Part:BBa_K2220020
Display beta-tubulin protein
It can display β-tubulin on the surface of S.cerevisiae.
Among various GPI-anchored proteins, α/a-agglutinins are one of the most common proteins have been utilized for the display of proteins on a yeast cell surface. The native a and α agglutinin receptors are believed to act as adhesion molecules to stabilize cell-cell interactions during mating and to facilitate fusion between the a and α haploid yeast cells. A-agglutinin has a core subunit encoded by AGA1 and a binding subunit encoded by AGA2. Both a-agglutinin and the core subunit of a-agglutinin consist of a secretion-signal region, a functional region, a support region, and a putative GPI anchor-attachment signal. After genetic engineering, foreign protein can be fused to the C-terminal of the binding subunit of a-agglutinin. As AGA1 protein is secreted from the cell and becomes covalently attached to the β-glucan in the extracellular matrix of the yeast cell wall, aga2 protein fused with foreign protein on its C-terminus will then bind to aga1p through two disulfides bonds. As a result, the heterologous proteins are covalently linked with glucan-layer.
α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. Microtubules function in many essential cellular processes, including mitosis.
This part can express AGA2-β-tubulin fusion protein, which can display β-tubulin onto the yeast cell wall.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 325
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 641
Illegal BamHI site found at 388
Illegal BamHI site found at 1424
Illegal XhoI site found at 1726 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1795
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1777
Illegal BsaI.rc site found at 985
Illegal SapI site found at 1521
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