Secretion of a bacterial protein by mammalian cells
| Autor: | Jean-Marie Clément, Muguette Jéhanno |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Vesicle-associated membrane protein 8
Monosaccharide Transport Proteins Genetic Vectors Molecular Sequence Data Bioengineering Biology Transfection Applied Microbiology and Biotechnology Maltose-Binding Proteins Cell Line Retinoblastoma-like protein 1 Mice L Cells Bacterial Proteins Cricetinae HSPA2 Escherichia coli Animals Secretion Amino Acid Sequence Base Sequence Escherichia coli Proteins Binding protein General Medicine Autophagy-related protein 13 Immunohistochemistry Recombinant Proteins GPS2 EIF4EBP1 Biochemistry Periplasmic Binding Proteins ATP-Binding Cassette Transporters Carrier Proteins Plasmids Biotechnology |
| Zdroj: | Journal of Biotechnology. 43:169-181 |
| ISSN: | 0168-1656 |
| DOI: | 10.1016/0168-1656(95)00127-1 |
| Popis: | The MalE protein is a periplasmic maltooligosaccharide binding protein from Escherichia coli. This protein is widely used as a model for protein export in bacteria and as a vector for the export and one-step affinity purification of foreign polypeptides. Expression of MalE was studied in various animal cell lines. The protein was exported into the culture medium, following the classical pathway of eukaryotic protein secretion. This was shown by a combination of approaches including the use of inhibitors of the Golgi complex and immunocytological methods. The signal sequence of MalE is required for secretion and a specific signal can be added to MalE that targets it to the endoplasmic reticulum. This work opens the way to the study of the secretion of a bacterial protein and to its use as a vector for protein secretion and purification from mammalian cells. |
| Databáze: | OpenAIRE |
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