Alterations in the cleavage site of the signal sequence for the secretion of human lysozyme by Saccharomyces cerevisiae.
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.
D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins; D009113:Muramidase / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D011498:Protein Precursors / Q000378:metabolism; D021382:Protein Sorting Signals / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D012697:Serine Endopeptidases; D013379:Substrate Specificity; D014170:Transformation, Genetic
D008565:Membrane Proteins; D011498:Protein Precursors; D021382:Protein Sorting Signals; D009113:Muramidase; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase