Difference between revisions of "Part:BBa K2255005"

Latest revision as of 09:26, 9 October 2017

Domain 3 of p3 from M13 (Rfc25)

The molecular interactions that mediate the entry of filamentous phages into their hosts are mediated by the protein 3. This protein consists 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 designed with the Freiburg (Rfc25) extension. Thus, it contains the restriction sites NgoMIV and AgeI that are compatible and allow the absence of a start and stop codon, which eases the assembly of multiple protein domains.

Usage and Biology

We used the protein D3 associated with multiple D1-D2 domains of p3 proteins coming from other filamentous phages to create phages that target various pathogenes. Thus, this biobrick was created to be associated with parts coming from our collection of attachment proteins. You can check out the first part of this collection: BBa_K2255008 and our [http://2017.igem.org/Team:Aix-Marseille/M13_Design design page].

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K2255005 short</partinfo>
-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 the protein 3. This protein consists 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.
-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.
+This part was designed with the Freiburg ([https://parts.igem.org/Assembly_standard_25 Rfc25]) extension. Thus, it contains the restriction sites NgoMIV and AgeI that are compatible and allow the absence of a start and stop codon, which eases the assembly of multiple protein domains.
-This part was design with Freiburg (RFC[25]) 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.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+We used the protein D3 associated with multiple D1-D2 domains of p3 proteins coming from other filamentous phages to create phages that target various pathogenes. Thus, this biobrick was created to be associated with parts coming from our collection of attachment proteins. You can check out the first part of this collection: [https://parts.igem.org/Part:BBa_K2255008 BBa_K2255008] and our [http://2017.igem.org/Team:Aix-Marseille/M13_Design design page].
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