Abstract
The modified Cry1Ac was expressed in transgenic tobacco plants. To allow secretion of the Cry1Ac protein into the intercellular space, the signal peptide sequence of potato proteinase inhibitor II (pinII) was N-terminally fused to the Cry1Ac encoding region. Expression of Cry1Ac in transgenic tobacco plants was assayed with ELISA. The results showed that pinII signal peptide sequence enhanced the expression of Cry1Ac protein and led to the secretion of the Cry1Ac protein in transgenic tobacco plants. GFP gene was also fused to the signal peptide sequence and transformed to tobacco. The results of fluorescent detection showed that GFP had localized in the apoplast of transgenic plants.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus thuringiensis Toxins
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Bacterial Proteins / genetics*
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Bacterial Toxins / genetics*
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Base Sequence
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DNA, Plant / genetics
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Endotoxins / genetics*
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Gene Expression
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Genes, Bacterial
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Genes, Plant
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Green Fluorescent Proteins / genetics
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Hemolysin Proteins
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Nicotiana / genetics
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Plant Proteins / genetics*
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Plants, Genetically Modified
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Plasmids / genetics
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Protein Sorting Signals / genetics*
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Recombinant Fusion Proteins / genetics
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Solanum tuberosum / genetics
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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DNA, Plant
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Endotoxins
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Hemolysin Proteins
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Plant Proteins
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Protein Sorting Signals
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Recombinant Fusion Proteins
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insecticidal crystal protein, Bacillus Thuringiensis
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proteinase inhibitor II protein, plant
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Green Fluorescent Proteins