Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide.

Junko Morita,Hiroshi Nishimasu,Takanori Nakane,Kazuki Kato,Ryuichiro Ishitani,Osamu Nureki,Hiroo Fukuda,Yuki Kondo

doi:10.1038/ncomms12383

Junko Morita, Hiroshi Nishimasu + Show 6 more

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https://doi.org/10.1038/ncomms12383

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Journal: Nature communications	Publication Date: Aug 8, 2016
Citations: 66	License type: CC BY 4.0

Affiliation: The University of Tokyo

Abstract

In plants, leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological processes. TDIF, a member of the CLE peptide family, specifically interacts with the LRR-RK TDR to inhibit meristem differentiation into tracheary elements, and promotes cell proliferation. Here we report the crystal structure of the extracellular domain of TDR in complex with the TDIF peptide. The extracellular domain of TDR adopts a superhelical structure comprising 22 LRRs, and specifically recognizes TDIF by its inner concave surface. Together with our biochemical and sequence analyses, our structure reveals a conserved TDIF-recognition mechanism of TDR among plant species. Furthermore, a structural comparison of TDR with other plant LRR-RKs suggested the activation mechanism of TDR by TDIF. The structure of this CLE peptide receptor provides insights into the recognition mechanism of the CLE family peptides.

Highlights

In plants, leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological processes
To measure the signalling activity of the C259A/C540S mutant, we reconstructed the Tracheary element differentiation factor (TDIF)–TDR–BIN2 pathway in Nicotiana benthamiana leaves with TDR or its mutants fused with the cyan fluorescent protein (TDR–CFP), together with BIN2 fused with the yellow fluorescent protein (BIN2–YFP), as previously described[11] (Supplementary Fig. 1b,c)
While our manuscript was under revision, Zhang et al.[23] reported the crystal structure of TDR–TDIF, which is essentially identical to our structure, confirming the functional relevance of the TDIF-recognition mechanism of TDR

Summary

Introduction

Leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological processes. TDIF, a member of the CLE peptide family, interacts with the LRR-RK TDR to inhibit meristem differentiation into tracheary elements, and promotes cell proliferation. A structural comparison of TDR with other plant LRR-RKs suggested the activation mechanism of TDR by TDIF The structure of this CLE peptide receptor provides insights into the recognition mechanism of the CLE family peptides. The CLE peptides are secreted into the apoplast, after proteolytic processing and posttranslational modifications They mainly interact with the extracellular regions of membrane associated leucine-rich receptor kinases (LRR-RKs), thereby triggering intracellular signalling cascades[2,8]. In conjunction with the structure-guided functional analysis, our results provide structural insights into the mechanism of TDIF recognition by TDR

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