Difference between revisions of "Part:BBa K2255005"
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The molecular interactions that mediate the entry of filamentous phages into their hosts are mediated by protein 3. This protein consist of three domains, separated by glycine-rich regions, that serve distinct roles in phage entry and release. The first two pIII domains, D1 and D2, are required for M13 adsorption and entry, while the third domain D3 is required for the assembly and release of M13 particles from host. | The molecular interactions that mediate the entry of filamentous phages into their hosts are mediated by protein 3. This protein consist of three domains, separated by glycine-rich regions, that serve distinct roles in phage entry and release. The first two pIII domains, D1 and D2, are required for M13 adsorption and entry, while the third domain D3 is required for the assembly and release of M13 particles from host. | ||
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This part was design with Freiburg ([https://parts.igem.org/Assembly_standard_25 Rfc25]) extension. Thus, it contain the restriction site NgoMIV and AgeI that are compatible and allow the missing of a start and stop codon, which ease the assemble of multiple protein domain. | This part was design with Freiburg ([https://parts.igem.org/Assembly_standard_25 Rfc25]) extension. Thus, it contain the restriction site NgoMIV and AgeI that are compatible and allow the missing of a start and stop codon, which ease the assemble of multiple protein domain. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
Revision as of 16:51, 26 September 2017
Domain 3 of p3 from M13 (Rfc25)
The molecular interactions that mediate the entry of filamentous phages into their hosts are mediated by protein 3. This protein consist of three domains, separated by glycine-rich regions, that serve distinct roles in phage entry and release. The first two pIII domains, D1 and D2, are required for M13 adsorption and entry, while the third domain D3 is required for the assembly and release of M13 particles from host.
This part was design with Freiburg (Rfc25) extension. Thus, it contain the restriction site NgoMIV and AgeI that are compatible and allow the missing of a start and stop codon, which ease the assemble of multiple protein domain.
Usage and Biology
We used the protein D3 to associated it with multiple D1-D2 domains of p3 protein coming from other filamentous phages in order to create phage that target various pathogenes. Thus, this biobrick was created to be associated with part coming from our collection of attachment protein. You can check out the first part of this collection : BBa_K2255008.
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]