Difference between revisions of "Part:BBa K3610006"
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− | + | Elongation factor-thermo unstable receptor (EFR) from A. thaliana is a plant pattern-recognition receptor (PRR). It is a cell surface receptor and part of the plants firts defence mechanism against potential pathogens. The EFR receptor is also a leucin-rich-repeats (LRR) receptor-like serine/threonine-protein kinase. The protein consists of an extracellular domain with leucin-rich repeats, a ligand binding domain found in many receptors, a single-pass transmembrane domain and finally an intracellular kinase domain. The ligand binding domain from EFR has high specificity to a bacterial pathogen-associated moleculat pattern (PAMP), namely the epitope elf18 of the abundant protein Elongation Factor Tu (EF-Tu), which is catalyzes the binding of aminoacyl-tRNA (aa-tRNA) to the ribosome in most prokaryotes and therefore is evolutionarily highly conserved. This makes the EFR a receptor that can be activated by the presence of a huge variety of bacteria. Upon binding of the ligand to the extracellular domain, the receptor dimerizes with its coreceptor BRI1-associated receptor kinase (BAK1). This interaction triggers the activation of the intracellular kinase domain of EFR and BAK1, initiating a signal cascade leading to an upregulation of immune response mechanisms. | |
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Latest revision as of 20:21, 27 October 2020
EFR from A. thaliana - without signal sequence
This part is the EFR receptor from A. thaliana. It is similar to Part:BBa K3610005 but it lacks the signal sequence and is therefore not in frame. It needs to be expressed with a signal sequence. Either with the native signal sequence or with a signal sequence from another organism.
Usage and Biology
Elongation factor-thermo unstable receptor (EFR) from A. thaliana is a plant pattern-recognition receptor (PRR). It is a cell surface receptor and part of the plants firts defence mechanism against potential pathogens. The EFR receptor is also a leucin-rich-repeats (LRR) receptor-like serine/threonine-protein kinase. The protein consists of an extracellular domain with leucin-rich repeats, a ligand binding domain found in many receptors, a single-pass transmembrane domain and finally an intracellular kinase domain. The ligand binding domain from EFR has high specificity to a bacterial pathogen-associated moleculat pattern (PAMP), namely the epitope elf18 of the abundant protein Elongation Factor Tu (EF-Tu), which is catalyzes the binding of aminoacyl-tRNA (aa-tRNA) to the ribosome in most prokaryotes and therefore is evolutionarily highly conserved. This makes the EFR a receptor that can be activated by the presence of a huge variety of bacteria. Upon binding of the ligand to the extracellular domain, the receptor dimerizes with its coreceptor BRI1-associated receptor kinase (BAK1). This interaction triggers the activation of the intracellular kinase domain of EFR and BAK1, initiating a signal cascade leading to an upregulation of immune response mechanisms.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 2683
Illegal XbaI site found at 363
Illegal XbaI site found at 2498
Illegal SpeI site found at 1044
Illegal PstI site found at 2337 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 2683
Illegal SpeI site found at 1044
Illegal PstI site found at 2337 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 2683
Illegal BglII site found at 2348
Illegal BglII site found at 2376
Illegal BglII site found at 2919
Illegal XhoI site found at 2372
Illegal XhoI site found at 2962 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 2683
Illegal XbaI site found at 363
Illegal XbaI site found at 2498
Illegal SpeI site found at 1044
Illegal PstI site found at 2337 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 2683
Illegal XbaI site found at 363
Illegal XbaI site found at 2498
Illegal SpeI site found at 1044
Illegal PstI site found at 2337
Illegal AgeI site found at 186 - 1000COMPATIBLE WITH RFC[1000]