Difference between revisions of "Part:BBa K4863004"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | Fusion of a recombinant protein to the C-terminus of PilA1 will yield a cell covered with the fusion protein on its Type IV pili. Only small affinity proteins (<6.5kDA) can be functionally displayed via this system, or else the fusion protein would interfere with the biological functions of the pili. We present a system where SpyTag is modified to display on the cell surface of < | + | Fusion of a recombinant protein to the C-terminus of PilA1 will yield a cell covered with the fusion protein on its Type IV pili. Only small affinity proteins (<6.5kDA) can be functionally displayed via this system, or else the fusion protein would interfere with the biological functions of the pili. We present a system where SpyTag is modified to display on the cell surface of <i>Synechocystis</i> via fusion with PilA1. |
PilA1 is a major protein subunit in Type IV pili (T4P), which is a surface-exposed appendage responsible for various essential functions in cyanobacteria,formed by polymerization of several pilin monomers. PilA1 constitutes the major pilin, which is the major structural component of T4P necessary for its biogenesis. SpyTag is a 13 amino acid-long peptide chain originally isolated from <i>Streptococcus pyogenes</i>. | PilA1 is a major protein subunit in Type IV pili (T4P), which is a surface-exposed appendage responsible for various essential functions in cyanobacteria,formed by polymerization of several pilin monomers. PilA1 constitutes the major pilin, which is the major structural component of T4P necessary for its biogenesis. SpyTag is a 13 amino acid-long peptide chain originally isolated from <i>Streptococcus pyogenes</i>. | ||
Revision as of 03:45, 11 October 2023
PpsbA2_PilA1_SpyTag
A PilA1-SpyTag complex with SpyTag(BBa_K1159200) fused to the C-terminus of PilA1(BBa_K4863001) is constructed to achieve surface display of SpyTag on the cell surface of Synechocystis PCC 6803.
Usage and Biology
Fusion of a recombinant protein to the C-terminus of PilA1 will yield a cell covered with the fusion protein on its Type IV pili. Only small affinity proteins (<6.5kDA) can be functionally displayed via this system, or else the fusion protein would interfere with the biological functions of the pili. We present a system where SpyTag is modified to display on the cell surface of Synechocystis via fusion with PilA1.
PilA1 is a major protein subunit in Type IV pili (T4P), which is a surface-exposed appendage responsible for various essential functions in cyanobacteria,formed by polymerization of several pilin monomers. PilA1 constitutes the major pilin, which is the major structural component of T4P necessary for its biogenesis. SpyTag is a 13 amino acid-long peptide chain originally isolated from Streptococcus pyogenes.
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]