Difference between revisions of "Part:BBa K2279003"

Revision as of 04:51, 31 October 2017

PapR

PapR encodes a signal peptide.

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]

Biological function

B. cereus cause acute diarrheal disease by the production and secretion of a variety of hemolysins, phospholipases, and toxins. The production of virulence factors is controlled by the PlcR-PapR QS system. PapR is 48 amino acids long and contains an N-terminal signal peptide that targets it for secretion. Outside the cell, the PapR pro-AIP is processed by the secreted neutral protease B (NprB) to form the active AIP. The mature PapR oligopeptide sequence is ADVPFEL.Inside the cell, PapR binds to the transcription factor PlcR, and this causes conformational changes in the DNA-binding domain of PlcR, facilitates PlcR oligomerization, DNA binding, and regulation of transcription.

Design

To develop a synthetic QS system in B. subtilis for target gene autoinduction, we are going to combine the expression of PlcR and PapR components.

Furthermore, we will develop a synthetic communication pathway between B. subtilis strains by co-culturing PapR-producing “sender” cells with PlcR-sensing “receiver” cells to induce gene expression.

Reference

[1] Grenha, R., Slamti, L., Nicaise, M., Refes, Y., Lereclus, D., and Nessler, S. (2013). Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR. Proc Natl Acad Sci U S A 110, 1047-1052.

@@ Line 12: / Line 12: @@
 <partinfo>BBa_K2279003 SequenceAndFeatures</partinfo>
+===Biological function===
+B. cereus cause acute diarrheal disease by the production and secretion of a variety of hemolysins, phospholipases, and toxins. The production of virulence factors is controlled by the PlcR-PapR QS system. PapR is 48 amino acids long and contains an N-terminal signal peptide that targets it for secretion. Outside the cell, the PapR pro-AIP is processed by the secreted neutral protease B (NprB) to form the active AIP. The mature PapR oligopeptide sequence is ADVPFEL.Inside the cell, PapR binds to the transcription factor PlcR, and this causes conformational changes in the DNA-binding domain of PlcR, facilitates PlcR oligomerization, DNA binding, and regulation of transcription.
+[[File:PlcR.jpeg]]
+===Design===
+To develop a synthetic QS system in B. subtilis for target gene autoinduction, we are going to combine the expression of PlcR and PapR components.
+[[File:PlcAuto.jpg]]
+Furthermore, we will develop a synthetic communication pathway between B. subtilis strains by co-culturing PapR-producing “sender” cells with PlcR-sensing “receiver” cells to induce gene expression.
+[[File:PlcSR.jpeg]]
+===Reference===
+[1] Grenha, R., Slamti, L., Nicaise, M., Refes, Y., Lereclus, D., and Nessler, S. (2013). Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR. Proc Natl Acad Sci U S A 110, 1047-1052.
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