AI Article Synopsis
- The secretion of recombinant proteins from yeast Pichia pastoris requires a signal peptide, which is crucial for proper processing.
- A study showed that including a Gateway recombination site within the signal peptide of synthetic human interferon still allowed for high levels of protein secretion.
- Both cloning methods (Gateway and traditional restriction enzyme/ligase) produced secreted proteins with identical amino termini that were effective in biological assays, making Gateway cloning a simpler option for plasmid construction.
Article Abstract
Secretion of a recombinant protein from the yeast Pichia pastoris requires the presence of a signal peptide at the amino terminus. Maintaining the full amino acid sequence of the signal peptide is thought to be important for proper signal processing and protein secretion. We show that at least for one protein, a synthetic human interferon, the presence of a Gateway recombination site within the signal peptide is fully compatible with high levels of protein secretion. The amino termini of the secreted interferon proteins cloned with Gateway and cloned with restriction enzymes and ligase are identical, and the proteins were highly active in biological assays. Compatibility with Gateway cloning simplifies construction of plasmids directing secretion of recombinant proteins from P. pastoris.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130006 | PMC |
| http://dx.doi.org/10.1016/j.pep.2004.12.006 | DOI Listing |
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