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

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 trachear...

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Vydáno v:	Nature communications Ročník 7; číslo 1; s. 12383
Hlavní autoři:	Morita, Junko, Kato, Kazuki, Nakane, Takanori, Kondo, Yuki, Fukuda, Hiroo, Nishimasu, Hiroshi, Ishitani, Ryuichiro, Nureki, Osamu
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 08.08.2016 Nature Publishing Group Nature Portfolio
Témata:	631/449/1741 631/449/2675 631/535/1266 96/33 Amino Acid Sequence Amino acids Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism Cell division Crystal structure Crystallography, X-Ray Flowers & plants Humanities and Social Sciences Kinases Ligands Models, Molecular multidisciplinary Oligopeptides - chemistry Oligopeptides - metabolism Peptides Physiology Plant species Protein Domains Protein Kinases - chemistry Protein Kinases - metabolism Proteins Proteins - chemistry Proteins - metabolism Science Science (multidisciplinary) Japan
ISSN:	2041-1723, 2041-1723
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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. The TDF peptide interacts with the leucine-rich repeat receptor-like kinase TDR to regulate meristem differentiation in plants. Here, the authors solve the structure of the extracellular domain of TDR in complex with TDIF and propose a mechanism for TDIF recognition.
AbstractList	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. The TDF peptide interacts with the leucine-rich repeat receptor-like kinase TDR to regulate meristem differentiation in plants. Here, the authors solve the structure of the extracellular domain of TDR in complex with TDIF and propose a mechanism for TDIF recognition. 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. The TDF peptide interacts with the leucine-rich repeat receptor-like kinase TDR to regulate meristem differentiation in plants. Here, the authors solve the structure of the extracellular domain of TDR in complex with TDIF and propose a mechanism for TDIF recognition.
ArticleNumber	12383
Author	Nishimasu, Hiroshi Nakane, Takanori Nureki, Osamu Kondo, Yuki Kato, Kazuki Fukuda, Hiroo Ishitani, Ryuichiro Morita, Junko
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Snippet	In plants, leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological... The TDF peptide interacts with the leucine-rich repeat receptor-like kinase TDR to regulate meristem differentiation in plants. Here, the authors solve the...
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SubjectTerms	631/449/1741 631/449/2675 631/535/1266 96/33 Amino Acid Sequence Amino acids Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism Cell division Crystal structure Crystallography, X-Ray Flowers & plants Humanities and Social Sciences Kinases Ligands Models, Molecular multidisciplinary Oligopeptides - chemistry Oligopeptides - metabolism Peptides Physiology Plant species Protein Domains Protein Kinases - chemistry Protein Kinases - metabolism Proteins Proteins - chemistry Proteins - metabolism Science Science (multidisciplinary)
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Title	Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide
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