Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy. Issue 12 (4th March 2022)

• Record Type: Journal Article
• Authors: Kugele, Anandi; Uzun, Buket; Müller, Lena; Schott-Verdugo, Stephan; Gohlke, Holger; Groth, Georg; Drescher, Malte
• Is Part Of: RSC advances. Volume 12:Issue 12(2022)
• Page Start: 7352
• Page End: 7356
• Publication Date: 2022-03-04
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d2ra00604a
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : The ethylene receptor 1 transmembrane domain was site-directedly spin labelled to obtain distance restraints. Abstract : 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.