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Amino acid sequences from the N‐terminal domain of Bacillus thuringiensis , subspecies alesti , δ‐endotoxin
Author(s) -
Chestukhina G.G.,
Tyurin S.A.,
Osterman A.L.,
Khodova O.P.,
Stepanov V.M.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80421-5
Subject(s) - bacillus thuringiensis , subspecies , amino acid , homology (biology) , bacillaceae , residue (chemistry) , bacillales , stereochemistry , alanine , biology , peptide sequence , amino acid residue , chemistry , biochemistry , bacteria , genetics , gene , ecology , bacillus subtilis
The tryptic peptides derived from the N‐terminal domain of δ‐endotoxin produced by Bacillus thuringiensis ssp. alesti have been sequenced and aligned by homology with the primary stuctures of δ‐endotoxins formed by B . t . kurstaki subspecies (K−1 and K−73). The N‐terminal regions of the domains (residues 1–346) show only marginal variations: 9 amino acid substitutions were found among 158 aligned residues of B . t . ssp. alesti δ‐endotoxin. In contrast, the following stretch of the sequence starting from residue 347 reveals ~ 50% of amino acid substitutions when compared with the structures of K−1 or K−73. As a rule, the fragments of B . t . ssp. alesti δ‐endotoxin that differ from K‐1 in structure precisely reproduce the corresponding sequences of K−73 δ‐endotoxin and, vice versa, those different from the K−73 sequences coincide with the respective structures of K−1 δ‐endotoxin. A few fragments present in B . t . ssp. alesti were also found but not in both B . t . ssp. kurstaki δ‐endotoxins. It appears that the structure of this region of B . thuringiensis δ‐endotoxins (347–625 residues) contains a pattern of relatively conservative and highly variable fragments. These variations might be responsible for the variations in specificity of the entomocidal action of δ‐endotoxins.