Structural and functional analysis of a cloned delta endotoxin of Bacillus thuringiensis berliner 1715

摘要: A plasmid-encoded crystal protein gene (bt2) has been cloned from Bacillus thuringiensis berliner 1715. In Escherichia coli, it directs the synthesis of 130-kDa (Bt2) which is toxic to larvae Pieris brassicae and Manduca sexta. Comparison deduced amino acid sequence this Bt2 with B. kurstaki HD1 Dipel, HD73 sotto sequences suggests that homologous recombination between different genes occurred during evolution. Treatment trypsin or chymotrypsin yields a 60-kDa protease-resistant fully polypeptide. The minimal portion required for toxicity determined by analysing polypeptides produced deletion derivatives bt2 gene. It coincides fragment starts acids 29 35 at N-terminus terminates positions 599 607 C-terminus.