Alterations in the cleavage site of the signal sequence for the secretion of human lysozyme by Saccharomyces cerevisiae

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Abstract
The amino acids corresponding to the cleavage site of a hybrid preprotein containing a chicken lysozyme signal and a mature portion of human lysozyme were altered. The processing of mutant signals of −3Pro and −3Asp/−1Ala decreased remarkably, while that of −2Pro was 75% of that of the native signal. The major cleavage site of −3Pro was the same as that of the native signal, but that of the −2Pro and −3Asp/−1Ala signals was shifted one residue closer to the N‐terminal side than the original site. The cleavage of the −2Pro signal, which was identical to the native processing of pheasant prelysozyme, suggested that the signal peptidases in yeast and bird are similar.