TY - JOUR
T1 - Cyt2Ba of Bacillus thuringiensis israelensis
T2 - Activation by putative endogenous protease
AU - Nisnevitch, Marina
AU - Cohen, Shmuel
AU - Ben-Dov, Eitan
AU - Zaritsky, Arieh
AU - Sofer, Yossef
AU - Cahan, Rivka
N1 - Funding Information:
We thank the following undergraduate students from the Chemical and Biotechnology Engineering department at the college of Judea and Samaria for assistance with this research: Ben-Horin Y., Danon S., Cohen A., and Cohen L. This research was partially supported by a grant (No. 2001-042) from the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel to A.Z.
PY - 2006/5/26
Y1 - 2006/5/26
N2 - 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.
AB - 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.
KW - Bacillus thuringiensis subsp. israelensis
KW - Camelysin
KW - Cyt2Ba
UR - https://www.scopus.com/pages/publications/33646048033
U2 - 10.1016/j.bbrc.2006.03.134
DO - 10.1016/j.bbrc.2006.03.134
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C2 - 16630537
AN - SCOPUS:33646048033
SN - 0006-291X
VL - 344
SP - 99
EP - 105
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -