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  3. FCEN - Facultad de Ciencias Exactas y Naturales. UBA
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dc.provenanceFacultad de Ciencias Exactas y Naturales de la UBA-
dc.contributorJozefkowicz, C.-
dc.contributorRosi, P.-
dc.contributor<div class="autor_fcen" id="8094">Sigaut, L.</div>-
dc.contributor<div class="autor_fcen" id="8253">Soto, G.</div>-
dc.contributorPietrasanta, L.I.-
dc.contributorAmodeo, G.-
dc.contributorAlleva, K.-
dc.creatorJozefkowicz, C.-
dc.creatorRosi, P.-
dc.creator<div class="autor_fcen" id="8094">Sigaut, L.</div>-
dc.creator<div class="autor_fcen" id="8253">Soto, G.</div>-
dc.creatorPietrasanta, L.I.-
dc.creatorAmodeo, G.-
dc.creatorAlleva, K.-
dc.date.accessioned2018-05-04T22:05:26Z-
dc.date.accessioned2018-05-28T15:49:25Z-
dc.date.available2018-05-04T22:05:26Z-
dc.date.available2018-05-28T15:49:25Z-
dc.date.issued2013-
dc.identifier.urihttp://10.0.0.11:8080/jspui/handle/bnmm/68643-
dc.descriptionResearch done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not completely elucidated. In this work we unveil some features of monomer-monomer interaction in Beta vulgaris PIP aquaporins. Our results show that while BvPIP2;2 is able to interact with BvPIP1;1, BvPIP2;1 shows no functional interaction. The lack of functional interaction between BvPIP2;1 and BvPIP1;1 was further corroborated by dose-response curves of water permeability due to aquaporin activity exposed to different acidic conditions. We also found that BvPIP2;1 is unable to translocate BvPIP1;1-ECFP from an intracellular position to the plasma membrane when co-expressed, as BvPIP2;2 does. Moreover we postulate that the first extracellular loop (loop A) of BvPIP2;1, could be relevant for the functional interaction with BvPIP1;1. Thus, we investigate BvPIP2;1 loop A at an atomic level by Molecular Dynamics Simulation (MDS) and by direct mutagenesis. We found that, within the tetramer, each loop A presents a dissimilar behavior. Besides, BvPIP2;1 loop A mutants restore functional interaction with BvPIP1;1. This work is a contribution to unravel how PIP2 and PIP1 interact to form functional heterooligomeric assemblies. We postulate that BvPIP2;1 loop A is relevant for the lack of functional interaction with BvPIP1;1 and that the monomer composition of PIP assemblies determines their functional properties. © 2013 Jozefkowicz et al.-
dc.descriptionFil:Sigaut, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttp://creativecommons.org/licenses/by/2.5/ar-
dc.sourcePLoS ONE 2013;8(3)-
dc.source.urihttp://digital.bl.fcen.uba.ar/Download/paper/paper_19326203_v8_n3_p_Jozefkowicz.pdf-
dc.subjectaquaporin-
dc.subjectcomplementary RNA-
dc.subjectarticle-
dc.subjectbeet-
dc.subjectcell membrane-
dc.subjectconfocal microscopy-
dc.subjectcontrolled study-
dc.subjectdose response-
dc.subjectmolecular dynamics-
dc.subjectmutagenesis-
dc.subjectnonhuman-
dc.subjectnucleotide sequence-
dc.subjectoocyte-
dc.subjectpH-
dc.subjectphylogeny-
dc.subjectprotein content-
dc.subjectprotein expression-
dc.subjectprotein function-
dc.subjectprotein localization-
dc.subjectprotein protein interaction-
dc.subjectRNA synthesis-
dc.subjectsequence analysis-
dc.subjectwater permeability-
dc.subjectwater transport-
dc.subjectAmino Acid Sequence-
dc.subjectAnimals-
dc.subjectAquaporins-
dc.subjectBeta vulgaris-
dc.subjectCell Membrane Permeability-
dc.subjectConserved Sequence-
dc.subjectHydrogen-Ion Concentration-
dc.subjectMolecular Dynamics Simulation-
dc.subjectMolecular Sequence Data-
dc.subjectMutant Proteins-
dc.subjectOsmosis-
dc.subjectPlant Proteins-
dc.subjectProtein Binding-
dc.subjectProtein Structure, Secondary-
dc.subjectRecombinant Proteins-
dc.subjectStructure-Activity Relationship-
dc.subjectXenopus laevis-
dc.titleLoop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:ar-repo/semantics/artículo-
dc.typeinfo:eu-repo/semantics/publishedVersion-
Aparece en las colecciones: FCEN - Facultad de Ciencias Exactas y Naturales. UBA

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