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Bacillus thuringiensis Cry1Aa toxin‐binding region of Bombyx mori aminopeptidase N
Author(s) -
Yaoi Katsuro,
Nakanishi Kazuko,
Kadotani Tomoyuki,
Imamura Morikazu,
Koizumi Nobuo,
Iwahana Hidenori,
Sato Ryoichi
Publication year - 1999
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/s0014-5793(99)01626-9
Subject(s) - bacillus thuringiensis , toxin , cry1ac , bombyx mori , aminopeptidase , escherichia coli , recombinant dna , binding site , biology , microbiology and biotechnology , biochemistry , bacteria , transgene , gene , amino acid , genetics , genetically modified crops , leucine
The Bacillus thuringiensis Cry1Aa toxin‐binding region of Bombyx mori aminopeptidase N (APN) was analyzed, to better understand the molecular mechanism of susceptibility to the toxin and the development of resistance in insects. APN was digested with lysylendopeptidase and the ability of the resulting fragments to bind to Cry1Aa and 1Ac toxins was examined. The binding abilities of the two toxins to these fragments were different. The Cry1Aa toxin bound to the fragment containing 40‐Asp to 313‐Lys, suggesting that the Cry1Aa toxin‐binding site is located in the region between 40‐Asp and 313‐Lys, while Cry1Ac toxin bound exclusively to mature APN. Next, recombinant APN of various lengths was expressed in Escherichia coli cells and its ability to bind to Cry1Aa toxin was examined. The results localized the Cry1Aa toxin binding to the region between 135‐Ile and 198‐Pro.