Difference between revisions of "Part:BBa K3799006"
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The biosynthesis of AIP requires AgrD which encodes the peptide precursor of AIP, and an integral membrane endopeptidase AgrB. AgrD propeptide produced initially localizes to the cytoplasmic membrane using the N-terminal amphipathic leader and the AgrB endopeptidase activity removes the AgrD C-terminal tail. | The biosynthesis of AIP requires AgrD which encodes the peptide precursor of AIP, and an integral membrane endopeptidase AgrB. AgrD propeptide produced initially localizes to the cytoplasmic membrane using the N-terminal amphipathic leader and the AgrB endopeptidase activity removes the AgrD C-terminal tail. | ||
| − | === | + | ===Cloning and Expression=== |
Revision as of 19:42, 21 October 2021
R0010(plac promoter)+I746001(AIP1 generator - agrB + agrD with RBSes and terminator)
This part consist of the AIP generator(I746001) under standard IPTG inducible plac promoter(R0010) of Ecoli.It is used to express S aureus quorum sensing molecule,AIP-1 in Ecoli host. The biosynthesis of AIP requires AgrD, the peptide precursor of AIP, and the integral membrane endopeptidase AgrB.AIP-1 regulates the production of extracellular virulence factors using the agr quorum-sensing system by regulating P2 and P3 promoters.
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]
Usage and Biology
Quorum sensing in S. aureus is regulated by cyclic thiolactone peptides known as autoinducing peptides (AIPs). The extracellular AIP produced by neighbouring bacteria is sensed by a two-component system encoded in the accessory gene regulator (agr) locus. At high concentration of AIP-1, the cascade is activated, leading to the production of virulence factors including toxins, superantigens, and exo-enzymes.
The biosynthesis of AIP requires AgrD which encodes the peptide precursor of AIP, and an integral membrane endopeptidase AgrB. AgrD propeptide produced initially localizes to the cytoplasmic membrane using the N-terminal amphipathic leader and the AgrB endopeptidase activity removes the AgrD C-terminal tail.
