Cyt2Ba of Bacillus thuringiensis israelensis:: Activation by putative endogenous protease
Cyt2Ba of Bacillus thuringiensis israelensis:: Activation by putative endogenous protease
复制标题
DOI：
10.1016/j.bbrc.2006.03.134
复制
发表时间：
2006-05-26
影响因子：
3.1
通讯作者：
Cahan, R
中科院分区：
文献类型：
--
作者：
Nisnevitch, M;Cohen, S;Cahan, R
苏云金芽孢杆菌（Bacillus thuringiensis subsp.）克隆Israelensis，用于在无晶体菌株中与p20一起表达。形成的大的六边形晶体由Cyt2Ba组成，这有助于其纯化。在内源性蛋白酶（具有孢子和细胞碎片）存在下的晶体增溶使得能够通过氨基酸残基34和35之间的切割（最可能是通过与活化的Cyt2Ba结合发现的骆驼溶素样蛋白酶）快速且简单地获得相当纯且活性的毒素种类。这种裂解的产物显示出与外源激活的Cyt2Ba相当的溶血活性。这种推定的蛋白酶的序列与密切相关的蜡状芽孢杆菌的细胞壁结合的金属蛋白酶（骆驼溶素）具有高度同源性。(c)2006爱思唯尔公司All rights reserved.
The gene cyt2 Ba of Bacillus thuringiensis subsp. israelensis was cloned for expression, together with p20, in an acrystalliferous strain. The large hexagonal crystals formed were composed of Cyt2Ba, which facilitated its purification. Crystal solubilization in the presence of endogenous proteases (with spores and cell debris) enabled quick and simple procedure to obtain rather pure and active toxin species by cleavage between amino acid residues 34 and 35, most likely by a camelysin-like protease that was discovered in association with activated Cyt2Ba. The product of this cleavage displayed haemolytic activity comparable to that of exogenously activated Cyt2Ba. The sequence of this putative protease shares high homology with the cell envelope-bound metalloprotcase (camelysin) of the closely related species Bacillus cereus. (c) 2006 Elsevier Inc. All rights reserved.