Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga
Yuqun Xu,
Takuya Miyakawa,
Shohei Nosaki,
Akira Nakamura,
Ying Lyu,
Hidemitsu Nakamura,
Umeharu Ohto,
Hanako Ishida,
Toshiyuki Shimizu,
Tadao Asami and
Masaru Tanokura ()
Additional contact information
Yuqun Xu: The University of Tokyo
Takuya Miyakawa: The University of Tokyo
Shohei Nosaki: The University of Tokyo
Akira Nakamura: The University of Tokyo
Ying Lyu: The University of Tokyo
Hidemitsu Nakamura: The University of Tokyo
Umeharu Ohto: The University of Tokyo
Hanako Ishida: The University of Tokyo
Toshiyuki Shimizu: The University of Tokyo
Tadao Asami: The University of Tokyo
Masaru Tanokura: The University of Tokyo
Nature Communications, 2018, vol. 9, issue 1, 1-11
Abstract:
Abstract HYPOSENSITIVE TO LIGHT (HTL) and DWARF14 (D14) mediate the perception of karrikin and strigolactone, which stimulates germination of the parasitic weed Striga. However, their role in parasitic seeds is poorly understood, and the basis for their differing responsiveness remains unclear. Here, we show that Striga hermonthica HTL proteins (ShHTLs) in ‘conserved’ and ‘intermediate’ clades are able to bind karrikin. The ‘divergent’ clade is able to hydrolyze strigolactone. Unexpectedly, we find that ShD14 is also capable of hydrolyzing strigolactone. Through comparative analysis of ShHTLs and ShD14 crystal structures, we provide insights into the basis for their selectivity. Moreover, we show that both ShD14 and divergent clade ShHTLs, but not conserved and intermediate clade ShHTLs, can interact with the putative downstream signaling component ShMAX2 in the presence of the synthetic strigolactone, rac-GR24. These findings provide insight into how strigolactone is perceived and how ligand specificity is determined.
Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (3)
Downloads: (external link)
https://www.nature.com/articles/s41467-018-06452-2 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06452-2
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-018-06452-2
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().