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Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1

The phytohormone gibberellin and the DELLA proteins act together to control key aspects of plant development. Gibberellin induces degradation of DELLA proteins by recruitment of an F-box protein using a molecular switch: a gibberellin-bound nuclear receptor interacts with the N-terminal domain of DE...

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Autores principales: Sheerin, David J., Buchanan, Jeremy, Kirk, Chris, Harvey, Dawn, Sun, Xiaolin, Spagnuolo, Julian, Li, Sheng, Liu, Tong, Woods, Virgil A., Foster, Toshi, Jones, William T., Rakonjac, Jasna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195444/
https://www.ncbi.nlm.nih.gov/pubmed/21323638
http://dx.doi.org/10.1042/BJ20101941
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author Sheerin, David J.
Buchanan, Jeremy
Kirk, Chris
Harvey, Dawn
Sun, Xiaolin
Spagnuolo, Julian
Li, Sheng
Liu, Tong
Woods, Virgil A.
Foster, Toshi
Jones, William T.
Rakonjac, Jasna
author_facet Sheerin, David J.
Buchanan, Jeremy
Kirk, Chris
Harvey, Dawn
Sun, Xiaolin
Spagnuolo, Julian
Li, Sheng
Liu, Tong
Woods, Virgil A.
Foster, Toshi
Jones, William T.
Rakonjac, Jasna
author_sort Sheerin, David J.
collection PubMed
description The phytohormone gibberellin and the DELLA proteins act together to control key aspects of plant development. Gibberellin induces degradation of DELLA proteins by recruitment of an F-box protein using a molecular switch: a gibberellin-bound nuclear receptor interacts with the N-terminal domain of DELLA proteins, and this event primes the DELLA C-terminal domain for interaction with the F-box protein. However, the mechanism of signalling between the N- and C-terminal domains of DELLA proteins is unresolved. In the present study, we used in vivo and in vitro approaches to characterize di- and tri-partite interactions of the DELLA protein RGL1 (REPRESSOR OF GA1-3-LIKE 1) of Arabidopsis thaliana with the gibberellin receptor GID1A (GIBBERELLIC ACID-INSENSITIVE DWARF-1A) and the F-box protein SLY1 (SLEEPY1). Deuterium-exchange MS unequivocally showed that the entire N-terminal domain of RGL1 is disordered prior to interaction with the GID1A; furthermore, association/dissociation kinetics, determined by surface plasmon resonance, predicts a two-state conformational change of the RGL1 N-terminal domain upon interaction with GID1A. Additionally, competition assays with monoclonal antibodies revealed that contacts mediated by the short helix Asp-Glu-Leu-Leu of the hallmark DELLA motif are not essential for the GID1A–RGL1 N-terminal domain interaction. Finally, yeast two- and three-hybrid experiments determined that unabated communication between N- and C-terminal domains of RGL1 is required for recruitment of the F-box protein SLY1.
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spelling pubmed-31954442011-11-01 Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1 Sheerin, David J. Buchanan, Jeremy Kirk, Chris Harvey, Dawn Sun, Xiaolin Spagnuolo, Julian Li, Sheng Liu, Tong Woods, Virgil A. Foster, Toshi Jones, William T. Rakonjac, Jasna Biochem J Research Article The phytohormone gibberellin and the DELLA proteins act together to control key aspects of plant development. Gibberellin induces degradation of DELLA proteins by recruitment of an F-box protein using a molecular switch: a gibberellin-bound nuclear receptor interacts with the N-terminal domain of DELLA proteins, and this event primes the DELLA C-terminal domain for interaction with the F-box protein. However, the mechanism of signalling between the N- and C-terminal domains of DELLA proteins is unresolved. In the present study, we used in vivo and in vitro approaches to characterize di- and tri-partite interactions of the DELLA protein RGL1 (REPRESSOR OF GA1-3-LIKE 1) of Arabidopsis thaliana with the gibberellin receptor GID1A (GIBBERELLIC ACID-INSENSITIVE DWARF-1A) and the F-box protein SLY1 (SLEEPY1). Deuterium-exchange MS unequivocally showed that the entire N-terminal domain of RGL1 is disordered prior to interaction with the GID1A; furthermore, association/dissociation kinetics, determined by surface plasmon resonance, predicts a two-state conformational change of the RGL1 N-terminal domain upon interaction with GID1A. Additionally, competition assays with monoclonal antibodies revealed that contacts mediated by the short helix Asp-Glu-Leu-Leu of the hallmark DELLA motif are not essential for the GID1A–RGL1 N-terminal domain interaction. Finally, yeast two- and three-hybrid experiments determined that unabated communication between N- and C-terminal domains of RGL1 is required for recruitment of the F-box protein SLY1. Portland Press Ltd. 2011-04-13 2011-05-01 /pmc/articles/PMC3195444/ /pubmed/21323638 http://dx.doi.org/10.1042/BJ20101941 Text en © yyyy The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Sheerin, David J.
Buchanan, Jeremy
Kirk, Chris
Harvey, Dawn
Sun, Xiaolin
Spagnuolo, Julian
Li, Sheng
Liu, Tong
Woods, Virgil A.
Foster, Toshi
Jones, William T.
Rakonjac, Jasna
Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title_full Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title_fullStr Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title_full_unstemmed Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title_short Inter- and intra-molecular interactions of Arabidopsis thaliana DELLA protein RGL1
title_sort inter- and intra-molecular interactions of arabidopsis thaliana della protein rgl1
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195444/
https://www.ncbi.nlm.nih.gov/pubmed/21323638
http://dx.doi.org/10.1042/BJ20101941
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