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Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella – their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin
Author(s) -
Nakanishi Kazuko,
Yaoi Katsuro,
Nagino Yasushi,
Hara Hirotaka,
Kitami Madoka,
Atsumi Shogo,
Miura Nami,
Sato Ryoichi
Publication year - 2002
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(02)02708-4
Subject(s) - bombyx mori , plutella , gene isoform , bacillus thuringiensis , midgut , biology , aminopeptidase , toxin , microbiology and biotechnology , isozyme , biochemistry , binding site , lepidoptera genitalia , enzyme , gene , botany , genetics , amino acid , bacteria , larva , leucine
Novel aminopeptidase N (APN) isoform cDNAs, BmAPN3 and PxAPN3 , from the midguts of Bombyx mori and Plutella xylostella , respectively, were cloned, and a total of eight APN isoforms cloned from B. mori and P. xylostella were classified into four classes. Bacillus thuringiensis Cry1Aa and Cry1Ab toxins were found to bind to specific APN isoforms from the midguts of B. mori and P. xylostella , and binding occurred with fragments that corresponded to the BmAPN1 Cry1Aa toxin‐binding region of each APN isoform. The results suggest that APN isoforms have a common toxin‐binding region, and that the apparent specificity of Cry1Aa toxin binding to each intact APN isoform seen in SDS–PAGE is determined by factors such as expression level in conjunction with differences in binding affinity.