Document Detail

Amino acids at N- and C-termini are required for the efficient production and folding of a cytolytic delta-endotoxin from Bacillus thuringiensis.
MedLine Citation:
PMID:  19017496     Owner:  NLM     Status:  MEDLINE    
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.
Siriya Thammachat; Wanwarang Pathaichindachote; Chartchai Krittanai; Boonhiang Promdonkoy
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  BMB reports     Volume:  41     ISSN:  1976-6696     ISO Abbreviation:  BMB Rep     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-11-21     Completed Date:  2009-01-16     Revised Date:  2009-04-27    
Medline Journal Info:
Nlm Unique ID:  101465334     Medline TA:  BMB Rep     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  820-5     Citation Subset:  IM    
Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, Nakhonpathom, Thailand.
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MeSH Terms
Amino Acid Sequence
Amino Acids / pharmacology*
Bacillus thuringiensis / chemistry
Bacterial Proteins / chemistry*,  isolation & purification*
Cytotoxins / chemistry,  isolation & purification
Endotoxins / chemistry*,  isolation & purification*
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
Reg. No./Substance:
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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