Nagahora H, Fujisawa H, Jigami Y
Bioorganic Chemistry Division, National Chemical Laboratory for Industry, Ibaraki, Japan.
FEBS Lett. 1988 Oct 10;238(2):329-32. doi: 10.1016/0014-5793(88)80506-4.
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.
