N-terminal activation is an essential early step in the mechanism of action of the Bacillus thuringiensis Cry1Ac insecticidal toxin.

被引：45

作者：

Bravo, A ^{[1
]}

Sánchez, J ^{[1
]}

Kouskoura, T ^{[1
]}

Crickmore, N ^{[1
]}

机构：

[1] Univ Sussex, Sch Biol Sci, Brighton BN1 9QG, E Sussex, England

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2002年 / 277卷 / 27期

关键词：

D O I：

10.1074/jbc.C200263200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A variant form of the Bacillus thuringiensis Cry1Ac toxin that is not cleaved at the N terminus during proteolytic activation with trypsin was found to be incapable of forming pores in Manduca sexta brush border membrane vesicles in vitro and had reduced insecticidal activity in vivo. Binding studies indicated an altered binding pattern of the mutant toxin in that bound toxin could not be fully displaced by a high molar excess of fully trypsin-activated toxin. These results suggest that proteolytic removal of the N-terminal peptide of Cry1Ac is an important step in toxin activation.

引用

页码：23985 / 23987

页数：3

共 10 条

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