Research Article: Ethylene Receptors Function as Components of High-Molecular-Mass Protein Complexes in Arabidopsis

Date Published: January 8, 2010

Publisher: Public Library of Science

Author(s): Yi-Feng Chen, Zhiyong Gao, Robert J. Kerris, Wuyi Wang, Brad M. Binder, G. Eric Schaller, Karin Schumacher. http://doi.org/10.1371/journal.pone.0008640

Abstract: The gaseous plant hormone ethylene is perceived in Arabidopsis thaliana by a five-member receptor family composed of ETR1, ERS1, ETR2, ERS2, and EIN4.

Partial Text: The gaseous plant hormone ethylene (C2H4) regulates a broad spectrum of developmental and physiological processes including germination, growth, senescence, ripening, and responses to biotic and abiotic stress [1], [2]. In Arabidopsis, ethylene is perceived by a receptor family composed of ETR1, ERS1, ETR2, ERS2, and EIN4 [3], [4], [5]. The ethylene receptors have a similar overall modular structure, each containing three conserved transmembrane domains near the N-terminus, followed by a GAF domain of unknown function, and then signal output motifs in the C-terminal half. Although similar, the ethylene receptors can be divided into two subfamilies based on phylogenetic analysis and some shared structural features, subfamily 1 being composed of ETR1 and ERS1, subfamily 2 being composed of ETR2, ERS2, and EIN4 [3], [5], [6].

Signal transduction involves protein-protein interactions and thus receptors typically function as multicomponent complexes or protein complexes [32], [33]. We find that all five ethylene receptors of Arabidopsis are solubilized from membranes as high-molecular-mass protein complexes, consistent with a protein complex being the functional unit for ethylene perception and signal transduction. Among the types of protein-protein interactions possible in a complex are homo- and hetero-oligomeric interactions, non-obligate and obligate interactions, and transient and permanent interactions [46]. Characterization of the ethylene receptors indicates that multiple types of interactions play roles in formation of the protein complex.

Source:

http://doi.org/10.1371/journal.pone.0008640

 

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