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- W2136106871 abstract "Hydrophobic stop-transfer sequences generally serve to halt the translocation of polypeptide chains across the endoplasmic reticulum membrane and become integrated as transmembrane alpha-helices. Using engineered glycosylation sites as topology reporters, we show that the length of the nascent chain between a hydrophobic segment and the carboxy terminus of the protein can affect stop-transfer efficiency. We also show that glycosylation sites located close to a protein's C terminus are modified in two distinct kinetic phases, one fast and one slow. Our findings suggest that membrane integration of a hydrophobic segment is not simply a question of thermodynamic equilibrium, but can be influenced by details of the translocation mechanism." @default.
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- W2136106871 date "2003-02-01" @default.
- W2136106871 modified "2023-10-09" @default.
- W2136106871 title "Stop‐transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy‐terminal tail" @default.
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- W2136106871 doi "https://doi.org/10.1038/sj.embor.embor728" @default.
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