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1.
Front Plant Sci ; 14: 1213454, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-37615024

RESUMO

Maintenance of optimal leaf tissue humidity is important for plant productivity and food security. Leaf humidity is influenced by soil and atmospheric water availability, by transpiration and by the coordination of water flux across cell membranes throughout the plant. Flux of water and solutes across plant cell membranes is influenced by the function of aquaporin proteins. Plants have numerous aquaporin proteins required for a multitude of physiological roles in various plant tissues and the membrane flux contribution of each aquaporin can be regulated by changes in protein abundance, gating, localisation, post-translational modifications, protein:protein interactions and aquaporin stoichiometry. Resolving which aquaporins are candidates for influencing leaf humidity and determining how their regulation impacts changes in leaf cell solute flux and leaf cavity humidity is challenging. This challenge involves resolving the dynamics of the cell membrane aquaporin abundance, aquaporin sub-cellular localisation and location-specific post-translational regulation of aquaporins in membranes of leaf cells during plant responses to changes in water availability and determining the influence of cell signalling on aquaporin permeability to a range of relevant solutes, as well as determining aquaporin influence on cell signalling. Here we review recent developments, current challenges and suggest open opportunities for assessing the role of aquaporins in leaf substomatal cavity humidity regulation.

2.
Funct Plant Biol ; 50(8): 633-648, 2023 08.
Artigo em Inglês | MEDLINE | ID: mdl-37277902

RESUMO

Dynamic changes in aquaporin gene expression occur during seed germination. One example is the ~30-fold increase in Arabidopsis thaliana PIP2;1 transcripts within 24h of seed imbibition. To investigate whether AtPIP2;1 can influence seed germination wild-type Columbia-0, single (Atpip2;1 ) and double (Atpip2;1-Atpip2;2 ) loss-of-function mutants, along with transgenic 2x35S::AtPIP2;1 over-expressing (OE) lines and null-segregant controls, were examined. The various genotypes were germinated in control and saline (75mM NaCl treatment) conditions and tested for germination efficiency, imbibed seed maximum cross sectional (MCS) area, imbibed seed mass, and seed Na+ and K+ content. Seed lacking functional AtPIP2;1 and/or AtPIP2;2 proteins or constitutively over-expressing AtPIP2;1 , had delayed germination in saline conditions relative to wild-type and null-segregant seed, respectively. Exposure to saline germination conditions resulted in Atpip2;1 mutants having greater imbibed seed mass and less accumulated Na+ than wild-type, whereas lines over-expressing AtPIP2;1 had reduced imbibed seed mass and greater seed K+ content than null-segregant control seed. The results imply a role for AtPIP2;1 in seed germination processes, whether directly through its capacity for water and ion transport or H2 O2 signalling, or indirectly through potentially triggering dynamic differential regulation of other aquaporins expressed during germination. Future research will aid in dissecting the aquaporin functions influencing germination and may lead to novel solutions for optimising germination in sub-optimal conditions, such as saline soils.


Assuntos
Aquaporinas , Proteínas de Arabidopsis , Arabidopsis , Aquaporinas/genética , Aquaporinas/metabolismo , Arabidopsis/genética , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Membrana Celular/genética , Membrana Celular/metabolismo , Estudos Transversais , Germinação/genética , Proteínas de Membrana/metabolismo , Salinidade , Sementes/genética
3.
Nat Biotechnol ; 41(7): 911-912, 2023 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-37308688
4.
Front Plant Sci ; 14: 1078220, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36760647

RESUMO

Introduction: Engineering membrane transporters to achieve desired functionality is reliant on availability of experimental data informing structure-function relationships and intelligent design. Plant aquaporin (AQP) isoforms are capable of transporting diverse substrates such as signaling molecules, nutrients, metalloids, and gases, as well as water. AQPs can act as multifunctional channels and their transport function is reliant on many factors, with few studies having assessed transport function of specific isoforms for multiple substrates. Methods: High-throughput yeast assays were developed to screen for transport function of plant AQPs, providing a platform for fast data generation and cataloguing of substrate transport profiles. We applied our high-throughput growth-based yeast assays to screen all 13 Arabidopsis PIPs (AtPIPs) for transport of water and several neutral solutes: hydrogen peroxide (H2O2), boric acid (BA), and urea. Sodium (Na+) transport was assessed using elemental analysis techniques. Results: All AtPIPs facilitated water and H2O2 transport, although their growth phenotypes varied, and none were candidates for urea transport. For BA and Na+ transport, AtPIP2;2 and AtPIP2;7 were the top candidates, with yeast expressing these isoforms having the most pronounced toxicity response to BA exposure and accumulating the highest amounts of Na+. Linking putative AtPIP isoform substrate transport profiles with phylogenetics and gene expression data, enabled us to align possible substrate preferences with known and hypothesized biological roles of AtPIPs. Discussion: This testing framework enables efficient cataloguing of putative transport functionality of diverse AQPs at a scale that can help accelerate our understanding of AQP biology through big data approaches (e.g. association studies). The principles of the individual assays could be further adapted to test additional substrates. Data generated from this framework could inform future testing of AQP physiological roles, and address knowledge gaps in structure-function relationships to improve engineering efforts.

5.
Plant Cell ; 35(1): 139-161, 2023 01 02.
Artigo em Inglês | MEDLINE | ID: mdl-36377770

RESUMO

Research into crop yield and resilience has underpinned global food security, evident in yields tripling in the past 5 decades. The challenges that global agriculture now faces are not just to feed 10+ billion people within a generation, but to do so under a harsher, more variable, and less predictable climate, and in many cases with less water, more expensive inputs, and declining soil quality. The challenges of climate change are not simply to breed for a "hotter drier climate," but to enable resilience to floods and droughts and frosts and heat waves, possibly even within a single growing season. How well we prepare for the coming decades of climate variability will depend on our ability to modify current practices, innovate with novel breeding methods, and communicate and work with farming communities to ensure viability and profitability. Here we define how future climates will impact farming systems and growing seasons, thereby identifying the traits and practices needed and including exemplars being implemented and developed. Critically, this review will also consider societal perspectives and public engagement about emerging technologies for climate resilience, with participatory approaches presented as the best approach.


Assuntos
Agricultura , Solo , Fenótipo , Estações do Ano , Estresse Fisiológico
6.
Biochim Biophys Acta Biomembr ; 1863(10): 183661, 2021 10 01.
Artigo em Inglês | MEDLINE | ID: mdl-34058166

RESUMO

Aquaporins are water and solute channel proteins found throughout the kingdoms of life. Ion-conducting aquaporins (icAQPs) have been identified in both plants and animals indicating that this function may be conserved through evolution. In higher plants icAQP function has been demonstrated for isoforms from two of five aquaporin subfamilies indicating that this function could have existed before the divergence of higher plants from green algae. Here a PIP-like aquaporin from the charophytic alga Klebsormidium nitens was functionally characterised in Xenopus laevis oocytes and its expression was found to induce water and ion conductance.


Assuntos
Aquaporinas/metabolismo , Alga Marinha/metabolismo , Água/metabolismo , Animais , Transporte de Íons , Xenopus laevis
7.
Annu Rev Plant Biol ; 72: 703-736, 2021 06 17.
Artigo em Inglês | MEDLINE | ID: mdl-33577345

RESUMO

Aquaporins function as water and neutral solute channels, signaling hubs, disease virulence factors, and metabolon components. We consider plant aquaporins that transport ions compared to some animal counterparts. These are candidates for important, as yet unidentified, cation and anion channels in plasma, tonoplast, and symbiotic membranes. For those individual isoforms that transport ions, water, and gases, the permeability spans 12 orders of magnitude. This requires tight regulation of selectivity via protein interactions and posttranslational modifications. A phosphorylation-dependent switch between ion and water permeation in AtPIP2;1 might be explained by coupling between the gates of the four monomer water channels and the central pore of the tetramer. We consider the potential for coupling between ion and water fluxes that could form the basis of an electroosmotic transducer. A grand challenge in understanding the roles of ion transporting aquaporins is their multifunctional modes that are dependent on location, stress, time, and development.


Assuntos
Aquagliceroporinas , Aquaporinas , Animais , Aquaporinas/metabolismo , Transporte de Íons , Plantas/metabolismo , Água/metabolismo
8.
Int J Mol Sci ; 21(19)2020 09 27.
Artigo em Inglês | MEDLINE | ID: mdl-32992595

