Structural basis for receptor recognition of pollen tube attraction peptides.

Structural basis for receptor recognition of pollen tube attraction peptides.
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DOI:
10.1038/s41467-017-01323-8
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发表时间:
2017-11-06
影响因子:
16.6
通讯作者:
Chai J
Chai J
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Zhang X;Liu W;Nagae TT;Takeuchi H;Zhang H;Han Z;Higashiyama T;Chai J

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通过花粉管将不动的精子输送到被胚珠包裹的雌性配子体中,对植物有性生殖具有重要意义。防御素样(DEFL)富含半胱氨酸肽(CRPs) LUREs在花粉管吸引胚珠的过程中起着重要作用,尽管它们的受体仍然存在争议。在这里,我们提供了几条生化证据,表明拟南芥富含亮氨酸的重复受体激酶(LRR-RK) PRK6的胞外结构域直接与AtLURE1肽相互作用。结构研究表明,LRR结构域的c端环(AtPRK6LRR)负责AtLURE1.2的识别,该环由一组在拟南芥和风衣PRK6同源物中大部分保守的残基介导,并得到了体外诱变和半体内花花管生长实验的支持。我们的研究提供了PRK6作为拟南芥中LURE肽受体的证据,并揭示了LRR-RKs独特的配体识别机制。富含半胱氨酸的多肽诱导剂在植物有性生殖中将花粉管吸引到胚珠中起着重要作用。Zhang等人在拟南芥中发现PRK6作为LUREs的受体,并揭示了其配体识别机制。
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 (AtPRK6LRR) 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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