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Structural basis for receptor recognition of pollen tube attraction peptides
Transportation of the immobile sperms directed by pollen tubes to the ovule-enclosed female gametophytes is important for plant sexual reproduction. The defensin-like (DEFL) cysteine-rich peptides (CRPs) LUREs play an essential role in pollen tube attraction to the ovule, though their receptors stil...
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Published in: | Nature communications 2017-11, Vol.8 (1), p.1331-9, Article 1331 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Transportation of the immobile sperms directed by pollen tubes to the ovule-enclosed female gametophytes is important for plant sexual reproduction. The defensin-like (DEFL) cysteine-rich peptides (CRPs) LUREs play an essential role in pollen tube attraction to the ovule, though their receptors still remain controversial. Here we provide several lines of biochemical evidence showing that the extracellular domain of the leucine-rich repeat receptor kinase (LRR-RK) PRK6 from
Arabidopsis thaliana
directly interacts with AtLURE1 peptides. Structural study reveals that a C-terminal loop of the LRR domain (AtPRK6
LRR
) is responsible for recognition of AtLURE1.2, mediated by a set of residues largely conserved among PRK6 homologs from
Arabidopsis lyrata
and
Capsella rubella
, supported by in vitro mutagenesis and semi-in-vivo pollen tube growth assays. Our study provides evidence showing that PRK6 functions as a receptor of the LURE peptides in
A. thaliana
and reveals a unique ligand recognition mechanism of LRR-RKs.
The cysteine-rich peptides LUREs play an essential role in pollen tube attraction to the ovule for plant sexual reproduction. Here Zhang et al. show that PRK6 functions as a receptor of the LUREs in
Arabidopsis thaliana
and reveal the ligand recognition mechanism. |
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ISSN: | 2041-1723 2041-1723 |
DOI: | 10.1038/s41467-017-01323-8 |