RESUMO

Some plasma membrane intrinsic protein (PIP) aquaporins can facilitate ion transport. Here we report that one of the 12 barley PIPs (PIP1 and PIP2) tested, HvPIP2;8, facilitated cation transport when expressed in Xenopus laevis oocytes. HvPIP2;8-associated ion currents were detected with Na+ and K+, but not Cs+, Rb+, or Li+, and was inhibited by Ba2+, Ca2+, and Cd2+ and to a lesser extent Mg2+, which also interacted with Ca2+. Currents were reduced in the presence of K+, Cs+, Rb+, or Li+ relative to Na+ alone. Five HvPIP1 isoforms co-expressed with HvPIP2;8 inhibited the ion conductance relative to HvPIP2;8 alone but HvPIP1;3 and HvPIP1;4 with HvPIP2;8 maintained the ion conductance at a lower level. HvPIP2;8 water permeability was similar to that of a C-terminal phosphorylation mimic mutant HvPIP2;8 S285D, but HvPIP2;8 S285D showed a negative linear correlation between water permeability and ion conductance that was modified by a kinase inhibitor treatment. HvPIP2;8 transcript abundance increased in barley shoot tissues following salt treatments in a salt-tolerant cultivar Haruna-Nijo, but not in salt-sensitive I743. There is potential for HvPIP2;8 to be involved in barley salt-stress responses, and HvPIP2;8 could facilitate both water and Na+/K+ transport activity, depending on the phosphorylation status.


Assuntos
Aquaporinas/metabolismo , Cálcio/metabolismo , Hordeum/metabolismo , Transporte de Íons , Oócitos/metabolismo , Proteínas de Plantas/metabolismo , Brotos de Planta/metabolismo , Potássio/metabolismo , Sódio/metabolismo , Animais , Aquaporinas/genética , Cátions/metabolismo , Membrana Celular/metabolismo , Células Cultivadas , Feminino , Regulação da Expressão Gênica de Plantas , Hordeum/genética , Técnicas de Patch-Clamp , Fosforilação , Proteínas de Plantas/genética , Brotos de Planta/genética , RNA Complementar/administração & dosagem , Água/metabolismo , Xenopus laevis
9.
Plant Cell Environ ; 43(10): 2428-2442, 2020 10.
Artigo em Inglês | MEDLINE | ID: mdl-32678928

RESUMO

The phosphorylation state of two serine residues within the C-terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization in response to salt and osmotic stress. Here, we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems. In Xenopus laevis oocytes, phosphomimic mutants AtPIP2;1 S280D, S283D, and S280D/S283D had significantly greater ion conductance for Na+ and K+ , whereas the S280A single phosphonull mutant had greater water permeability. We observed a phosphorylation-dependent inverse relationship between AtPIP2;1 water and ion transport with a 10-fold change in both. The results revealed that phosphorylation of S280 and S283 influences the preferential facilitation of ion or water transport by AtPIP2;1. The results also hint that other regulatory sites play roles that are yet to be elucidated. Expression of the AtPIP2;1 phosphorylation mutants in Saccharomyces cerevisiae confirmed that phosphorylation influences plasma membrane localization, and revealed higher Na+ accumulation for S280A and S283D mutants. Collectively, the results show that phosphorylation in the C-terminal domain of AtPIP2;1 influences its subcellular localization and cation transport capacity.


Assuntos
Aquaporinas/metabolismo , Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Canais Iônicos/metabolismo , Animais , Animais Geneticamente Modificados , Aquaporinas/fisiologia , Proteínas de Arabidopsis/fisiologia , Oócitos , Fosforilação , Água/metabolismo , Xenopus laevis
10.
J Exp Bot ; 71(6): 1763-1773, 2020 03 25.
Artigo em Inglês | MEDLINE | ID: mdl-32109278

RESUMO

Seeds are the typical dispersal and propagation units of angiosperms and gymnosperms. Water movement into and out of seeds plays a crucial role from the point of fertilization through to imbibition and seed germination. A class of membrane intrinsic proteins called aquaporins (AQPs) assist with the movement of water and other solutes within seeds. These highly diverse and abundant proteins are associated with different processes in the development, longevity, imbibition, and germination of seed. However, there are many AQPs encoded in a plant's genome and it is not yet clear how, when, or which AQPs are involved in critical stages of seed biology. Here we review the literature to examine the evidence for AQP involvement in seeds and analyse Arabidopsis seed-related transcriptomic data to assess which AQPs are likely to be important in seed water relations and explore additional roles for AQPs in seed biology.


