The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the "-3, -1" rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.
|Original language||English (US)|
|Number of pages||7|
|Publication status||Published - Sep 1997|
- Alkaline phosphatase
- Amino acid substitutions
- E. coli
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