Cargando…
Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop
The binding of the plant phytohormone Abscisic acid (ABA) to the family of ABA receptors (PYR/PYL/RCAR) triggers plant responses to abiotic stress. Thus, the implementation of genetic or chemical strategies to modulate PYR/PYL activity might be biotechnologically relevant. We have employed the avail...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207482/ https://www.ncbi.nlm.nih.gov/pubmed/35734246 http://dx.doi.org/10.3389/fpls.2022.884029 |
_version_ | 1784729542733070336 |
---|---|
author | Infantes, Lourdes Rivera-Moreno, Maria Daniel-Mozo, Miguel Benavente, Juan Luis Ocaña-Cuesta, Javier Coego, Alberto Lozano-Juste, Jorge Rodriguez, Pedro L. Albert, Armando |
author_facet | Infantes, Lourdes Rivera-Moreno, Maria Daniel-Mozo, Miguel Benavente, Juan Luis Ocaña-Cuesta, Javier Coego, Alberto Lozano-Juste, Jorge Rodriguez, Pedro L. Albert, Armando |
author_sort | Infantes, Lourdes |
collection | PubMed |
description | The binding of the plant phytohormone Abscisic acid (ABA) to the family of ABA receptors (PYR/PYL/RCAR) triggers plant responses to abiotic stress. Thus, the implementation of genetic or chemical strategies to modulate PYR/PYL activity might be biotechnologically relevant. We have employed the available structural information on the PYR/PYL receptors to design SlPYL1, a tomato receptor, harboring a single point mutation that displays enhanced ABA dependent and independent activity. Interestingly, crystallographic studies show that this mutation is not directly involved in ABA recognition or in the downstream phosphatase (PP2C) inhibitory interaction, rather, molecular dynamic based ensemble refinement restrained by crystallographic data indicates that it enhances the conformational variability required for receptor activation and it is involved in the stabilization of an active form of the receptor. Moreover, structural studies on this receptor have led to the identification of niacin as an ABA antagonist molecule in vivo. We have found that niacin blocks the ABA binding site by mimicking ABA receptor interactions, and the niacin interaction inhibits the biochemical activity of the receptor. |
format | Online Article Text |
id | pubmed-9207482 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92074822022-06-21 Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop Infantes, Lourdes Rivera-Moreno, Maria Daniel-Mozo, Miguel Benavente, Juan Luis Ocaña-Cuesta, Javier Coego, Alberto Lozano-Juste, Jorge Rodriguez, Pedro L. Albert, Armando Front Plant Sci Plant Science The binding of the plant phytohormone Abscisic acid (ABA) to the family of ABA receptors (PYR/PYL/RCAR) triggers plant responses to abiotic stress. Thus, the implementation of genetic or chemical strategies to modulate PYR/PYL activity might be biotechnologically relevant. We have employed the available structural information on the PYR/PYL receptors to design SlPYL1, a tomato receptor, harboring a single point mutation that displays enhanced ABA dependent and independent activity. Interestingly, crystallographic studies show that this mutation is not directly involved in ABA recognition or in the downstream phosphatase (PP2C) inhibitory interaction, rather, molecular dynamic based ensemble refinement restrained by crystallographic data indicates that it enhances the conformational variability required for receptor activation and it is involved in the stabilization of an active form of the receptor. Moreover, structural studies on this receptor have led to the identification of niacin as an ABA antagonist molecule in vivo. We have found that niacin blocks the ABA binding site by mimicking ABA receptor interactions, and the niacin interaction inhibits the biochemical activity of the receptor. Frontiers Media S.A. 2022-06-06 /pmc/articles/PMC9207482/ /pubmed/35734246 http://dx.doi.org/10.3389/fpls.2022.884029 Text en Copyright © 2022 Infantes, Rivera-Moreno, Daniel-Mozo, Benavente, Ocaña-Cuesta, Coego, Lozano-Juste, Rodriguez and Albert. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Infantes, Lourdes Rivera-Moreno, Maria Daniel-Mozo, Miguel Benavente, Juan Luis Ocaña-Cuesta, Javier Coego, Alberto Lozano-Juste, Jorge Rodriguez, Pedro L. Albert, Armando Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title | Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title_full | Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title_fullStr | Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title_full_unstemmed | Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title_short | Structure-Based Modulation of the Ligand Sensitivity of a Tomato Dimeric Abscisic Acid Receptor Through a Glu to Asp Mutation in the Latch Loop |
title_sort | structure-based modulation of the ligand sensitivity of a tomato dimeric abscisic acid receptor through a glu to asp mutation in the latch loop |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207482/ https://www.ncbi.nlm.nih.gov/pubmed/35734246 http://dx.doi.org/10.3389/fpls.2022.884029 |
work_keys_str_mv | AT infanteslourdes structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT riveramorenomaria structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT danielmozomiguel structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT benaventejuanluis structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT ocanacuestajavier structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT coegoalberto structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT lozanojustejorge structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT rodriguezpedrol structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop AT albertarmando structurebasedmodulationoftheligandsensitivityofatomatodimericabscisicacidreceptorthroughaglutoaspmutationinthelatchloop |