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Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki
Author(s) -
Kumar N. Suresh,
Venkateswerlu G.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203341
Subject(s) - proteases , bacillus thuringiensis , metalloproteinase , protease , toxin , endogeny , enzyme , biochemistry , microbiology and biotechnology , biology , proteolytic enzymes , chemistry , bacteria , genetics
Insecticidal crystal proteins harvested from sporulated cultures of Bacillus thuringiensis subsp, kurstaki contain the protoxin (Mr 132 kDa) and minor amounts of toxin (66 kDa). The proteolytic processing of 132 kDa protoxin to an active 66 kDa toxin is brought about by exogenous proteases or larval gut enzymes. Under denaturing / reducing conditions this conversion is also mediated by endogenous protease(s) of the producer organism. This endogenous protease is identified as a metalloprotease as the activation process is inhibited by ethylenediamine tetraacetic acid at 2 mM concentration.