RBS + Antifungal GAFP-1 + Double terminator
The Gastrodia anti-fungal protein (GAFP-1), also known as gastrodianin, is a mannose and chitin binding lectin originating from the Asiatic orchid Gastrodia elata, a traditional Chinese medicinal herb cultured for thousands of years. GAFP-1 is composed of 15 amino acids LDSLSFSYNNFEEDD and is able to inhibit the growth of multiples species of plant pathogenic fungi.
This part is composed of a strong RBS and the coding sequence of the Gastrodia anti-fungal protein 1 (GAFP-1) optimized for its expression and its secretion in Bacillus subtilis (K1364002) and a double terminator (B0015).
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21COMPATIBLE WITH RFC
- 23COMPATIBLE WITH RFC
- 25Illegal NgoMIV site found at 59
- 1000COMPATIBLE WITH RFC
Xiaochen Wang, Guy Bauw, Els J.M. Van Damme, Willy J. Peumans, Zhang-Liang Chen, Marc Van Montagu. Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties. The Plant Journal . 2001, Vol. 25(6), 651±661
Schnabel, K. D. Cox · D. R. Layne · R. Scorza · G. Gastrodia anti-fungal protein from the orchid Gastrodia elata confers disease resistance to root pathogens in transgenic tobacco. Planta . 2006, Vol. 224:1373–1383.
Alexis Nagel. Understanding GAFP, A Plant Lectin with Broad spectrum Inhibitory Activity.
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