Cyt2Ba of Bacillus thuringiensis israelensis: activation by putative endogenous protease

Biochemical and Biophysical Research Communications
Marina NisnevitchRivka Cahan

Abstract

The gene cyt2Ba of Bacillus thuringiensis subsp. israelensis was cloned for expression, together with p20, in an acrystalliferous strain. The large hexagonal crystals formed were composed of Cyt2Ba, which facilitated its purification. Crystal solubilization in the presence of endogenous proteases (with spores and cell debris) enabled quick and simple procedure to obtain rather pure and active toxin species by cleavage between amino acid residues 34 and 35, most likely by a camelysin-like protease that was discovered in association with activated Cyt2Ba. The product of this cleavage displayed haemolytic activity comparable to that of exogenously activated Cyt2Ba. The sequence of this putative protease shares high homology with the cell envelope-bound metalloprotease (camelysin) of the closely related species Bacillus cereus.

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Citations

Aug 10, 2012·Cell Biochemistry and Biophysics·Marina NisnevitchYeshayahu Nitzan
Dec 7, 2010·Journal of Bacteriology·Kathryn J PflughoeftTheresa M Koehler
Dec 17, 2014·Toxins·Leopoldo PalmaPrimitivo Caballero
Oct 1, 2011·Journal of Molecular Biology·Shmuel CohenOrly Dym
Oct 30, 2008·Microbiology·Rivka CahanYeshayahu Nitzan
Aug 9, 2016·Journal of Invertebrate Pathology·Colin Berry, Jason Board
Jun 26, 2012·Insect Biochemistry and Molecular Biology·Alan I JiménezMario Soberón
Dec 15, 2018·Molecular Microbiology·Thomas CandelaMichel Gohar
Dec 6, 2018·International Journal of Molecular Sciences·Sudarat TharadJosé L Toca-Herrera

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