TY  - JOUR
AU  - Kugele, Anandi
AU  - Uzun, Buket
AU  - Müller, Lena
AU  - Schott-Verdugo, Stephan
AU  - Gohlke, Holger
AU  - Groth, Georg
AU  - Drescher, Malte
TI  - Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
JO  - RSC Advances
VL  - 12
SN  - 2046-2069
CY  - London
PB  - RSC Publishing
M1  - FZJ-2022-01668
SP  - 7352 - 7356
PY  - 2022
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000764246300001
DO  - DOI:10.1039/D2RA00604A
UR  - https://juser.fz-juelich.de/record/906750
ER  -