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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:
 [1];  [1]; ORCiD logo [1];  [2]
  1. North Carolina State Univ., Raleigh, NC (United States)
  2. Univ. of Queensland (Australia)
Publication Date:
Research Org.:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1355045
Resource Type:
Accepted Manuscript
Journal Name:
PLoS ONE
Additional Journal Information:
Journal Volume: 12; Journal Issue: 4; Journal ID: ISSN 1932-6203
Publisher:
Public Library of Science
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; Crystal structure; Arabidopsis thaliana; Alanine; Sequence alignment; Molecular structure; Sequence motif analysis; Cell differentiation; Histidine

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. https://doi.org/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. https://doi.org/10.1371/journal.pone.0175317. https://www.osti.gov/servlets/purl/1355045.
@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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Cited by: 11 works
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Works referencing / citing this record:

CLE peptide-mediated signaling in shoot and vascular meristem development
journal, December 2017


The Extracellular Domain of Pollen Receptor Kinase 3 is structurally similar to the SERK family of co-receptors
journal, February 2018


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The Extracellular Domain of Pollen Receptor Kinase 3 is structurally similar to the SERK family of co-receptors
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