INVOLVEMENT OF A POSSIBLE CHAPERONIN IN THE EFFICIENT EXPRESSION OF A CLONED CRYIIA DELTA-ENDOTOXIN GENE IN BACILLUS-THURINGIENSIS

被引：74

作者：

CRICKMORE, N ^{[1
]}

ELLAR, DJ ^{[1
]}

机构：

[1] UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CB2 1QW,ENGLAND

来源：

MOLECULAR MICROBIOLOGY | 1992年 / 6卷 / 11期

基金：

英国惠康基金;

关键词：

D O I：

10.1111/j.1365-2958.1992.tb00874.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Bacillus thuringiensis cryllA delta-endotoxin gene is found as the third-gene in a three-gene operon, with a sporulation-dependent promoter lying upstream of the first gene, orf1. We show here that the polypeptide product of the middle gene (orf2) is required for efficient expression of the toxin gene. In the absence of a functional ORF2 polypeptide the toxin does not form the crystalline inclusions characteristic of other known Bacillus thuringiensis toxins. We discuss the importance of this finding with respect to the possible role of chaperonins in the crystallization of these proteins.

引用

页码：1533 / 1537

页数：5

共 24 条

[1] A 20-KILODALTON PROTEIN IS REQUIRED FOR EFFICIENT PRODUCTION OF THE BACILLUS-THURINGIENSIS SUBSP ISRAELENSIS 27-KILODALTON CRYSTAL PROTEIN IN ESCHERICHIA-COLI [J].