High-Resolution Crystal Structure of Arabidopsis FLOWERING LOCUS T Illuminates Its Phospholipid-Binding Site in Flowering

Yuki Nakamura, Ying Chen Lin, Satoshi Watanabe, Yu chi Liu, Kentaro Katsuyama, Kazue Kanehara, Kenji Inaba

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Arabidopsis FLOWERING LOCUS T (FT) is a pivotal component of florigen, a long-range mobile flowering signal. Here, we determined the 1.0 Å-resolution crystal structure of FT, a significantly higher-resolution crystal structure of FT than previously reported one (2.6 Å). The present crystallographic studies revealed 4 alternative configurations with the precise location of the surrounding water molecules. Using this structural data, computational docking simulation predicted the putative binding sites for phosphatidylcholine (PC), an endogenous ligand that interacts with FT to modulate flowering time. In vitro reconstitution of the lipid–protein interaction showed that mutations at two of the predicted sites significantly compromised the lipid binding ability of FT. In planta, one of the mutant FT proteins significantly affected FT function in flowering, emphasizing the involvement of PC binding in modulating FT function. Our structural, biochemical, and transgenic analyses reveal the molecular mechanism of PC binding in FT-mediated flowering time control.

Original languageEnglish
Pages (from-to)577-586
Number of pages10
JournaliScience
Volume21
DOIs
Publication statusPublished - 2019 Nov 22

Keywords

  • Biological Sciences
  • Plant Biochemistry
  • Plant Biology
  • Structural Biology

ASJC Scopus subject areas

  • General

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