondrial surface does not destabilize importing precursor proteins in its vicinity." @default.
• W2072694199 created "2016-06-24" @default.
• W2072694199 creator A5047553318 @default.
• W2072694199 creator A5049009587 @default.
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• W2072694199 date "2000-11-07" @default.
• W2072694199 modified "2023-09-23" @default.
• W2072694199 title "Effect of the protein import machinery at the mitochondrial surface on precursor stability" @default.
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• W2072694199 doi "https://doi.org/10.1073/pnas.230243097" @default.
• W2072694199 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/27166" @default.
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