The Library
Structural and functional insights into the mechanism of action of plant borate transporters
Tools
Saouros, Savvas, Mohan, Thotegowdanapalya C., Cecchetti, Cristina, Lehmann, Silke, Barritt, Joseph D., Scull, Nicola J., Simpson, Paul, Alguel, Yilmaz, Cameron, Alexander D., Jones, Alexandra M. E. and Byrne, Bernadette (2021) Structural and functional insights into the mechanism of action of plant borate transporters. Scientific Reports, 11 (1). 12328. doi:10.1038/s41598-021-91763-6 ISSN 2045-2322.
|
PDF
WRAP-structural-functional-insights-mechanism-action-plant-borate-transporters-2021.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2600Kb) | Preview |
Official URL: http://dx.doi.org/10.1038/s41598-021-91763-6
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.
Item Type: | Journal Article | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry Q Science > QK Botany S Agriculture > SB Plant culture |
|||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||
Library of Congress Subject Headings (LCSH): | Boron, Irrigation water -- Boron content, Plant translocation , Plants, Motion of fluids in | |||||||||
Journal or Publication Title: | Scientific Reports | |||||||||
Publisher: | Nature Publishing Group | |||||||||
ISSN: | 2045-2322 | |||||||||
Official Date: | 10 June 2021 | |||||||||
Dates: |
|
|||||||||
Volume: | 11 | |||||||||
Number: | 1 | |||||||||
Article Number: | 12328 | |||||||||
DOI: | 10.1038/s41598-021-91763-6 | |||||||||
Status: | Peer Reviewed | |||||||||
Publication Status: | Published | |||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||
Date of first compliant deposit: | 11 June 2021 | |||||||||
Date of first compliant Open Access: | 14 June 2021 | |||||||||
RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |
Downloads
Downloads per month over past year