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Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor

Striga hermonthica is a root parasitic plant that infests cereals, decimating yields, particularly in sub‐Saharan Africa. For germination, Striga seeds require host‐released strigolactones that are perceived by the family of HYPOSENSITIVE to LIGHT (ShHTL) receptors. Inhibiting seed germination would...

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Autores principales: Shahul Hameed, Umar, Haider, Imran, Jamil, Muhammad, Kountche, Boubacar A, Guo, Xianrong, Zarban, Randa A, Kim, Dongjin, Al‐Babili, Salim, Arold, Stefan T
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123649/
https://www.ncbi.nlm.nih.gov/pubmed/30021834
http://dx.doi.org/10.15252/embr.201745619
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author Shahul Hameed, Umar
Haider, Imran
Jamil, Muhammad
Kountche, Boubacar A
Guo, Xianrong
Zarban, Randa A
Kim, Dongjin
Al‐Babili, Salim
Arold, Stefan T
author_facet Shahul Hameed, Umar
Haider, Imran
Jamil, Muhammad
Kountche, Boubacar A
Guo, Xianrong
Zarban, Randa A
Kim, Dongjin
Al‐Babili, Salim
Arold, Stefan T
author_sort Shahul Hameed, Umar
collection PubMed
description Striga hermonthica is a root parasitic plant that infests cereals, decimating yields, particularly in sub‐Saharan Africa. For germination, Striga seeds require host‐released strigolactones that are perceived by the family of HYPOSENSITIVE to LIGHT (ShHTL) receptors. Inhibiting seed germination would thus be a promising approach for combating Striga. However, there are currently no strigolactone antagonists that specifically block ShHTLs and do not bind to DWARF14, the homologous strigolactone receptor of the host. Here, we show that the octyl phenol ethoxylate Triton X‐100 inhibits S. hermonthica seed germination without affecting host plants. High‐resolution X‐ray structures reveal that Triton X‐100 specifically plugs the catalytic pocket of ShHTL7. ShHTL7‐specific inhibition by Triton X‐100 demonstrates the dominant role of this particular ShHTL receptor for Striga germination. Our structural analysis provides a rationale for the broad specificity and high sensitivity of ShHTL7, and reveals that strigolactones trigger structural changes in ShHTL7 that are required for downstream signaling. Our findings identify Triton and the related 2‐[4‐(2,4,4‐trimethylpentan‐2‐yl)phenoxy]acetic acid as promising lead compounds for the rational design of efficient Striga‐specific herbicides.
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spelling pubmed-61236492018-09-10 Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor Shahul Hameed, Umar Haider, Imran Jamil, Muhammad Kountche, Boubacar A Guo, Xianrong Zarban, Randa A Kim, Dongjin Al‐Babili, Salim Arold, Stefan T EMBO Rep Articles Striga hermonthica is a root parasitic plant that infests cereals, decimating yields, particularly in sub‐Saharan Africa. For germination, Striga seeds require host‐released strigolactones that are perceived by the family of HYPOSENSITIVE to LIGHT (ShHTL) receptors. Inhibiting seed germination would thus be a promising approach for combating Striga. However, there are currently no strigolactone antagonists that specifically block ShHTLs and do not bind to DWARF14, the homologous strigolactone receptor of the host. Here, we show that the octyl phenol ethoxylate Triton X‐100 inhibits S. hermonthica seed germination without affecting host plants. High‐resolution X‐ray structures reveal that Triton X‐100 specifically plugs the catalytic pocket of ShHTL7. ShHTL7‐specific inhibition by Triton X‐100 demonstrates the dominant role of this particular ShHTL receptor for Striga germination. Our structural analysis provides a rationale for the broad specificity and high sensitivity of ShHTL7, and reveals that strigolactones trigger structural changes in ShHTL7 that are required for downstream signaling. Our findings identify Triton and the related 2‐[4‐(2,4,4‐trimethylpentan‐2‐yl)phenoxy]acetic acid as promising lead compounds for the rational design of efficient Striga‐specific herbicides. John Wiley and Sons Inc. 2018-07-18 2018-09 /pmc/articles/PMC6123649/ /pubmed/30021834 http://dx.doi.org/10.15252/embr.201745619 Text en © 2018 The Authors. Published under the terms of the CC BY 4.0 license This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Shahul Hameed, Umar
Haider, Imran
Jamil, Muhammad
Kountche, Boubacar A
Guo, Xianrong
Zarban, Randa A
Kim, Dongjin
Al‐Babili, Salim
Arold, Stefan T
Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title_full Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title_fullStr Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title_full_unstemmed Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title_short Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor
title_sort structural basis for specific inhibition of the highly sensitive shhtl7 receptor
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123649/
https://www.ncbi.nlm.nih.gov/pubmed/30021834
http://dx.doi.org/10.15252/embr.201745619
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