Ethylene-regulated dimeric ETR1 kinase reveals multi-site EIN2 docking targeted by peptides that delay climacteric ripening.

Authors

Zhendong He, Yifan Xu, Jinying Shi, Ze Ding, Peng Peng, Yongsen Chen, Qingshan Bill Fu, Wen Chen

Published in

Science advances. Volume 12. Issue 33. Pages eaef8713. Aug 14, 2026. Epub Aug 14, 2026.

Abstract

Ethylene receptors are ER membrane histidine kinases that repress ethylene responses, and the central transducer ETHYLENE INSENSITIVE 2 (EIN2) docks to receptors through its C-terminal tail. Here we express full-length Arabidopsis ETR1 in Pichia pastoris and show that ethylene selectively suppresses the autokinase activity of the dimer, establishing a ligand-responsive receptor preparation. Bio-layer interferometry shows that EIN2-C binds both full-length ETR1 and an isolated transmembrane-GAF module with low-micromolar affinity. NMR mapping of EIN2-C titrated with ETR1-GAF identifies three discrete docking segments, including the known NOP-1 octapeptide and two additional peptides (DP1 and DP2). Synthetic peptides engage ETR1-GAF with distinct kinetics and affinities, and docking models place DP2 in a hydrophobic pocket at the GAF dimer interface. When applied as surface coatings to tomato and mango, these peptides delay ripening in proportion to binding strength. Multi-site competitive inhibition at the EIN2-ETR1 interface thus provides a tunable strategy to modulate ethylene signaling and extend climacteric fruit shelf life.

PMID:
42599998
Bibliographic data and abstract were imported from PubMed on 15 Aug 2026.

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