Difference between revisions of "Part:BBa K3610010"

Revision as of 19:52, 3 October 2020

CORE ectodomain from S. lycopersicum

This part compromises the cell surface receptor CORE of S. lycopersicum and contains the ectodomain and the transmembrane domain, including the juxtamembrane domain. It does not, however, include the native signal sequence in order to make it easier to express the CORE ectodomain in different organisms that do not recognize the signal sequence.

Usage and Biology

The cold shock protein receptor (CORE) is a plant pattern recognition receptor (PRR) and as such activates host innate immunity through detection of pathogen-associated molecular patterns (PAMPs). CORE is a leucine-rich repeat receptor-like kinase with 22 LRRs, there additionally is a 6 amino acid insert at LRR 11. It consists of an extracellular domain that perceives an epitope, csp22, from the highly conserved nucleic acid binding motif RNP-1 of bacterial cold-shock proteins (CSPs), which are highly abundant proteins found in the cytosol of bacteria. Further domains are a single pass transmembrane domain and an intracellular kinase domain (The sequence encoding the kinase domain is not in this part). Interaction of CORE with brassinosteroid-associated kinase (BAK)1 is necessary for inducing an immune response in the plant. The dimerization of CORE and BAK1 depends on the csp22, the ligand of CORE. The function of CORE in S. lycopersicum has been confirmed by expressing the receptor in A. thaliana, which made the plant responsive to csp22, a PAMP that is otherwise not perceived by PRRs from A. thaliana.

In our project we use this part to coexpress it together with the ectodomain of BAK1 in S. cerevisiae. The N-terminus of both parts are fused to a split-protein in order to visualize the interaction of the two LRR receptors. Used as system for a visual output to confirm dimerization were split-mCherry and split-NanoLuc.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 1467
Illegal BamHI site found at 100
Illegal BamHI site found at 1492
Illegal BamHI site found at 1844
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K3610010 short</partinfo>
-This part compromises the CORE receptor from S. lycopersicum and contains the ectodomain and the transmembrane domain, including the juxtamembrane domain. It does not, however, include the native signal sequence in order to make it easier to express the CORE ectodomain in different organisms that do not recognize the signal sequence from S. lycopersicum.
+This part compromises the cell surface receptor CORE of S. lycopersicum and contains the ectodomain and the transmembrane domain, including the juxtamembrane domain. It does not, however, include the native signal sequence in order to make it easier to express the CORE ectodomain in different organisms that do not recognize the signal sequence.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+The cold shock protein receptor (CORE) is a plant pattern recognition receptor (PRR) and as such activates host innate immunity through detection of pathogen-associated molecular patterns (PAMPs).
+CORE is a leucine-rich repeat receptor-like kinase with 22 LRRs, there additionally is a 6 amino acid insert at LRR 11. It consists of an extracellular domain that perceives an epitope, csp22, from the highly conserved nucleic acid binding motif RNP-1 of bacterial cold-shock proteins (CSPs), which are highly abundant proteins found in the cytosol of bacteria. Further domains are a single pass transmembrane domain and an intracellular kinase domain (The sequence encoding the kinase domain is not in this part).
+Interaction of CORE with brassinosteroid-associated kinase (BAK)1 is necessary for inducing an immune response in the plant. The dimerization of CORE and BAK1 depends on the csp22, the ligand of CORE.
+The function of CORE in S. lycopersicum has been confirmed by expressing the receptor in A. thaliana, which made the plant responsive to csp22, a PAMP that is otherwise not perceived by PRRs from A. thaliana.
+In our project we use this part to coexpress it together with the ectodomain of BAK1 in S. cerevisiae. The N-terminus of both parts are fused to a split-protein in order to visualize the interaction of the two LRR receptors.
+Used as system for a visual output to confirm dimerization were split-mCherry and split-NanoLuc.
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