Details
| Original language | English |
|---|---|
| Article number | e15075 |
| Journal | ELIFE |
| Volume | 5 |
| Issue number | April 2016 |
| Publication status | Published - 8 Apr 2016 |
Abstract
Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.
ASJC Scopus subject areas
- Neuroscience(all)
- General Neuroscience
- Immunology and Microbiology(all)
- General Immunology and Microbiology
- Biochemistry, Genetics and Molecular Biology(all)
- General Biochemistry,Genetics and Molecular Biology
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In: ELIFE, Vol. 5, No. April 2016, e15075, 08.04.2016.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission
AU - Santiago, Julia
AU - Brandt, Benjamin
AU - Wildhagen, Mari
AU - Hohmann, Ulrich
AU - Hothorn, Ludwig A.
AU - Butenko, Melinka A.
AU - Hothorn, Michael
N1 - Funding Information: Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung 31003A_156920 Michael Hothorn Human Frontier Science Program CDA00057/2012 Michael Hothorn European Molecular Biology Organization YIP2904 Michael Hothorn Norges Forskningsrad 13785/F20,230849/ F20,348256/F20 Melinka A Butenko European Molecular Biology Organization ALTF 913-2014 Benjamin Brandt European Molecular Biology Organization ALTF 169-2013, 1673-2014 Julia Santiago.
PY - 2016/4/8
Y1 - 2016/4/8
N2 - Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.
AB - Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.
UR - http://www.scopus.com/inward/record.url?scp=84969150862&partnerID=8YFLogxK
U2 - 10.7554/eLife.15075
DO - 10.7554/eLife.15075
M3 - Article
C2 - 27058169
AN - SCOPUS:84969150862
VL - 5
JO - ELIFE
JF - ELIFE
SN - 2050-084X
IS - April 2016
M1 - e15075
ER -