Structural and functional insights into the mechanism of action of plant borate transporters

Abstract Boron has essential roles in plant growth and development. BOR proteins are key in the active uptake and distribution of boron, and regulation of intracellular boron concentrations. However, their mechanism of action remains poorly studied. BOR proteins are homologues of the human SLC4 fami...

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Autores principales:	Savvas Saouros, Thotegowdanapalya C. Mohan, Cristina Cecchetti, Silke Lehmann, Joseph D. Barrit, Nicola J. Scull, Paul Simpson, Yilmaz Alguel, Alexander D. Cameron, Alexandra M. E. Jones, Bernadette Byrne
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c2c8b0b5c6a9433dae0794ffd203cba5
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spelling	oai:doaj.org-article:c2c8b0b5c6a9433dae0794ffd203cba52021-12-02T17:38:26ZStructural and functional insights into the mechanism of action of plant borate transporters10.1038/s41598-021-91763-62045-2322https://doaj.org/article/c2c8b0b5c6a9433dae0794ffd203cba52021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91763-6https://doaj.org/toc/2045-2322Abstract Boron has essential roles in plant growth and development. BOR proteins are key in the active uptake and distribution of boron, and regulation of intracellular boron concentrations. However, their mechanism of action remains poorly studied. BOR proteins are homologues of the human SLC4 family of transporters, which includes well studied mammalian transporters such as the human Anion Exchanger 1 (hAE1). Here we generated Arabidopsis thaliana BOR1 (AtBOR1) variants based (i) on known disease causing mutations of hAE1 (S466R, A500R) and (ii) a loss of function mutation (D311A) identified in the yeast BOR protein, ScBOR1p. The AtBOR1 variants express in yeast and localise to the plasma membrane, although both S466R and A500R exhibit lower expression than the WT AtBOR1 and D311A. The D311A, S466R and A500R mutations result in a loss of borate efflux activity in a yeast bor1p knockout strain. A. thaliana plants containing these three individual mutations exhibit substantially decreased growth phenotypes in soil under conditions of low boron. These data confirm an important role for D311 in the function of the protein and show that mutations equivalent to disease-causing mutations in hAE1 have major effects in AtBOR1. We also obtained a low resolution cryo-EM structure of a BOR protein from Oryza sativa, OsBOR3, lacking the 30 C-terminal amino acid residues. This structure confirms the gate and core domain organisation previously observed for related proteins, and is strongly suggestive of an inward facing conformation.Savvas SaourosThotegowdanapalya C. MohanCristina CecchettiSilke LehmannJoseph D. BarritNicola J. ScullPaul SimpsonYilmaz AlguelAlexander D. CameronAlexandra M. E. JonesBernadette ByrneNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Savvas Saouros Thotegowdanapalya C. Mohan Cristina Cecchetti Silke Lehmann Joseph D. Barrit Nicola J. Scull Paul Simpson Yilmaz Alguel Alexander D. Cameron Alexandra M. E. Jones Bernadette Byrne Structural and functional insights into the mechanism of action of plant borate transporters
description	Abstract Boron has essential roles in plant growth and development. BOR proteins are key in the active uptake and distribution of boron, and regulation of intracellular boron concentrations. However, their mechanism of action remains poorly studied. BOR proteins are homologues of the human SLC4 family of transporters, which includes well studied mammalian transporters such as the human Anion Exchanger 1 (hAE1). Here we generated Arabidopsis thaliana BOR1 (AtBOR1) variants based (i) on known disease causing mutations of hAE1 (S466R, A500R) and (ii) a loss of function mutation (D311A) identified in the yeast BOR protein, ScBOR1p. The AtBOR1 variants express in yeast and localise to the plasma membrane, although both S466R and A500R exhibit lower expression than the WT AtBOR1 and D311A. The D311A, S466R and A500R mutations result in a loss of borate efflux activity in a yeast bor1p knockout strain. A. thaliana plants containing these three individual mutations exhibit substantially decreased growth phenotypes in soil under conditions of low boron. These data confirm an important role for D311 in the function of the protein and show that mutations equivalent to disease-causing mutations in hAE1 have major effects in AtBOR1. We also obtained a low resolution cryo-EM structure of a BOR protein from Oryza sativa, OsBOR3, lacking the 30 C-terminal amino acid residues. This structure confirms the gate and core domain organisation previously observed for related proteins, and is strongly suggestive of an inward facing conformation.
format	article
author	Savvas Saouros Thotegowdanapalya C. Mohan Cristina Cecchetti Silke Lehmann Joseph D. Barrit Nicola J. Scull Paul Simpson Yilmaz Alguel Alexander D. Cameron Alexandra M. E. Jones Bernadette Byrne
author_facet	Savvas Saouros Thotegowdanapalya C. Mohan Cristina Cecchetti Silke Lehmann Joseph D. Barrit Nicola J. Scull Paul Simpson Yilmaz Alguel Alexander D. Cameron Alexandra M. E. Jones Bernadette Byrne
author_sort	Savvas Saouros
title	Structural and functional insights into the mechanism of action of plant borate transporters
title_short	Structural and functional insights into the mechanism of action of plant borate transporters
title_full	Structural and functional insights into the mechanism of action of plant borate transporters
title_fullStr	Structural and functional insights into the mechanism of action of plant borate transporters
title_full_unstemmed	Structural and functional insights into the mechanism of action of plant borate transporters
title_sort	structural and functional insights into the mechanism of action of plant borate transporters
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c2c8b0b5c6a9433dae0794ffd203cba5
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Structural and functional insights into the mechanism of action of plant borate transporters

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