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• W2068611282 abstract "To get insight into the insertion mechanism of small newly synthesized single-spanning membrane proteins, Pf3 coat protein mutants were constructed with potential glycosylation sites in the N-terminus. Some of these proteins, when synthesized in vitro in the presence of microsomes, became efficiently glycosylated, proving that they insert into the membrane and translocate their N-terminus to the lumenal side. Such Pf3 constructs also insert efficiently into Escherichia coli vesicles and even in pure lipid vesicles, suggesting a common mechanism, which might be spontaneous. Glycosylation was sensitive to changes in the amino acid sequence of the N-terminus, suggesting that it depends on the structure of the protein and/or its positioning with respect to the lipid-water interface." @default.
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• W2068611282 date "2002-01-25" @default.
• W2068611282 modified "2023-09-23" @default.
• W2068611282 title "Insertion and glycosylation of Pf3-derived membrane proteins in microsomes" @default.
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• W2068611282 doi "https://doi.org/10.1016/s0014-5793(02)02312-8" @default.
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