Difference between revisions of "Part:BBa K4825008"
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In our project, this part is used to secrete heterologous protein Cry1518-35 out of S.cerevisiae, of which the efficiency is examined by secreting red fluorescence protein (RFP). This part can be applied as for a more efficient expression of heterologous proteins in S.cerevisiae than the yeast's native signal peptide, especially for the expression of large molecule proteins. " | In our project, this part is used to secrete heterologous protein Cry1518-35 out of S.cerevisiae, of which the efficiency is examined by secreting red fluorescence protein (RFP). This part can be applied as for a more efficient expression of heterologous proteins in S.cerevisiae than the yeast's native signal peptide, especially for the expression of large molecule proteins. " | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
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| + | JFm, optimized from the inulinase signal peptide, JF, in K.smarxianu, is a 74bp signal peptide located in the N-terminal of targeted proteins. Its role in translocating proteins to the periplasmic space or out of the cell starts with the N-region orienting the secretion by interactions with negatively charged phosphate group of the lipid bilayer of the cells; and because of the presence of Lys-Arg at the C-terminal of JF that can be recognized by S.cerevisiae's endoprotease, the translocation ends with the C-region being cleaved by signal peptidase. As a result, the targeted heterologous proteins will be secreted to extracellular space with a much higher level of bioactivity than the bioactivity inside the cells, whereas the signal peptide itself remains in the cytosol. | ||
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Revision as of 18:40, 11 October 2023
JF m
"JFm is a mutated version of the signal peptide originated in K.smarxianu, JF, and utilized in our project's chassis, S.cerevisiae, to target heterologous proteins to the extracellular environment of yeast cells.
This part as a signal peptide can function in S.cerevisiae to enhance the secretion level of heterologous proteins or recombinant enzymes by determining and trafficing the secretion pathway of target genes,and the modifications in the genetic sequence remarkably increase the secretion level in yeasts, compared to the original JF signal peptide
In our project, this part is used to secrete heterologous protein Cry1518-35 out of S.cerevisiae, of which the efficiency is examined by secreting red fluorescence protein (RFP). This part can be applied as for a more efficient expression of heterologous proteins in S.cerevisiae than the yeast's native signal peptide, especially for the expression of large molecule proteins. "
Usage and Biology
JFm, optimized from the inulinase signal peptide, JF, in K.smarxianu, is a 74bp signal peptide located in the N-terminal of targeted proteins. Its role in translocating proteins to the periplasmic space or out of the cell starts with the N-region orienting the secretion by interactions with negatively charged phosphate group of the lipid bilayer of the cells; and because of the presence of Lys-Arg at the C-terminal of JF that can be recognized by S.cerevisiae's endoprotease, the translocation ends with the C-region being cleaved by signal peptidase. As a result, the targeted heterologous proteins will be secreted to extracellular space with a much higher level of bioactivity than the bioactivity inside the cells, whereas the signal peptide itself remains in the cytosol.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]