Assuntos
Aquaporinas , Regulação da Expressão Gênica de Plantas , Aquaporinas/genética , Aquaporinas/metabolismo , Biologia , Germinação , Sementes/genética , Sementes/metabolismo
11.
J Exp Bot ; 71(1): 138-153, 2020 01 01.
Artigo em Inglês | MEDLINE | ID: mdl-31536111

RESUMO

In cereal grain, sucrose is converted into storage carbohydrates: mainly starch, fructan, and mixed-linkage (1,3;1,4)-ß-glucan (MLG). Previously, endosperm-specific overexpression of the HvCslF6 gene in hull-less barley was shown to result in high MLG and low starch content in mature grains. Morphological changes included inwardly elongated aleurone cells, irregular cell shapes of peripheral endosperm, and smaller starch granules of starchy endosperm. Here we explored the physiological basis for these defects by investigating how changes in carbohydrate composition of developing grain impact mature grain morphology. Augmented MLG coincided with increased levels of soluble carbohydrates in the cavity and endosperm at the storage phase. Transcript levels of genes relating to cell wall, starch, sucrose, and fructan metabolism were perturbed in all tissues. The cell walls of endosperm transfer cells (ETCs) in transgenic grain were thinner and showed reduced mannan labelling relative to the wild type. At the early storage phase, ruptures of the non-uniformly developed ETCs and disorganization of adjacent endosperm cells were observed. Soluble sugars accumulated in the developing grain cavity, suggesting a disturbance of carbohydrate flow from the cavity towards the endosperm, resulting in a shrunken mature grain phenotype. Our findings demonstrate the importance of regulating carbohydrate partitioning in maintenance of grain cellularization and filling processes.


Assuntos
Metabolismo dos Carboidratos , Grão Comestível/crescimento & desenvolvimento , Regulação da Expressão Gênica de Plantas , Hordeum/genética , Proteínas de Plantas/genética , Transporte Biológico , Grão Comestível/genética , Endosperma/genética , Endosperma/crescimento & desenvolvimento , Hordeum/crescimento & desenvolvimento , Hordeum/metabolismo , Proteínas de Plantas/metabolismo , Plantas Geneticamente Modificadas/genética , Plantas Geneticamente Modificadas/crescimento & desenvolvimento , Plantas Geneticamente Modificadas/metabolismo
12.
New Phytol ; 225(3): 1072-1090, 2020 02.
Artigo em Inglês | MEDLINE | ID: mdl-31004496

RESUMO

Agriculture is expanding into regions that are affected by salinity. This review considers the energetic costs of salinity tolerance in crop plants and provides a framework for a quantitative assessment of costs. Different sources of energy, and modifications of root system architecture that would maximize water vs ion uptake are addressed. Energy requirements for transport of salt (NaCl) to leaf vacuoles for osmotic adjustment could be small if there are no substantial leaks back across plasma membrane and tonoplast in root and leaf. The coupling ratio of the H+ -ATPase also is a critical component. One proposed leak, that of Na+ influx across the plasma membrane through certain aquaporin channels, might be coupled to water flow, thus conserving energy. For the tonoplast, control of two types of cation channels is required for energy efficiency. Transporters controlling the Na+ and Cl- concentrations in mitochondria and chloroplasts are largely unknown and could be a major energy cost. The complexity of the system will require a sophisticated modelling approach to identify critical transporters, apoplastic barriers and root structures. This modelling approach will inform experimentation and allow a quantitative assessment of the energy costs of NaCl tolerance to guide breeding and engineering of molecular components.


Assuntos
Produtos Agrícolas/fisiologia , Metabolismo Energético , Tolerância ao Sal/fisiologia , Transporte Biológico , Respiração Celular , Raízes de Plantas/anatomia & histologia
13.
New Phytol ; 225(3): 1091-1096, 2020 02.
Artigo em Inglês | MEDLINE | ID: mdl-31006123

RESUMO

Plant roots must exclude almost all of the Na+ and Cl- in saline soil while taking up water, otherwise these ions would build up to high concentrations in leaves. Plants evaporate c. 50 times more water than they retain, so 98% exclusion would result in shoot NaCl concentrations equal to that of the external medium. Taking up just 2% of the NaCl allows a plant to osmotically adjust the Na+ and Cl- in vacuoles, while organic solutes provide the balancing osmotic pressure in the cytoplasm. We quantify the costs of this exclusion by roots, the regulation of Na+ and Cl- transport through the plant, and the costs of osmotic adjustment with organic solutes in roots.


