The biochemistry of the protein crystal toxin of Bacillus thuringiensis

Abstract

The crystal consists of dimeric protein subunits. The monomer peptide chains are held together in the subunit and the subunit in the crystal by disulfide and non-covalent bonds. The monomer peptide has a molecular weight of about 130 kdaltons which, in the presence of proteases, is hydrolyzed to a protease-resistant-protein of 65 kda that is toxic both to larvae by injection and to tissue culture cells and thus is the active toxin. The gene for this protein is on a plasmid which greatly simplifies the work of the genetic engineers. The gene has been partially sequenced and the secondary structure of this part has been predicted but not demonstrated.

Parent Publication

• Proceedings, Symposium: Microbial control of spruce budworms and gypsy moths

Citation

Fast, Paul G. 1985. The biochemistry of the protein crystal toxin of Bacillus thuringiensis. In: Grimble, David G.; Lewis, Franklin B., coords. Proceedings, Symposium: Microbial control of spruce budworms and gypsy moths; 1984 April 10-12; Windsor Locks, CT. Gen. Tech. Rep. NE-100. Broomall, PA: U.S. Department of Agriculture, Forest Service, Northeastern Forest Experiment Station. 109-113