Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail |
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Authors: | Hessa Tara Monné Magnus von Heijne Gunnar |
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Affiliation: | Tara Hessa, Magnus Monné, and Gunnar von Heijne |
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Abstract: | Hydrophobic stop-transfer sequences generally serve to halt the translocation of polypeptide chains across the endoplasmic reticulum membrane and become integrated as transmembrane α-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. |
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