Subdomain organization of Bacillus thuringiensis entomocidal proteins' N-terminal domains.

N-Terminal domain (65 kD) of delta-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 delta-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 delta-endotoxins that belong to the kurstaki group. Entomicidal protein produced by ssp. israelensis (70 kD), which differs strongly from alesti and other kurstaki group delta-endotoxins, retains a similar type of molecular organization and consists of two subdomains with molecular mass of approximately 35 kD. Apparently, the characteristic pattern of the delta-endotoxins' molecular structure reflects separation of functions (e.g., host recognition and toxicity per se) between domains and subdomains of these proteins.