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Insights into the selectivity mechanisms of grapevine NIP aquaporins

2020Journal article Open access
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dc.contributor.authorSabir, Farzana
dc.contributor.authorDi Pizzio, Antonella
dc.contributor.authorLoureiro-Dias, M. C.
dc.contributor.authorCasini, Angela
dc.contributor.authorSoveral, Graça
dc.contributor.authorPrista, Catarina
dc.date.accessioned2020-09-24T13:26:13Z
dc.date.available2020-09-24T13:26:13Z
dc.date.issued2020
dc.description.abstractNodulin 26-like intrinsic proteins (NIPs) of the plant aquaporin family majorly facilitate the transport of physiologically relevant solutes. The present study intended to investigate how substrate selectivity in grapevine NIPs is influenced by the aromatic/arginine (ar/R) selectivity filter within the pore and the possible underlying mechanisms. A mutational approach was used to interchange the ar/R residues between grapevine NIPs (VvTnNIP1;1 withUniversidade de Lisboa, VvTnNIP6;1, and VvTnNIP2;1 with VvTnNIP5;1). Their functional characterization by stopped-flow spectroscopy in Saccharomyces cerevisiae revealed that mutations in residues of H2/H5 helices in VvTnNIP1;1 and VvTnNIP6;1 caused a general decline in membrane glycerol permeability but did not impart the expected substrate conductivity in the mutants. This result suggests that ar/R filter substitution could alter the NIP channel activity, but it was not su cient to interchange their substrate preferences. Further, homology modeling analyses evidenced that variations in the pore radius combined with the di erences in the channel’s physicochemical properties (hydrophilicity/hydrophobicity) may drive substrate selectivity. Furthermore, yeast growth assays showed that H5 residue substitution alleviated the sensitivity of VvTnNIP2;1 and VvTnNIP5;1 to As, B, and Se, implying importance of H5 sequence for substrate selection. These results contribute to the knowledge of the overall determinants of substrate selectivity in NIPspt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationInt. J. Mol. Sci. 2020, 21, 6697pt_PT
dc.identifier.doi10.3390/ijms21186697pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.5/20391
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relation.publisherversionwww.mdpi.com/journal/ijmspt_PT
dc.subjectnodulin 26-like intrinsic proteinspt_PT
dc.subjectgrapevinept_PT
dc.subjectar/R selectivity filterpt_PT
dc.subjectsite-directed mutagenesispt_PT
dc.subjectsubstrate selectivitypt_PT
dc.subjecthomology modelingpt_PT
dc.titleInsights into the selectivity mechanisms of grapevine NIP aquaporinspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.titleInternational Journal of Molecular Sciencespt_PT
person.familyNameLoureiro-Dias
person.familyNamePrista
person.givenNameMaria
person.givenNameCatarina
person.identifier23269
person.identifier.ciencia-id3C19-C25A-182D
person.identifier.orcid0000-0002-6340-2416
person.identifier.orcid0000-0001-9307-1905
person.identifier.ridN-7331-2013
person.identifier.ridN-7079-2013
person.identifier.scopus-author-id7003888372
person.identifier.scopus-author-id6603433211
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication718c0dc9-c89f-444d-97fc-b8aa6f1edb57
relation.isAuthorOfPublication344c4593-4c36-41ca-ab28-8ea76f20c5b5
relation.isAuthorOfPublication.latestForDiscovery344c4593-4c36-41ca-ab28-8ea76f20c5b5

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