A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin

Abstract Auxin levels are tightly regulated within the plant cell, and its storage in the isolated cavity of proteins is a measure adopted by cells to maintain the availability of auxin. We report the first crystal structure of Wrightia tinctoria 11S globulin (WTG) in complex with Indole-3-acetic ac...

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Autores principales:	Pramod Kumar, Pooja Kesari, Sonali Dhindwal, Ashish K. Choudhary, Madhusudhanarao Katiki, Neetu, Aparna Verma, Kiran Ambatipudi, Shailly Tomar, Ashwani Kumar Sharma, Girish Mishra, Pravindra Kumar
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6a003f7855e041b2bdbfdcf9262e3c9d
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spelling	oai:doaj.org-article:6a003f7855e041b2bdbfdcf9262e3c9d2021-12-02T11:52:27ZA novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin10.1038/s41598-017-04518-72045-2322https://doaj.org/article/6a003f7855e041b2bdbfdcf9262e3c9d2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04518-7https://doaj.org/toc/2045-2322Abstract Auxin levels are tightly regulated within the plant cell, and its storage in the isolated cavity of proteins is a measure adopted by cells to maintain the availability of auxin. We report the first crystal structure of Wrightia tinctoria 11S globulin (WTG) in complex with Indole-3-acetic acid (IAA), an auxin, at 1.7 Å resolution. WTG hexamers assemble as a result of the stacking interaction between the hydrophobic surfaces of two trimers, leaving space for the binding of charged ligands. The bound auxin is stabilized by non-covalent interactions, contributed by four chains in each cavity. The presence of bound ligand was confirmed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and high-resolution mass spectrometry (HRMS). Here, we hypothesize that the cleavage of globulins by endopeptidases leads to the movement of the hydrophilic loop region from the surface to the periphery, leaving space for the binding of auxin, and promotes hexamer formation. As the process of germination proceeds, there is a change in the pH, which induces the dissociation of the hexamer and the release of auxin. The compact hexameric assembly ensures the long-term, stable storage of the hormone. This suggests a role for globulin as a novel player in auxin homeostasis.Pramod KumarPooja KesariSonali DhindwalAshish K. ChoudharyMadhusudhanarao KatikiNeetuAparna VermaKiran AmbatipudiShailly TomarAshwani Kumar SharmaGirish MishraPravindra KumarNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Pramod Kumar Pooja Kesari Sonali Dhindwal Ashish K. Choudhary Madhusudhanarao Katiki Neetu Aparna Verma Kiran Ambatipudi Shailly Tomar Ashwani Kumar Sharma Girish Mishra Pravindra Kumar A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
description	Abstract Auxin levels are tightly regulated within the plant cell, and its storage in the isolated cavity of proteins is a measure adopted by cells to maintain the availability of auxin. We report the first crystal structure of Wrightia tinctoria 11S globulin (WTG) in complex with Indole-3-acetic acid (IAA), an auxin, at 1.7 Å resolution. WTG hexamers assemble as a result of the stacking interaction between the hydrophobic surfaces of two trimers, leaving space for the binding of charged ligands. The bound auxin is stabilized by non-covalent interactions, contributed by four chains in each cavity. The presence of bound ligand was confirmed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and high-resolution mass spectrometry (HRMS). Here, we hypothesize that the cleavage of globulins by endopeptidases leads to the movement of the hydrophilic loop region from the surface to the periphery, leaving space for the binding of auxin, and promotes hexamer formation. As the process of germination proceeds, there is a change in the pH, which induces the dissociation of the hexamer and the release of auxin. The compact hexameric assembly ensures the long-term, stable storage of the hormone. This suggests a role for globulin as a novel player in auxin homeostasis.
format	article
author	Pramod Kumar Pooja Kesari Sonali Dhindwal Ashish K. Choudhary Madhusudhanarao Katiki Neetu Aparna Verma Kiran Ambatipudi Shailly Tomar Ashwani Kumar Sharma Girish Mishra Pravindra Kumar
author_facet	Pramod Kumar Pooja Kesari Sonali Dhindwal Ashish K. Choudhary Madhusudhanarao Katiki Neetu Aparna Verma Kiran Ambatipudi Shailly Tomar Ashwani Kumar Sharma Girish Mishra Pravindra Kumar
author_sort	Pramod Kumar
title	A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
title_short	A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
title_full	A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
title_fullStr	A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
title_full_unstemmed	A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin
title_sort	novel function for globulin in sequestering plant hormone: crystal structure of wrightia tinctoria 11s globulin in complex with auxin
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6a003f7855e041b2bdbfdcf9262e3c9d
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A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin

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