[Thermodynamic analysis of domain organization of Bacillus thuringiensis toxins].

The structure of delta-endotoxins CryIA(c) and CryIIIA from Bacillus thuringiensis was studied by differential scanning microcalorimerty. The analysis of molecular melting showed that the N- and C-terminal halves of the CryIA(c) protoxin from B. thuringiensis subspecies kurstaki HD-73 are thermodynamically independent subunits, with the C-terminal fragment being denatured at a much lower temperature than the N-terminal fragment. The tertiary structure of the N-terminal fragment undergoes no changes during the protoxin-toxin transition. The melting of the native structure of CryIA(c) at pH 9.7-11.0 suggests that it consists of two domains. In CryIIIA from B. thuringiensis subspecies tenebrionis, the transition from the native to denatured state under alkaline conditions (pH 9.7-11.0) proceeds by the "two-state" principle; i.e., the protein melts as one cooperative domain. The melting of the CryIIIA toxin at pH 2.2-3.5 is described by two transitions overlapping by temperatures, indicating the presence of two domains.