CLONING AND CHARACTERIZATION OF PEPC, A GENE ENCODING A SERINE PROTEASE FROM ASPERGILLUS-NIGER

被引:46
作者
FREDERICK, GD [1 ]
ROMBOUTS, P [1 ]
BUXTON, FP [1 ]
机构
[1] CIBA GEIGY AG,CH-4002 BASEL,SWITZERLAND
关键词
SERINE ENDOPEPTIDASE; PROTEINASE-B; PROTEINASE-K; SUBTILISIN; SIGNAL SEQUENCE; GENE STRUCTURE; INTRON; EXON;
D O I
10.1016/0378-1119(93)90745-O
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
We have cloned a gene, pepC, encoding a serine proteinase, PEPC, from Aspergillus niger by screening a phage lambda genomic DNA library with a gene (PRB1) from Saccharomyces cerevisiae which codes for proteinase YscB. The nucleotide (nt) sequence of pepC revealed that the gene is composed of two exons of 369 nt and 1230 nt separated by a single 70-nt intron. The deduced protein of 533 amino acids (aa) has a putative signal sequence for transport into the endoplasmic reticulum. Based on the extensive homology shown with serine proteinases (SerP) of the subtilisin family, which includes the active site triad, we hypothesise that the protein is made as a larger precursor which is matured by the cleavage of 130-140 aa from its N terminus and possibly by the removal of approx. 70 aa from its C terminus.
引用
收藏
页码:57 / 64
页数:8
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