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13C, 15N and 1H resonance assignments of receiver domain of ethylene receptor ETR1

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Abstract

Ethylene plays versatile functions in regulating plant physiology. Although the high affinity ethylene receptor and its downstream regulators have been identified, the molecular recognition of the receptor interacting domains remains to be established. It has been speculated that the cytoplasmic signaling of the ethylene receptor is a two-component regulatory system involving the conserved receiver domain (RD). Here, we report the NMR chemical shift assignments for RD from Arabidopsis thaliana ethylene receptor ETR1. Nearly complete backbone and side-chain assignments were achieved at pH 6.0 and 25 °C. The assignments and backbone dynamics revealed the secondary structure and showed that ETR1-RD is a monomer in solution. These results will make it possible to monitor downstream binding partners and elucidates our understanding of phosphotransfer in the plant two-component regulatory system in the ethylene signaling pathway.

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Acknowledgments

We are grateful to Dr. Chi-Kuang Wen (Chinese Academy of Science, Shanhui) for initiating the study. We received financial support from the National Science Council (NSC), Taiwan. We acknowledge the NMR facility at National Tsing Hua University supported by NSC and Core facility for protein structural analysis at Academia Sincia supported by National Core facility Program for Biotechnology.

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Correspondence to Shih-Che Sue.

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Yi-Lin Hung and Yi-Jan Lin contributed equally to this work.

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Hung, YL., Lin, YJ. & Sue, SC. 13C, 15N and 1H resonance assignments of receiver domain of ethylene receptor ETR1. Biomol NMR Assign 9, 119–122 (2015). https://doi.org/10.1007/s12104-014-9556-0

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  • DOI: https://doi.org/10.1007/s12104-014-9556-0

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