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Article

Insights into the Selectivity Mechanisms of Grapevine NIP Aquaporins

1
Linking Landscape, Environment, Agriculture and Food (LEAF), Departmento de Recursos Biológicos, Ambiente e Território (DRAT), Instituto Superior de Agronomia, Universidade de Lisboa, Tapada da Ajuda, 1349-017 Lisbon, Portugal
2
Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, 1649-003 Lisbon, Portugal
3
Leibniz-Institute for Food Systems Biology at the Technical University of Munich, Lise-Meitner-Str. 34, 85354 Freising, Germany
4
Department of Chemistry, Technical University of Munich, Lichtenbergstr. 4, 85748 München, Germany
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(18), 6697; https://doi.org/10.3390/ijms21186697
Received: 21 August 2020 / Revised: 5 September 2020 / Accepted: 10 September 2020 / Published: 13 September 2020
(This article belongs to the Special Issue Channels and Transporters in Cells and Tissues 2.0)
Nodulin 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 with 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 sufficient to interchange their substrate preferences. Further, homology modeling analyses evidenced that variations in the pore radius combined with the differences 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 NIPs. View Full-Text
Keywords: nodulin 26-like intrinsic proteins; grapevine; ar/R selectivity filter; site-directed mutagenesis; substrate selectivity; homology modeling nodulin 26-like intrinsic proteins; grapevine; ar/R selectivity filter; site-directed mutagenesis; substrate selectivity; homology modeling
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MDPI and ACS Style

Sabir, F.; Di Pizio, A.; Loureiro-Dias, M.C.; Casini, A.; Soveral, G.; Prista, C. Insights into the Selectivity Mechanisms of Grapevine NIP Aquaporins. Int. J. Mol. Sci. 2020, 21, 6697. https://doi.org/10.3390/ijms21186697

AMA Style

Sabir F, Di Pizio A, Loureiro-Dias MC, Casini A, Soveral G, Prista C. Insights into the Selectivity Mechanisms of Grapevine NIP Aquaporins. International Journal of Molecular Sciences. 2020; 21(18):6697. https://doi.org/10.3390/ijms21186697

Chicago/Turabian Style

Sabir, Farzana, Antonella Di Pizio, Maria C. Loureiro-Dias, Angela Casini, Graça Soveral, and Catarina Prista. 2020. "Insights into the Selectivity Mechanisms of Grapevine NIP Aquaporins" International Journal of Molecular Sciences 21, no. 18: 6697. https://doi.org/10.3390/ijms21186697

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