Difference between revisions of "Part:BBa K1592007"
ShuyanTang (Talk | contribs) |
ShuyanTang (Talk | contribs) |
||
| Line 4: | Line 4: | ||
This is the cell display system of Yarrowia lipolytica, composed of LIP prepro, interest protein, and YLcwp3. | This is the cell display system of Yarrowia lipolytica, composed of LIP prepro, interest protein, and YLcwp3. | ||
| − | LIP prepro is signal peptide used to secrete the interest protein out of the cell, and the YLcwp3 is the anchor domain binding the interest protein to the cell wall of yeast. | + | |
| − | We use this system to display silica-tag and test its binding characteristics. | + | LIP prepro is signal peptide used to secrete the interest protein out of the cell, and the YLcwp3 is the anchor domain binding the interest protein to the cell wall of yeast.We use this system to display silica-tag and test its binding characteristics. |
| + | |||
E.coli ribosomal protein L2 was found to bind tightly to silicon particles, which have surfaces that are oxidized to silica. This L2 silica-binding tag, called the 'Si-tag', can be used for one-step targeting of functional proteins on silica surfaces. The silica-binding domains of E. coli L2 was mapped to amino acids 1–60, 61-202 and 203–273, called Si-tag1, Si-tag2 and Si-tag3. We respectively test the silica-binding characteristics of this three regions and their combinations. | E.coli ribosomal protein L2 was found to bind tightly to silicon particles, which have surfaces that are oxidized to silica. This L2 silica-binding tag, called the 'Si-tag', can be used for one-step targeting of functional proteins on silica surfaces. The silica-binding domains of E. coli L2 was mapped to amino acids 1–60, 61-202 and 203–273, called Si-tag1, Si-tag2 and Si-tag3. We respectively test the silica-binding characteristics of this three regions and their combinations. | ||
Revision as of 03:00, 7 September 2015
LIP prepro + E. coli ribosomal protein L2 (1-60aa) + YLcwp3 Fusion
This is the cell display system of Yarrowia lipolytica, composed of LIP prepro, interest protein, and YLcwp3.
LIP prepro is signal peptide used to secrete the interest protein out of the cell, and the YLcwp3 is the anchor domain binding the interest protein to the cell wall of yeast.We use this system to display silica-tag and test its binding characteristics.
E.coli ribosomal protein L2 was found to bind tightly to silicon particles, which have surfaces that are oxidized to silica. This L2 silica-binding tag, called the 'Si-tag', can be used for one-step targeting of functional proteins on silica surfaces. The silica-binding domains of E. coli L2 was mapped to amino acids 1–60, 61-202 and 203–273, called Si-tag1, Si-tag2 and Si-tag3. We respectively test the silica-binding characteristics of this three regions and their combinations.