Structural and functional characterization of the .alpha.5 segment of Bacillus thuringiensis .delta.-endotoxin

Biochemistry ◽  
1993 ◽  
Vol 32 (13) ◽  
pp. 3429-3436 ◽  
Author(s):  
Ehud Gazit ◽  
Yechiel Shai
Keyword(s):  
Bacillus Thuringiensis ◽  
Functional Characterization ◽  
Delta Endotoxin

scholarly journals Identification and Functional Characterization of Two Homologous SpoVS Proteins Involved in Sporulation of Bacillus thuringiensis

2021 ◽  
Author(s):  
Xinlu Liu ◽  
Ruibin Zhang ◽  
Shuo Hou ◽  
Huanhuan Liu ◽  
Jiaojiao Wang ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Functional Characterization ◽  
Content Type

There is only one spoVS gene in B. subtilis , and its effects on sporulation have been reported. In this study, two homologous spoVS genes were found and identified in B. thuringiensis .

scholarly journals Whole genome analysis and functional characterization of a novel Bacillus thuringiensis (Bt 62) isolate against sugarcane whitegrub Holotrichia serrata (F)

Genomics ◽  
2021 ◽  
Author(s):  
Murugan Naveenarani ◽  
Giriyapura Shivalingamurthy Suresha ◽  
Jandhyala Srikanth ◽  
Kuppusamy Hari ◽  
Chellappa Sankaranarayanan ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Genome Analysis ◽  
Functional Characterization ◽  
Whole Genome ◽  
Whole Genome Analysis ◽  
Holotrichia Serrata

Genetic diversity and functional characterization of endophytic Bacillus thuringiensis isolates from the North Western Indian Himalayas

2016 ◽  
Vol 67 (2) ◽  
pp. 143-155 ◽  
Author(s):  
Pankaj Kumar Mishra ◽  
Shekhar Chandra Bisht ◽  
Pooja Ruwari ◽  
Avupati Raja Naga Satya Subbanna ◽  
Jaideep Kumar Bisht ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Bacillus Thuringiensis ◽  
Functional Characterization ◽  
The North ◽  
North Western ◽  
Indian Himalayas

scholarly journals The α-5 segment of Bacillus thuringiensis δ-endotoxin: in vitro activity, ion channel formation and molecular modelling

1994 ◽  
Vol 304 (3) ◽  
pp. 895-902 ◽  
Author(s):  
E Gazit ◽  
D Bach ◽  
I D Kerr ◽  
M S P Sansom ◽  
N Chejanovsky ◽  
...  
Keyword(s):  
Ion Channels ◽  
Bacillus Thuringiensis ◽  
Molecular Modelling ◽  
Lipid Membranes ◽  
Functional Characterization ◽  
Coiled Coil ◽  
Emission Spectra ◽  
Blue Shift ◽  
Delta Endotoxin

A peptide with a sequence corresponding to the highly conserved alpha-5 segment of the Cry delta-endotoxin family (amino acids 193-215 of Bacillus thuringiensis CryIIIA [Gazit and Shai (1993) Biochemistry 32, 3429-3436]), was investigated with respect to its interaction with insect membranes, cytotoxicity in vitro towards Spodoptera frugiperda (Sf-9) cells, and its propensity to form ion channels in planar lipid membranes (PLMs). Selectively labelled analogues of alpha-5 at either the N-terminal amino acid or the epsilon-amine of its lysine, were used to monitor the interaction of the peptides with insect membranes. The fluorescent emission spectra of the 7-nitrobenz-2-oxa-1,3-diazole-4-yl (NBD)-labelled alpha-5 peptides displayed a blue shift upon binding to insect (Spodoptera littoralis) mid-gut membranes, reflecting the relocation of the fluorescent probes to an environment of increased apolarity, i.e. within the lipidic constituent of the membrane. Moreover, midgut membrane-bound NBD-labelled alpha-5 peptides were protected from enzymic proteolysis. Functional characterization of alpha-5 has revealed that it is cytotoxic to Sf-9 insect cells, and that it forms ion channels in PLMs with conductances ranging from 30 to 1000 pS. A proline-substituted analogue of alpha-5 is less cytolytic and slightly more exposed to enzymic digestion. Molecular modelling utilizing simulated annealing via molecular dynamics suggests that a transbilayer pore may be formed by alpha-5 monomers that assemble to form a left-handed coiled coil of approximately parallel helices. These findings further support a role for alpha-5 in the toxic mechanism of delta-endotoxins, and assign alpha-5 as one of the transmembrane helices which form the toxic pore. The suggested role is consistent with the recent finding that cleavage of CryIVB delta-endotoxin in a loop between alpha-5 and alpha-6 is highly important for its larvicidal activity [Angsuthanasombat, Crickmore and Ellar (1993) FEMS Microbiol. Lett. 111, 255-262].

Production, purification and functional characterization of phospholipase C from Bacillus thuringiensis with high catalytic activity

2019 ◽  
Vol 83 ◽  
pp. 122-130 ◽  
Author(s):  
Ahlem Eddehech ◽  
Nabil Smichi ◽  
Yani Arhab ◽  
Alexandre Noiriel ◽  
Abdelkarim Abousalham ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Bacillus Thuringiensis ◽  
Phospholipase C ◽  
Functional Characterization ◽  
High Catalytic Activity
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