Barley Nodulin 26-like intrinsic protein permeates water, metalloids, saccharides, and ion pairs due to structural plasticity and diversification

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dc.contributor.authorVenkataraghavan, A.
dc.contributor.authorSchwerdt, J.G.
dc.contributor.authorTyerman, S.D.
dc.contributor.authorHrmova, M.
dc.date.issued2023
dc.descriptionPublished, Papers in Press, October 31, 2023,
dc.description.abstractAquaporins can facilitate the passive movement of water, small polar molecules and some ions. Here, we examined solute selectivity for the barley Nodulin 26-like Intrinsic Protein (HvNIP2;1) embedded in liposomes and examined through stopped-flow light scattering spectrophotometry and Xenopus laevis oocyte swelling assays. We found that HvNIP2;1 permeates water, boric and germanic acids, sucrose, and lactose but not d-glucose or d-fructose. Other saccharides, such as neutral (d-mannose, d-galactose, d-xylose, d-mannoheptaose) and charged (N-acetyl d-glucosamine, d-glucosamine, d-glucuronic acid) aldoses, disaccharides (cellobiose, gentiobiose, trehalose), trisaccharide raffinose, and urea, glycerol, and acyclic polyols were permeated to a much lower extent. We observed apparent permeation of hydrated KCl and MgSO4 ions, while CH3COONa and NaNO3 permeated at significantly lower rates. Our experiments with boric acid and sucrose revealed no apparent interaction between solutes when permeated together, and AgNO3 or H[AuCl4] blocked the permeation of all solutes. Docking of sucrose in HvNIP2;1 and spinach water-selective SoPIP2;1 aquaporins revealed the structural basis for sucrose permeation in HvNIP2;1 but not in SoPIP2;1, and defined key residues interacting with this permeant. In a biological context, sucrose transport could constitute a novel element of plant saccharide-transporting machinery. Phylogenomic analyses of 164 Viridiplantae and 2,993 Archaean, bacterial, fungal, and Metazoan aquaporins rationalized solute poly-selectivity in NIP3 sub-clade entries and suggested that they diversified from other sub-clades to acquire a unique specificity of saccharide transporters. Solute specificity definition in NIP aquaporins could inspire developing plants for food production.
dc.description.statementofresponsibilityAkshayaa Venkataraghavan, Julian G. Schwerdt, Stephen D. Tyerman, Maria Hrmova
dc.identifier.citationJournal of Biological Chemistry, 2023; 299(12):105410-1-105410-14
dc.identifier.doi10.1016/j.jbc.2023.105410
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.orcidSchwerdt, J.G. [0000-0002-0476-031X]
dc.identifier.orcidTyerman, S.D. [0000-0003-2455-1643]
dc.identifier.orcidHrmova, M. [0000-0002-3545-0605]
dc.identifier.urihttps://hdl.handle.net/2440/139878
dc.language.isoen
dc.publisherElsevier
dc.relation.granthttp://purl.org/au-research/grants/arc/DP120100900
dc.relation.granthttp://purl.org/au-research/grants/arc/CE1400008
dc.rights© 2023 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article distributed under the terms of the Creative Commons CC-BY license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.source.urihttps://doi.org/10.1016/j.jbc.2023.105410
dc.subject3D molecular modelling of aquaporins
dc.subjectheterologous protein expression
dc.subjectphylogenomics
dc.subjectsolute permeation selectivity
dc.subjectstopped-flow spectrophotometry
dc.titleBarley Nodulin 26-like intrinsic protein permeates water, metalloids, saccharides, and ion pairs due to structural plasticity and diversification
dc.typeJournal article
pubs.publication-statusPublished

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