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1. Cooperativity in proton sensing by<scp>PIP</scp>aquaporins

Author

Karina Alleva, Agustina Canessa Fortuna, Gabriela Soto, Cintia Jozefkowicz, Victoria Andrea Vitali, and F. Luis González Flecha

Subjects
0301 basic medicine, genetic structures, Proton binding, Protein Conformation, Intracellular pH, PARALOGUES, Aquaporin, Cooperativity, Xenopus Proteins, Aquaporins, WATER TRANSPORT, STOICHIOMETRY, Biochemistry, AQUAPORIN, purl.org/becyt/ford/1 [https], Cell membrane, Xenopus laevis, 03 medical and health sciences, 0302 clinical medicine, Tetramer, medicine, Animals, purl.org/becyt/ford/1.6 [https], Molecular Biology, Water transport, Chemistry, Cell Membrane, COOPERATIVITY, fungi, Water, Cooperative binding, Cell Biology, Hydrogen-Ion Concentration, 030104 developmental biology, medicine.anatomical_structure, 030220 oncology & carcinogenesis, Biophysics, Protons
Abstract

One of the most intriguing properties of plasma membrane intrinsic protein (PIP) aquaporins (AQPs) is their ability to modulate water transport by sensing different levels of intracellular pH through the assembly of homo- and heterotetrameric molecular species in the plasma membrane. In this work, using a phenomenological modeling approach, we demonstrate that cooperativity in PIP biological response cannot be directly attributed to a cooperative proton binding, as it is usually considered, since it could also be the consequence of a cooperative conformation transition between open and closed states of the channel. Moreover, our results show that, when mixed populations of homo- and heterotetrameric PIP channels are coexpressed in the plasma membrane of the same cell, the observed decrease in the degree of positive cooperativity would result from the simultaneous presence of molecular species with different levels of proton sensing. Indeed, the random mixing between different PIP paralogues as subunits in a single tetramer, plus the possibility of mixed populations of homo- and heterotetrameric PIP channels widen the spectrum of cooperative responses of a cell membrane. Our approach offers a deep understanding of cooperative transport of AQP channels, as members of a multiprotein family where the relevant proton binding sites of each member have not been clearly elucidated yet. Fil: Vitali, Victoria Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Canessa Fortuna, Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Soto, Gabriela Cynthia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria; Argentina Fil: Gonzalez Flecha, Francisco Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina

Published
2018
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2. Tonoplast (Bv TIP1;2) and plasma membrane (Bv PIP2;1) aquaporins show different mechanosensitive properties

Author

Agustina Canessa Fortuna, Karina Alleva, Ramiro Pablo Goldman, Cintia Jozefkowicz, Moira Sutka, and Marcelo Ozu

Subjects
0301 basic medicine, Osmosis, Biophysics, Aquaporin, Vacuole, Aquaporins, Biochemistry, 03 medical and health sciences, 0302 clinical medicine, Structural Biology, Genetics, Molecular Biology, Osmotic response, Elastic modulus, Plant Proteins, Water transport, Chemistry, Cell Membrane, Cell Biology, Permeability coefficient, 030104 developmental biology, Membrane, lipids (amino acids, peptides, and proteins), Mechanosensitive channels, Beta vulgaris, 030217 neurology & neurosurgery
Abstract

Previous works proposed that aquaporins behave as mechanosensitive channels. However, principal issues about mechanosensitivity of aquaporins are not known. In this work, we characterized the mechanosensitive properties of the water channels BvTIP1;2 (TIP1) and BvPIP2;1 (PIP2) from red beet (Beta vulgaris). We simultaneously measured the mechanical behavior and the water transport rates during the osmotic response of emptied-out oocytes expressing TIP1 or PIP2. Our results indicate that TIP1 is a mechanosensitive aquaporin, whereas PIP2 is not. We found that a single exponential function between the osmotic permeability coefficient and the volumetric elastic modulus governs the mechanosensitivity of TIP1. Finally, homology modeling analysis indicates that putative residues involved in mechanosensitivity show different quantity and distribution in TIP1 and PIP2.

Published
2017
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3. Absence of the Nitrous Oxide Reductase Gene Cluster in Commercial Alfalfa Inoculants Is Probably Due to the Extensive Loss of Genes During Rhizobial Domestication

Author

Nicolás Daniel Ayub, Romina Frare, Silvina Maricel Brambilla, Gabriela Cinthia Soto, and Cintia Jozefkowicz

Subjects
0301 basic medicine, COMMERCIAL INOCULANTS, Denitrification, NITROUS OXIDE, Biotecnología del Medio Ambiente, 030106 microbiology, Nitrous Oxide, Soil Science, Biotecnología Medioambiental, Nitrous-oxide reductase, INGENIERÍAS Y TECNOLOGÍAS, Biology, Reductase, Evolution, Molecular, 03 medical and health sciences, chemistry.chemical_compound, Nitrate, Genome Size, Nitrogen Fixation, Botany, Gene cluster, Symbiosis, Microbial inoculant, Ecology, Evolution, Behavior and Systematics, Nitrites, Nitrates, Ecology, Bacteria, NOS CLUSTER, equipment and supplies, biology.organism_classification, EVOLUTION, 030104 developmental biology, chemistry, Multigene Family, Nitrogen fixation, Rhizobium, Oxidoreductases, Medicago sativa
Abstract

As other legume crops, alfalfa cultivation increases the emission of the greenhouse gas nitrous oxide (N2O). Since legume-symbiotic nitrogen-fixing bacteria play a crucial role in this emission, it is important to understand the possible impacts of rhizobial domestication on the evolution of denitrification genes. In comparison with the genomes of non-commercial strains, those of commercial alfalfa inoculants exhibit low total genome size, low number of ORFs and high numbers of both frameshifted genes and pseudogenes, suggesting a dramatic loss of genes during bacterial domestication. Genomic analysis focused on denitrification genes revealed that commercial strains have perfectly conserved the nitrate (NAP), nitrite (NIR) and nitric (NOR) reductase clusters related to the production of N2O from nitrate but completely lost the nitrous oxide (NOS) reductase cluster (nosRZDFYLX genes) associated with the reduction of N2O to gas nitrogen. Based on these results, we propose future screenings for alfalfa-nodulating isolates containing both nitrogen fixation and N2O reductase genes for environmental sustainability of alfalfa production. Fil: Brambilla, Silvina Maricel. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo.; Argentina Fil: Frare, Romina Alejandra. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo.; Argentina Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo.; Argentina Fil: Jozefkowicz, Cintia. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo.; Argentina Fil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Genetica "ewald A. Favret" Al Iabimo.; Argentina

Published
2017

4. Stable symbiotic nitrogen fixation under water-deficit field conditions by a stress-tolerant alfalfa microsymbiont and its complete genome sequence

Author

Silvina Maricel Brambilla, Margarita Stritzler, Carlos Fabian Piccinetti, Gabriela Soto, Cintia Jozefkowicz, Carolina Berini, Nicolás Daniel Ayub, Romina Frare, Mariana Puente, and Pedro Reyes Pérez

Subjects
0301 basic medicine, SINORHIZOBIUM MELILOTI, 030106 microbiology, Biotecnología del Medio Ambiente, ALFALFA, Bioengineering, INGENIERÍAS Y TECNOLOGÍAS, Applied Microbiology and Biotechnology, Genome, GLYCINE BETAINE, 03 medical and health sciences, chemistry.chemical_compound, Betaine, Biosynthesis, Nitrogen Fixation, Botany, Symbiosis, Bioremediación, Diagnóstico Biotecnológico en Gestión Medioambiental, Sinorhizobium meliloti, biology, COMPLETE GENOME, food and beverages, Genomics, General Medicine, biology.organism_classification, Adaptation, Physiological, Droughts, 030104 developmental biology, chemistry, Biochemistry, Glycine, Nitrogen fixation, Osmoprotectant, Genome, Bacterial, Bacteria, Medicago sativa, Biotechnology
Abstract

We here characterized the stress-tolerant alfalfa microsymbiont Sinorhizobium meliloti B401. B401-treated plants showed high nitrogen fixation rates under humid and semiarid environments. The production of glycine betaine in isolated bacteroids positively correlated with low precipitation levels, suggesting that this compound acts as a critical osmoprotectant under field conditions. Genome analysis revealed that strain B401 contains alternative pathways for the biosynthesis and uptake of glycine betaine and its precursors. Such genomic information will offer substantial insight into the environmental physiology of this biotechnologically valuable nitrogen-fixingbacterium. Fil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Brambilla, Silvina Maricel. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina Fil: Frare, Romina Alejandra. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Stritzler, Margarita. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Piccinetti, Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Microbiología y Zoología Agrícola; Argentina Fil: Puente, Mariana L. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Microbiología y Zoología Agrícola; Argentina Fil: Berini, Carolina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas en Retrovirus y Sida. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas en Retrovirus y Sida; Argentina Fil: Pérez, Pedro Reyes. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina

Published
2017

6. Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins

Author

Cintia Jozefkowicz, Pablo Rosi, Karina Alleva, Lía I. Pietrasanta, Lorena Sigaut, Gabriela Amodeo, and Gabriela Soto

Subjects
Macromolecular Assemblies, Osmosis, Cell Membrane Permeability, sequence analysis, complementary RNA, Plasma protein binding, Molecular Dynamics, confocal microscopy, phylogeny, Biochemistry, Protein Structure, Secondary, Conserved sequence, Transmembrane Transport Proteins, purl.org/becyt/ford/1 [https], Molecular dynamics, Plasma membrane intrinsic proteins, Xenopus laevis, Protein structure, Computational Chemistry, dose response, Macromolecular Structure Analysis, Biochemistry Simulations, Conserved Sequence, Plant Proteins, Genetics, Multidisciplinary, pH, article, Bioquímica y Biología Molecular, protein function, Hydrogen-Ion Concentration, protein content, Recombinant Proteins, Chemistry, protein protein interaction, Medicine, beet, Beta vulgaris, CIENCIAS NATURALES Y EXACTAS, mutagenesis, Research Article, Protein Binding, Protein Structure, water transport, Science, Molecular Sequence Data, Biophysics, Aquaporin, protein localization, Biology, Molecular Dynamics Simulation, Aquaporins, water permeability, Ciencias Biológicas, Structure-Activity Relationship, Tetramer, Animals, controlled study, Amino Acid Sequence, RNA synthesis, Protein Interactions, purl.org/becyt/ford/1.6 [https], oocyte, protein expression, nonhuman, Mutagenesis, Proteins, Computational Biology, nucleotide sequence, molecular dynamics, Transmembrane Proteins, aquaporin, Membrane protein, Mutant Proteins, cell membrane
Abstract

Research 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. Fil: Jozefkowicz, Cintia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Rosi, Pablo Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina; Fil: Sigaut, Lorena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Pietrasanta, Lia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Amodeo, Gabriela. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina

Published
2013

7. Plant Aquaporins Co-Expression Senses Differentially the Intracelluar pH

Author

Karina Alleva, Victoria Andrea Vitali, Gabriela Soto, Gabriela Amodeo, Mercedes Marquez, Jorge Bellati, and Cintia Jozefkowicz

Subjects
Water transport, biology, Chemistry, Biophysics, Xenopus, Aquaporin, Gating, biology.organism_classification, Cytosol, Membrane, Biochemistry, Permeability (electromagnetism), lipids (amino acids, peptides, and proteins), Heterologous expression
Abstract

The plant plasma membrane (PM) expresses two types of aquaporins: PIP1 and PIP2. These PIP are characterized by: i- the faculty to reduce water permeation through the pore after cytosolic acidification as a consequence of gating process, ii- the ability to modulate membrane water permeability by co-expression of both types.We investigated if these functional characteristics of PIP can act together to give a new and relevant modulation response to acidification. To test our hypothesis we used PIP1 and PIP2 from different plant sources (Beta vulgaris roots and Fragaria x ananassa fruits). The experimental approach used was to perform a functional study of PIP by means of the heterologous expression system Xenopus oocytes and analyzed the oocyte PM water permeability coefficient (Pf) when PIP are injected.Briefly, the Pf was increased ten-fold by PIP2, but it remained low for both control oocytes and PIP1 injected ones. Moreover, when oocytes expressed PIP2, a partial (70%) pH inhibitory response under cytosolic acidification (pH 6) was detected.When PIP1-PIP2 co-expression was assayed, Pf was enhanced seven-fold in comparison with Pf obtained by PIP2 expression alone. Furthermore, the pH dependent behavior showed that PIP1-PIP2 co-expression accounts for different pH sensitivity by shifting the EC50 of the inhibitory response from pH 6.1 to pH 6.9, compared to PIP2.Our results show that: i- PIP co-expression impacts on the membrane water permeability not only by modulating the water transport capacity but also the pH regulatory response, improving in this way membrane plasticity, ii- this PIP behavior is not a tissue specific and/or species-dependent response but a more general one.In conclusion, aquaporin co-expression widens and enhances regulatory properties that control adjustment of water movements which might be of great importance to react to variable osmotic and pH stress.

Published
2010
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