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DOI | 10.1038/s41467-018-06273-3 |
Structural basis for receptor recognition of pollen tube attraction peptides | |
Zhang, Xiaoxiao1; Liu, Weijia1; Nagae, Takuya T.2; Takeuchi, Hidenori3; Zhang, Heqiao1; Han, Zhifu1; Higashiyama, Tetsuya2,4,5; Chai, Jijie1,6,7 | |
2017-11-06 | |
发表期刊 | NATURE COMMUNICATIONS
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ISSN | 2041-1723 |
出版年 | 2017 |
卷号 | 8 |
文章类型 | Article |
语种 | 英语 |
国家 | Peoples R China; Japan; Austria; Germany |
英文摘要 | 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. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000414422100016 |
WOS关键词 | TORENIA-FOURNIERI ; CRYSTAL-STRUCTURE ; SYNERGID CELL ; GUIDANCE ; GROWTH ; ARABIDOPSIS ; PERCEPTION ; ACTIVATION ; COMPLEX ; IDENTIFICATION |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/204012 |
专题 | 资源环境科学 |
作者单位 | 1.Tsinghua Univ, Tsinghua Peking Joint Ctr Sci, Sch Life Sci, Struct Biol Ctr,Minist Educ,Key Lab Prot Sci, Beijing 100084, Peoples R China; 2.Nagoya Univ, Grad Sch Sci, Div Biol Sci, Chikusa Ku, Furo Cho, Nagoya, Aichi 4648602, Japan; 3.Austrian Acad Sci, Vienna Bioctr VBC, Gregor Mendel Inst, Dr Bohr Gasse 3, A-1030 Vienna, Austria; 4.Nagoya Univ, Inst Transformat BioMol ITbM, Chikusa Ku, Furo Cho, Nagoya, Aichi 4648601, Japan; 5.Nagoya Univ, JST ERATO Higashiyama Live Holon Project, Furo Cho, Nagoya, Aichi 4648602, Japan; 6.Max Planck Inst Plant Breeding Res, D-50674 Cologne, Germany; 7.Univ Cologne, Inst Biochem, Zuelpicher Str 47, D-50674 Cologne, Germany |
推荐引用方式 GB/T 7714 | Zhang, Xiaoxiao,Liu, Weijia,Nagae, Takuya T.,et al. Structural basis for receptor recognition of pollen tube attraction peptides[J]. NATURE COMMUNICATIONS,2017,8. |
APA | Zhang, Xiaoxiao.,Liu, Weijia.,Nagae, Takuya T..,Takeuchi, Hidenori.,Zhang, Heqiao.,...&Chai, Jijie.(2017).Structural basis for receptor recognition of pollen tube attraction peptides.NATURE COMMUNICATIONS,8. |
MLA | Zhang, Xiaoxiao,et al."Structural basis for receptor recognition of pollen tube attraction peptides".NATURE COMMUNICATIONS 8(2017). |
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