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AuthorDammak, Mariam
AuthorAli, Mamdouh Ben
AuthorJaoua, Samir
AuthorTounsi, Slim
Available date2017-02-19T11:17:59Z
Publication Date2012-02-10
Publication NameFEMS Microbiology Lettersen_US
Identifierhttp://dx.doi.org/10.1111/j.1574-6968.2012.02504.x
CitationMariam Dammak, Mamdouh Ben Ali, Samir Jaoua, Slim Tounsi "Amino acids Y229 and F603 are involved in Bacillus thuringiensis Cry1Ac δ-endotoxin stability and toxicity" FEMS Microbiol Lett (2012) 329 (1): 54-60
ISSN0378-1097
URIhttp://hdl.handle.net/10576/5282
AbstractBacillus thuringiensis Cry1Ac toxin shares structurally five conserved blocs with the other δ-endotoxins. To study the role of some amino acids belonging to these regions, two mutations, Y(229) P and F(603) S, were introduced respectively in blocs 2 and 5. The stability and crystallization of the resulting mutant proteins Cry1Ac'1 and Cry1Ac'3 were affected. Both of them lost their toxicity to the Lepidopteran larvae Ephestia kuehniella. Unlike Cry1Ac'1, Cry1Ac'3 became very sensitive to proteases. Accordingly, the three-dimensional structures of the two mutants were studied. The obtained models showed that both of the residues, Y229, located near the bottom of the α7 helix, and F603, located in the core of domain III, are involved in hydrophobic interactions essential for protein stability and toxicity. These results reveal that conserved amino acids blocs of Cry toxins have conformational and functional roles.
SponsorThis work was supported by grants from the Ministère de l'Enseignement Supérieur, de la Recherche Scientifique et de la Technologie.
Languageen
PublisherBlackwell Publishing
SubjectStructure
SubjectActivity
SubjectConserved blocs
SubjectSpecific mutation
SubjectBacillus thuringiensis
Subjectδ-endotoxin
TitleAmino acids Y229 and F603 are involved in Bacillus thuringiensis Cry1Ac delta-endotoxin stability and toxicity
TypeArticle
Pagination54-60
Issue Number1
Volume Number329
dc.identifier.essn 1574-6968


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