Secretion of miraculin through the function of a signal peptide conserved in the Kunitz‐type soybean trypsin inhibitor family
| Autor: | Takashi Aoyama, Rieko Nakata, Hiroyasu Inoue, Akane Ito, Ayako Takai, Makiko Satoh, Tomomi Matsuyama |
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| Rok vydání: | 2013 |
| Předmět: |
Signal peptide
Miraculin Recombinant Fusion Proteins Trypsin inhibitor Molecular Sequence Data Taste-modifying protein Arabidopsis Intracellular Space Biophysics Signal sequence Protein Sorting Signals Biology Biochemistry Conserved sequence Apoplast Cellulase Structural Biology Genetics medicine Amino Acid Sequence Molecular Biology Peptide sequence Conserved Sequence Glycoproteins Plant Proteins chemistry.chemical_classification Kunitz-type soybean protease inhibitor Kunitz STI protease inhibitor Cell Membrane Cell Biology Plants Genetically Modified Trypsin Protein Transport chemistry Trypsin Inhibitor Kunitz Soybean Glycoprotein medicine.drug |
| Zdroj: | FEBS Letters. 587:1767-1772 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1016/j.febslet.2013.04.026 |
| Popis: | Miraculin, a glycoprotein that modifies sour tastes into sweet ones, belongs to the Kunitz-type soybean trypsin inhibitor (STI) family. To clarify the functional relation of miraculin with Kunitz-type STIs, we investigated its subcellular localization and trypsin inhibitory activity. In transgenic Arabidopsis thaliana, miraculin, fused to yellow fluorescent protein, localized to and outside the plasma membrane depending on the putative secretion signal peptide. When transgenic seedlings were cultured in liquid medium, miraculin was present in the supernatant only after cellulase treatment. No trypsin inhibitory activity was detected in native or recombinant miraculin. In conclusion, miraculin is secreted outside the plasma membrane through the function of a signal peptide, conserved in Kunitz-type STIs, whereas its trypsin inhibitory activity may be lost during its evolution. |
| Databáze: | OpenAIRE |
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