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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| Veröffentlicht in: | Nature communications Jg. 7; H. 1; S. 12383 |
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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. |
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| 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 |
| Author_xml | – sequence: 1 givenname: Junko surname: Morita fullname: Morita, Junko organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 2 givenname: Kazuki surname: Kato fullname: Kato, Kazuki organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 3 givenname: Takanori surname: Nakane fullname: Nakane, Takanori organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 4 givenname: Yuki surname: Kondo fullname: Kondo, Yuki organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 5 givenname: Hiroo surname: Fukuda fullname: Fukuda, Hiroo organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 6 givenname: Hiroshi surname: Nishimasu fullname: Nishimasu, Hiroshi organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, JST, PRESTO – sequence: 7 givenname: Ryuichiro surname: Ishitani fullname: Ishitani, Ryuichiro email: ishitani@bs.s.u-tokyo.ac.jp organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo – sequence: 8 givenname: Osamu surname: Nureki fullname: Nureki, Osamu email: nureki@bs.s.u-tokyo.ac.jp organization: Department of Biological Sciences, Graduate School of Science, The University of Tokyo |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27498761$$D View this record in MEDLINE/PubMed |
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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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| Title | Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide |
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