Expression and secretion of scytalidopepsin B, an acid protease from Scytalidium lignicolum, in yeast.
An expression and secretion system for scytalidopepsin B, an acid protease from Scytalidium lignicolum, was constructed in yeast. Saccharomyces cerevisiae AH22 was transformed with an yeast-E. coli shuttle vector, pAM82, in which an yeast invertase signal segment and the cDNA encoding the pro- and mature enzyme regions were inserted. The transformant was found to secret a pepstatin-insensitive acid protease, when cultured aerobically in a low phosphate (Pi) medium. Amino terminal amino acid sequencing analysis indicated that the recombinant acid protease was accurately processed and secreted as a mature form.
Shimuta
K
K
Department of Applied Microbial Technology, sojo University, Kumamoto, Japan.
Oda-Ueda
N
N
Washio
M
M
Oyama
H
H
Oda
K
K
Tsuru
D
D
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000235:genetics*; D001483:Base Sequence; D004271:DNA, Fungal; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004792:Enzyme Precursors / Q000235:genetics*; D015870:Gene Expression; D003904:Mitosporic Fungi / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000378:metabolism
D004271:DNA, Fungal; D004792:Enzyme Precursors; D016282:Aspartic Acid Endopeptidases; C041236:Scytalidium lignicolum acid proteases