Molecular cloning of a complimentary DNA sequence encoding a cuticle degrading protease produced by entomopathogenic fungi

摘要: We have studied the regulation of extracellular chymoelastase protease (Pr1) Metarhizium anisopliae, an enzyme involved in penetration insect cuticle by and other entomopathogenic fungi. report here isolation characterization a Pr1 cDNA clone with full length insert. is synthesized as large precursor (40.3 kDa) containing signal peptide propeptide mature protein predicted to relative molecular mass 28.6 kDa. The primary structure shares extensive homology (30-60%) enzymes subtilisin subclass serine endopeptidases serine, histidine aspartyl components active site subtilisins are preserved. genes coding for or slightly altered versions thereof, can be used transform various organisms (i.e. fungi, viruses, plants, bacteria, etc.) such that transformed capable producing recoverable quantities. Fragments derviatives DNA sequence could code polypeptide having activity which can: a) bind cuticle; b) enhance processing proteins; c) hydrolyse polypepetides; d) suppress expression; e) probe identify homologous organisms. While chymoelastases been previously isolated, new novel uses disclosed, wherein selectively degrade presence non-protein polymers. A insecticide disclosed comprises recombinant virus, microorganism, cell, plant fungi infects, eaten otherwise taken up by, expresses within said activates prophenoloxidase system insect.