Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal delta-endotoxin of Bacillus thuringiensis subsp. tenebrionis

FEMS Microbiol Lett. 2000 Feb 1;183(1):63-6. doi: 10.1111/j.1574-6968.2000.tb08934.x.

Abstract

The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal delta-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus thuringiensis / enzymology*
  • Bacillus thuringiensis / growth & development
  • Bacillus thuringiensis / metabolism
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / metabolism*
  • Bacterial Toxins*
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases / isolation & purification*
  • Endopeptidases / metabolism*
  • Endotoxins / metabolism*
  • Hemolysin Proteins
  • Humans
  • Immunoblotting
  • Metalloendopeptidases / metabolism*
  • Protease Inhibitors / pharmacology

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Hemolysin Proteins
  • Protease Inhibitors
  • insecticidal crystal protein, Bacillus Thuringiensis
  • Endopeptidases
  • Metalloendopeptidases