Kikuchi M, Kitamoto N, Shishido K
Department of Life Science, Tokyo Institute of Technology, Graduate School of Bioscience and Biotechnology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Appl Microbiol Biotechnol. 2004 Feb;63(6):728-33. doi: 10.1007/s00253-003-1436-y. Epub 2003 Sep 26.
The signal peptide of Aspergillus oryzae endo-(1,4)-beta-xylanase XynF1 contains a C-terminal serine-arginine that directs efficient secretion of the enzyme into the culture medium. In the basidiomycete Coprinus cinereus, however, there is little secretion of XynF1 into the culture medium. Modification of the C-terminal sequence of the signal peptide to lysine-arginine resulted in efficient secretion of C. cinereus XynF1, suggesting the presence of a KEX2-like protease in this fungus.
米曲霉内切(1,4)-β-木聚糖酶XynF1的信号肽含有一个C端丝氨酸-精氨酸,可将该酶高效分泌到培养基中。然而,在灰盖鬼伞这种担子菌中,XynF1几乎不分泌到培养基中。将信号肽的C端序列修饰为赖氨酸-精氨酸后,灰盖鬼伞XynF1实现了高效分泌,这表明该真菌中存在类似KEX2的蛋白酶。