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Alterations in the cleavage site of the signal sequence for the secretion of human lysozyme by Saccharomyces cerevisiae
Author(s) -
Nagahora Hitoshi,
Fujisawa Hirofumi,
Jigami Yoshifumi
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80506-4
Subject(s) - lysozyme , signal peptide , cleavage (geology) , saccharomyces cerevisiae , biochemistry , yeast , secretion , biology , mutant , signal peptidase , chemistry , peptide sequence , gene , paleontology , fracture (geology)
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.