SUBDOMAIN ORGANIZATION OF BACILLUS-THURINGIENSIS ENTOMOCIDAL PROTEINS N-TERMINAL DOMAINS

被引:11
作者
CHESTUKHINA, GG
TYURIN, SA
KOSTINA, LI
OSTERMAN, AL
ZALUNIN, IA
KHODOVA, OA
STEPANOV, VM
机构
[1] Laboratory of Protein Chemistry, Institute of Genetics and Selection of Industrial Microorganisms, Moscow
来源
JOURNAL OF PROTEIN CHEMISTRY | 1990年 / 9卷 / 04期
关键词
Bacillus thuringiensis; δ-endotoxins; limited proteolysis;
D O I
10.1007/BF01024627
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
N-Terminal domain (65 kD) of δ-endotoxin produced by Bacillus thuringiensis ssp. alesti, as shown by limited proteolysis, consists of two subdomains of molecular mass 30 and 33 kD that correspond, respectively, to conservative and variable regions of the δ-endotoxin primary structure. Furthermore, proteolysis of these subdomains leads to their conversion into at least two fragments of molecular mass 10 kD stable to proteinase action. Such a pattern of molecular organization appears to be common for several structurally related δ-endotoxins that belong to the kurstaki group. Entomicidal protein produced by ssp. israelensis (70 kD), which differs strongly from alesti and other kurstaki group δ-endotoxins, retains a similar type of molecular organization and consists of two subdomains with molecular mass of ∼35 kD. Apparently, the characteristic pattern of the δ-endotoxins' molecular structure reflects separation of functions (e.g., host recognition and toxicity per se) between domains and subdomains of these proteins. © 1990 Plenum Publishing Corporation.
引用
收藏
页码:501 / 507
页数:7
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