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Title: Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions

Abstract

Tracheary Element Differentiation Inhibitory Factor (TDIF) belongs to the family of post-translationally modified CLE (CLAVATA3/embryo surrounding region (ESR)-related) peptide hormones that control root growth and define the delicate balance between stem cell proliferation and differentiation in SAM (shoot apical meristem) or RAM (root apical meristem). In Arabidopsis, Tracheary Element Differentiation Inhibitory Factor Receptor (TDR) and its ligand TDIF signaling pathway is involved in the regulation of procambial cell proliferation and inhibiting its differentiation into xylem cells. Here we present the crystal structures of the extracellular domains (ECD) of TDR alone and in complex with its ligand TDIF resolved at 2.65 Åand 2.75 Å respectively. These structures provide insights about the ligand perception and specific interactions between the CLE peptides and their cognate receptors. Our in vitro biochemical studies indicate that the interactions between the ligands and the receptors at the C-terminal anchoring site provide conserved binding. While the binding interactions occurring at the N-terminal anchoring site dictate differential binding specificities between different ligands and receptors. Our studies will open different unknown avenues of TDR-TDIF signaling pathways that will enhance our knowledge in this field highlighting the receptor ligand interaction, receptor activation, signaling network, modes of action and will serve asmore » a structure function relationship model between the ligand and the receptor for various similar leucine-rich repeat receptor-like kinases (LRR-RLKs).« less

Authors:
; ; ORCiD logo;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1355045
Resource Type:
Journal Article
Resource Relation:
Journal Name: PLoS ONE; Journal Volume: 12; Journal Issue: 4
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Li, Zhijie, Chakraborty, Sayan, Xu, Guozhou, and Kobe, Bostjan. Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions. United States: N. p., 2017. Web. doi:10.1371/journal.pone.0175317.
Li, Zhijie, Chakraborty, Sayan, Xu, Guozhou, & Kobe, Bostjan. Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions. United States. doi:10.1371/journal.pone.0175317.
Li, Zhijie, Chakraborty, Sayan, Xu, Guozhou, and Kobe, Bostjan. Thu . "Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions". United States. doi:10.1371/journal.pone.0175317.
@article{osti_1355045,
title = {Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions},
author = {Li, Zhijie and Chakraborty, Sayan and Xu, Guozhou and Kobe, Bostjan},
abstractNote = {Tracheary Element Differentiation Inhibitory Factor (TDIF) belongs to the family of post-translationally modified CLE (CLAVATA3/embryo surrounding region (ESR)-related) peptide hormones that control root growth and define the delicate balance between stem cell proliferation and differentiation in SAM (shoot apical meristem) or RAM (root apical meristem). In Arabidopsis, Tracheary Element Differentiation Inhibitory Factor Receptor (TDR) and its ligand TDIF signaling pathway is involved in the regulation of procambial cell proliferation and inhibiting its differentiation into xylem cells. Here we present the crystal structures of the extracellular domains (ECD) of TDR alone and in complex with its ligand TDIF resolved at 2.65 Åand 2.75 Å respectively. These structures provide insights about the ligand perception and specific interactions between the CLE peptides and their cognate receptors. Our in vitro biochemical studies indicate that the interactions between the ligands and the receptors at the C-terminal anchoring site provide conserved binding. While the binding interactions occurring at the N-terminal anchoring site dictate differential binding specificities between different ligands and receptors. Our studies will open different unknown avenues of TDR-TDIF signaling pathways that will enhance our knowledge in this field highlighting the receptor ligand interaction, receptor activation, signaling network, modes of action and will serve as a structure function relationship model between the ligand and the receptor for various similar leucine-rich repeat receptor-like kinases (LRR-RLKs).},
doi = {10.1371/journal.pone.0175317},
journal = {PLoS ONE},
number = 4,
volume = 12,
place = {United States},
year = {Thu Apr 06 00:00:00 EDT 2017},
month = {Thu Apr 06 00:00:00 EDT 2017}
}
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