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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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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. |
format | Online Article Text |
id | pubmed-6123649 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
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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