Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy

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2022
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Uzun, Buket
Müller, Lena
Schott-Verdugo, Stephan
Gohlke, Holger
Groth, Georg
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RSC Advances. Royal Society of Chemistry. 2022, 12(12), pp. 7352-7356. eISSN 2046-2069. Available under: doi: 10.1039/d2ra00604a
Zusammenfassung

The plant ethylene receptor ETR1 is a key player in the perception of the phytohormone and subsequent downstream ethylene signal transmission, crucial for processes such as ripening, senescence and abscission. However, to date, there is sparse structural knowledge about the transmembrane sensor domain (TMD) of ETR1 that is responsible for the binding of the plant hormone and initiates the downstream signal transmission. Sequence information and ab initio modelling suggest that the TMD consists of three transmembrane helices. Here, we combined site-directed spin labelling with electron paramagnetic resonance spectroscopy and obtained distance restraints for liposome-reconstituted ETR1_TMD on the orientation and arrangement of the transmembrane helices. We used these data to scrutinize different computational structure predictions of the TMD.

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ISO 690KUGELE, Anandi, Buket UZUN, Lena MÜLLER, Stephan SCHOTT-VERDUGO, Holger GOHLKE, Georg GROTH, Malte DRESCHER, 2022. Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy. In: RSC Advances. Royal Society of Chemistry. 2022, 12(12), pp. 7352-7356. eISSN 2046-2069. Available under: doi: 10.1039/d2ra00604a
BibTex
@article{Kugele2022-03-01Mappi-57007,
  year={2022},
  doi={10.1039/d2ra00604a},
  title={Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy},
  number={12},
  volume={12},
  journal={RSC Advances},
  pages={7352--7356},
  author={Kugele, Anandi and Uzun, Buket and Müller, Lena and Schott-Verdugo, Stephan and Gohlke, Holger and Groth, Georg and Drescher, Malte},
  note={This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) project no. 267205415/CRC 1208 grant to GG (TP B06) and HG (TP 03).}
}
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This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) project no. 267205415/CRC 1208 grant to GG (TP B06) and HG (TP 03).
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