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- W1520794681 abstract "Leader peptidase (Lep) is a membrane-bound enzyme of the Escherichia coli inner membrane that serves to remove signal peptides from exported proteins. Statistical and experimental studies of known signal peptides have defined a short C-terminal region that seems to provide the information for correct by Lep. Based on the patterns of conserved amino acids found in this region, we have designed a signal peptide cleavage cassette. This cassette is processed at the expected site when introduced after an uncleaved signal peptide. Furthermore, processing is blocked in the predicted manner when the (-3, -1)-rule for signal peptide is violated. This suggests that current understanding of the sequence requirements for signal peptide is sufficiently advanced to be used in, e.g. protein engineering applications." @default.
- W1520794681 created "2016-06-24" @default.
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- W1520794681 date "1991-02-01" @default.
- W1520794681 modified "2023-09-30" @default.
- W1520794681 title "A de novo designed signal peptide cleavage cassette functions in vivo" @default.
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- W1520794681 doi "https://doi.org/10.1016/s0021-9258(19)67808-7" @default.
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