| Amino acids Y229 and F603 are involved in Bacillus thuringiensis Cry1Ac delta-endotoxin stability and toxicity. | |
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MedLine Citation:
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PMID: 22268917 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Bacillus thuringiensis Cry1Ac toxin shares structurally five conserved blocs with the other delta-endotoxins. In order to study the role of some amino acids belonging to these regions, two mutations, Y(229) P and F(603) S, have been introduced separately and respectively in blocs 2 and 5. The resulting mutant proteins Cry1Ac'1 and Cry1Ac'3 were affected in their stability and crystallization. Both of them lost their toxicity to the Lepidopteran larvae Ephestia kuehniella. Unlike Cry1Ac'1, Cry1Ac'3 becomes very sensitive to proteases. Accordingly, 3-Dimential structures of the two mutants have been studied. The obtained models showed that both of the residuesY229, located near the bottom of the α7 helix, and F603, located in the core of the 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. |
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Authors:
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Mariam Dammak; Mamdouh Ben Ali; Samir Jaoua; Slim Tounsi |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-1-23 |
Journal Detail:
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Title: FEMS microbiology letters Volume: - ISSN: 1574-6968 ISO Abbreviation: - Publication Date: 2012 Jan |
Date Detail:
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Created Date: 2012-1-24 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7705721 Medline TA: FEMS Microbiol Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved. |
Affiliation:
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Biopesticides team (LPAP), Centre of Biotechnology of Sfax, University of Sfax, P.O. Box "1177″, 3018, Sfax, Tunisia. dammak_mar@yahoo.fr. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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