Efficient expression of genetically engineered hepatitis B virus surface antigen P31 proteins in yeast
| Autor: | Fujisawa Yukio, Kuroda Shunichi, Otaka-Imai Sachiko, Itoh Yasuaki, Miyazaki Takeshi |
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| Rok vydání: | 1989 |
| Předmět: |
Hepatitis B virus
HBsAg Genes Viral Protein Conformation Blotting Western Molecular Sequence Data Saccharomyces cerevisiae Protein Sorting Signals Endoplasmic Reticulum law.invention Transformation Genetic Plasmid law Gene expression Genetics Amino Acid Sequence RNA Messenger Cloning Molecular Gene Hepatitis B Surface Antigens Base Sequence biology Biological Transport Intracellular Membranes General Medicine biology.organism_classification Molecular biology Yeast Gene Expression Regulation Membrane protein DNA Viral Recombinant DNA Plasmids |
| Zdroj: | Gene. 78:297-308 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(89)90232-1 |
| Popis: | We have constructed plasmids that express modified hepatitis B virus surface antigen (HBsAg) P31-coding genes ( M-P31c, d, e, f, and i having various genetically engineered pre-S2 regions. The plasmids contain the GAPDH (gene coding for glyceraldehyde-3-phosphate dehydrogenase) promoter and the PGK (gene coding for 3-phosphoglycerate kinase) terminator, both isolated from sake brewing yeast, Saccharomyces cerevisiae Kyokai III. Expression levels of the modified HBsAg P31 proteins in yeast are greatly increased from 0.4% to 11.7% of total cell protein. However, the specific mRNAs are expressed at equal levels and the degradation rates of the modified P31 proteins do not vary significantly. Therefore, we considered that different expression levels of the modified P31 proteins are attributed to the changes of the post-translational efficiency. And it was suggested that the conformational stability of the N-terminal peptide (Met-l-Phe-46) in the endoplasmic reticulum membrane determines the expression level of modified P31 proteins. |
| Databáze: | OpenAIRE |
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