Linked Life Data

8405934

Source:http://linkedlifedata.com/resource/pubmed/id/8405934

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pubmed-article:8405934pubmed:abstractTextWhen activated by treatment with mosquito (Aedes aegypti) gut extract, the Bacillus thuringiensis CryIVB delta-endotoxin lysed A. aegypti cells in vitro. SDS-PAGE and N-terminal sequence determination showed that in addition to removal of the C-terminal half of the molecule, the activated toxin had undergone proteolytic cleavage at two internal regions producing 47-48-kDa and 16-18-kDa polypeptides. Aligning the CryIVB protein sequence with the crystallographic structure of the CryIIIA toxin suggested that one set of cleavages occurred in a region before the start of the N-terminal helical bundle and the second cleavage site occurred in a predicted loop between helices 5 and 6 in the bundle at arginine-203. To investigate the suggestion by Li et al. that interhelical proteolysis is important in the cytolytic mechanism of these toxins, arginine-203 was substituted by alanine. The mutated toxin now resisted proteolysis at this position and showed a marked decrease in cytolysis in vitro but an increase in larvicidal activity.lld:pubmed
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pubmed-article:8405934pubmed:articleTitleEffects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB delta-endotoxin.lld:pubmed
pubmed-article:8405934pubmed:affiliationDepartment of Biochemistry, University of Cambridge, UK.lld:pubmed
pubmed-article:8405934pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8405934pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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