Difference between revisions of "Part:BBa K4825005"
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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 a robust control for heterologous expression in S.cerevisiae." | 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 a robust control for heterologous expression in S.cerevisiae." | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
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| + | ScMα, originated from S.cerevisiae, is a 267bp 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 ends with the C-region being cleaved by signal peptidase. As a result, the targeted heterologous proteins will be secreted to extracellular space, whereas the signal peptide itself remains in the cytosol. | ||
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Revision as of 18:30, 11 October 2023
SC Ma
"ScMα is the native signal peptide in S.cerevisiae that can target heterologous proteins to the extracellular environment of yeast cells.
This part as a signal peptide can enhance the ability of S.cerevisiae in secreting heterologous or recombinant enzymes by determining and trafficing the secretion pathway of target genes, but yet the secretion efficiency is not efficient enough.
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 a robust control for heterologous expression in S.cerevisiae."
Usage and Biology
ScMα, originated from S.cerevisiae, is a 267bp 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 ends with the C-region being cleaved by signal peptidase. As a result, the targeted heterologous proteins will be secreted to extracellular space, 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]