| Amino acids at N- and C-termini are required for the efficient production and folding of a cytolytic delta-endotoxin from Bacillus thuringiensis. | |
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MedLine Citation:
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PMID: 19017496 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Bacillus thuringiensis Cyt2Aa toxin is a mosquito-larvicidal and cytolytic delta-endotoxin, which is synthesized as a protoxin and forms crystalline inclusions within the cell. These inclusions are solubilized under alkaline conditions and are activated by proteases within the larval gut. In order to assess the functions of the N-and C-terminal regions of the protoxin, several N- and C-terminal truncated forms of Cyt2Aa were constructed. It was determined that amino acid removal at the N-terminal, which disrupts the beta1 structure, might critically influence toxin production and inclusion formation. The deletion of 22 amino acids from the C-terminus reduced the production and solubility of the toxin. However, the removal of more than 22 amino acids from the C-terminus or the addition of a bulky group to this region could result in the inability of the protein to adopt the proper folding. These findings directly demonstrated the critical roles of N- and C- terminal amino acids on the production and folding of the B. thuringiensis cytolytic delta-endotoxin. |
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Authors:
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Siriya Thammachat; Wanwarang Pathaichindachote; Chartchai Krittanai; Boonhiang Promdonkoy |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: BMB reports Volume: 41 ISSN: 1976-6696 ISO Abbreviation: BMB Rep Publication Date: 2008 Nov |
Date Detail:
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Created Date: 2008-11-21 Completed Date: 2009-01-16 Revised Date: 2009-04-27 |
Medline Journal Info:
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Nlm Unique ID: 101465334 Medline TA: BMB Rep Country: Korea (South) |
Other Details:
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Languages: eng Pagination: 820-5 Citation Subset: IM |
Affiliation:
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Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, Nakhonpathom, Thailand. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acids / pharmacology* Bacillus thuringiensis / chemistry Bacterial Proteins / chemistry*, isolation & purification* Cytotoxins / chemistry, isolation & purification Efficiency Endotoxins / chemistry*, isolation & purification* Fluorescence Hemolysin Proteins / chemistry*, isolation & purification* Molecular Sequence Data Peptide Fragments / chemistry, metabolism Peptide Hydrolases / metabolism Protein Folding / drug effects* Protein Structure, Secondary / physiology Protein Structure, Tertiary / physiology Spectrum Analysis |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Bacterial Proteins; 0/Cytotoxins; 0/Endotoxins; 0/Hemolysin Proteins; 0/Peptide Fragments; 0/insecticidal crystal protein, Bacillus Thuringiensis; EC 3.4.-/Peptide Hydrolases |
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