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

FEBS Letters

Nagahora, Hitoshi¹  Fujisawa, Hirofumi¹  Jigami, Yoshifumi¹ 

[1] Bioorganic Chemistry Division, National Chemical Laboratory for Industry, Higashi 1-1, Tsukuba, Ibaraki 305, Japan

关键词: Signal peptidase;    Yeast;    Cleavage site;    Lysozyme signal;    (Chicken);    HLY;    human lysozyme;    CLY;    chicken lysozyme;    aa;    amino acid;    preHLY;    precursor HLY;   

DOI  :  10.1016/0014-5793(88)80506-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown