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Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga
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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158167/ https://www.ncbi.nlm.nih.gov/pubmed/30258184 http://dx.doi.org/10.1038/s41467-018-06452-2 |
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author | Xu, Yuqun Miyakawa, Takuya Nosaki, Shohei Nakamura, Akira Lyu, Ying Nakamura, Hidemitsu Ohto, Umeharu Ishida, Hanako Shimizu, Toshiyuki Asami, Tadao Tanokura, Masaru |
author_facet | Xu, Yuqun Miyakawa, Takuya Nosaki, Shohei Nakamura, Akira Lyu, Ying Nakamura, Hidemitsu Ohto, Umeharu Ishida, Hanako Shimizu, Toshiyuki Asami, Tadao Tanokura, Masaru |
author_sort | Xu, Yuqun |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6158167 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61581672018-10-01 Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga Xu, Yuqun Miyakawa, Takuya Nosaki, Shohei Nakamura, Akira Lyu, Ying Nakamura, Hidemitsu Ohto, Umeharu Ishida, Hanako Shimizu, Toshiyuki Asami, Tadao Tanokura, Masaru Nat Commun Article 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. Nature Publishing Group UK 2018-09-26 /pmc/articles/PMC6158167/ /pubmed/30258184 http://dx.doi.org/10.1038/s41467-018-06452-2 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Xu, Yuqun Miyakawa, Takuya Nosaki, Shohei Nakamura, Akira Lyu, Ying Nakamura, Hidemitsu Ohto, Umeharu Ishida, Hanako Shimizu, Toshiyuki Asami, Tadao Tanokura, Masaru Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title | Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title_full | Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title_fullStr | Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title_full_unstemmed | Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title_short | Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga |
title_sort | structural analysis of htl and d14 proteins reveals the basis for ligand selectivity in striga |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158167/ https://www.ncbi.nlm.nih.gov/pubmed/30258184 http://dx.doi.org/10.1038/s41467-018-06452-2 |
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