从白色灰链霉菌S-3253的枯草杆菌蛋白酶抑制剂缺陷型突变体中分离出的一种编码细胞外丝氨酸蛋白酶的基因的分子特征分析。
Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253.
作者信息
Taguchi S, Odaka A, Watanabe Y, Momose H
机构信息
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
出版信息
Appl Environ Microbiol. 1995 Jan;61(1):180-6. doi: 10.1128/aem.61.1.180-186.1995.
Abstract
An extracellular serine protease produced by a mutant, M1, derived from Streptomyces albogriseolus S-3253 that no longer produces a protease inhibitor (Streptomyces subtilisin inhibitor [SSI]) was isolated. A 20-kDa protein was purified by its affinity for SSI and designated SAM-P20. The amino acid sequence of the amino-terminal region of SAM-P20 revealed high homology with the sequences of Streptomyces griseus proteases A and B, and the gene sequence confirmed the relationships. The sequence also revealed a putative amino acid signal sequence for SAM-P20 that apparently functioned to allow secretion of SAM-P20 from Escherichia coli carrying the recombinant gene. SAM-P20 produced by E. coli cells was shown to be sensitive to SSI inhibition.
摘要
从不再产生蛋白酶抑制剂（链霉菌枯草杆菌蛋白酶抑制剂[SSI]）的白灰链霉菌S-3253衍生的突变体M1中分离出一种细胞外丝氨酸蛋白酶。一种20 kDa的蛋白质通过其对SSI的亲和力被纯化，并命名为SAM-P20。SAM-P20氨基末端区域的氨基酸序列与灰色链霉菌蛋白酶A和B的序列具有高度同源性，基因序列证实了这种关系。该序列还揭示了SAM-P20的一个推定氨基酸信号序列，其明显起到使携带重组基因的大肠杆菌分泌SAM-P20的作用。大肠杆菌细胞产生的SAM-P20显示对SSI抑制敏感。
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