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Molecular Association of the Arabidopsis ETR1 Ethylene Receptor and a Regulator of Ethylene Signaling, RTE1 SCIE SCOPUS

Title
Molecular Association of the Arabidopsis ETR1 Ethylene Receptor and a Regulator of Ethylene Signaling, RTE1
Authors
Dong, CHJang, MScharein, BMalach, ARivarola, MLiesch, JGroth, GHwang, IChang, C
Date Issued
2010-12-24
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Abstract
The plant hormone ethylene plays important roles in growth and development. Ethylene is perceived by a family of membrane-bound receptors that actively repress ethylene responses. When the receptors bind ethylene, their signaling is shut off, activating responses. REVERSION-TO-ETHYLENE SENSITIVITY (RTE1) encodes a novel membrane protein conserved in plants and metazoans. Genetic analyses in Arabidopsis thaliana suggest that RTE1 promotes the signaling state of the ethylene receptor ETR1 through the ETR1 N-terminal domain. RTE1 and ETR1 have been shown to co-localize to the endoplasmic reticulum (ER) and Golgi apparatus in Arabidopsis. Here, we demonstrate a physical association of RTE1 and ETR1 using in vivo and in vitro methods. Interaction of RTE1 and ETR1 was revealed in vivo by bimolecular fluorescence complementation (BiFC) in a tobacco cell transient assay and in stably transformed Arabidopsis. The association was also observed using a truncated version of ETR1 comprising the N terminus (amino acids 1-349). Interaction of RTE1 and ETR1 was confirmed by co-immunoprecipitation from Arabidopsis. The interaction occurs with high affinity (K-d, 117 nM) based on tryptophan fluorescence spectroscopy using purified recombinant RTE1 and a tryptophan-less version of purified recombinant ETR1. An amino acid substitution (C161Y) in RTE1 that is known to confer an ETR1 loss-of-function phenotype correspondingly gives a nearly 12-fold increase in the dissociation constant (K-d, 1.38 mu M). These findings indicate that a high affinity association of RTE1 and ETR1 is important in the regulation of ETR1.
Keywords
BIMOLECULAR FLUORESCENCE COMPLEMENTATION; PROTEIN-PROTEIN INTERACTIONS; HISTIDINE KINASE-ACTIVITY; SUBCELLULAR-LOCALIZATION; ENDOPLASMIC-RETICULUM; ESCHERICHIA-COLI; FAMILY-MEMBERS; GENE FAMILY; THALIANA; BINDING
URI
https://oasis.postech.ac.kr/handle/2014.oak/25155
DOI
10.1074/JBC.M110.146605
ISSN
0021-9258
Article Type
Article
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 285, no. 52, page. 40706 - 40713, 2010-12-24
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황인환HWANG, INHWAN
Dept of Life Sciences
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