Assuntos
Metabolismo Energético , Osmose , Desenvolvimento Vegetal , Salinidade , Solo/química , Raízes de Plantas/metabolismo
14.
Ann Bot ; 124(2): 201-208, 2019 09 24.
Artigo em Inglês | MEDLINE | ID: mdl-31162525

RESUMO

BACKGROUND: Plant membrane transporters are involved in diverse cellular processes underpinning plant physiology, such as nutrient acquisition, hormone movement, resource allocation, exclusion or sequestration of various solutes from cells and tissues, and environmental and developmental signalling. A comprehensive characterization of transporter function is therefore key to understanding and improving plant performance. SCOPE AND CONCLUSIONS: In this review, we focus on the complexities involved in characterizing transporter function and the impact that this has on current genomic annotations. Specific examples are provided that demonstrate why sequence homology alone cannot be relied upon to annotate and classify transporter function, and to show how even single amino acid residue variations can influence transporter activity and specificity. Misleading nomenclature of transporters is often a source of confusion in transporter characterization, especially for people new to or outside the field. Here, to aid researchers dealing with interpretation of large data sets that include transporter proteins, we provide examples of transporters that have been assigned names that misrepresent their cellular functions. Finally, we discuss the challenges in connecting transporter function at the molecular level with physiological data, and propose a solution through the creation of new databases. Further fundamental in-depth research on specific transport (and other) proteins is still required; without it, significant deficiencies in large-scale data sets and systems biology approaches will persist. Reliable characterization of transporter function requires integration of data at multiple levels, from amino acid residue sequence annotation to more in-depth biochemical, structural and physiological studies.


Assuntos
Proteínas de Membrana Transportadoras , Sequência de Aminoácidos , Fenótipo , Fenômenos Fisiológicos Vegetais , Plantas
15.
Plant Sci ; 269: 47-55, 2018 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-29606216

RESUMO

The root growth of most crop plants is inhibited by soil salinity. Roots respond by modulating metabolism, gene expression and protein activity, which results in changes in cell wall composition, transport processes, cell size and shape, and root architecture. Here, we focus on the effects of salt stress on cell wall modifying enzymes, cellulose microfibril orientation and non-cellulosic polysaccharide deposition in root elongation zones, as important determinants of inhibition of root elongation, and highlight cell wall changes linked to tolerance to salt stressed and water limited roots. Salt stress induces changes in the wall composition of specific root cell types, including the increased deposition of lignin and suberin in endodermal and exodermal cells. These changes can benefit the plant by preventing water loss and altering ion transport pathways. We suggest that binding of Na+ ions to cell wall components might influence the passage of Na+ and that Na+ can influence the binding of other ions and hinder the function of pectin during cell growth. Naturally occurring differences in cell wall structure may provide new resources for breeding crops that are more salt tolerant.


Assuntos
Produtos Agrícolas/fisiologia , Salinidade , Solo/química , Estresse Fisiológico , Parede Celular/enzimologia , Celulose/química , Produtos Agrícolas/enzimologia , Produtos Agrícolas/crescimento & desenvolvimento , Microfibrilas/química , Raízes de Plantas/enzimologia , Raízes de Plantas/crescimento & desenvolvimento , Raízes de Plantas/fisiologia , Polissacarídeos/metabolismo , Água/metabolismo
16.
Cell Mol Life Sci ; 75(6): 1133-1144, 2018 03.
Artigo em Inglês | MEDLINE | ID: mdl-29177534

RESUMO

An important trait associated with the salt tolerance of wheat is the exclusion of sodium ions (Na+) from the shoot. We have previously shown that the sodium transporters TmHKT1;5-A and TaHKT1;5-D, from Triticum monoccocum (Tm) and Triticum aestivum (Ta), are encoded by genes underlying the major shoot Na+-exclusion loci Nax1 and Kna1, respectively. Here, using heterologous expression, we show that the affinity (K m) for the Na+ transport of TmHKT1;5-A, at 2.66 mM, is higher than that of TaHKT1;5-D at 7.50 mM. Through 3D structural modelling, we identify residues D471/a gap and D474/G473 that contribute to this property. We identify four additional mutations in amino acid residues that inhibit the transport activity of TmHKT1;5-A, which are predicted to be the result of an occlusion of the pore. We propose that the underlying transport properties of TmHKT1;5-A and TaHKT1;5-D contribute to their unique ability to improve Na+ exclusion in wheat that leads to an improved salinity tolerance in the field.


Assuntos
Proteínas de Transporte de Cátions/química , Regulação da Expressão Gênica de Plantas , Proteínas de Plantas/química , Brotos de Planta/metabolismo , Tolerância ao Sal/genética , Sódio/metabolismo , Simportadores/química , Triticum/metabolismo , Motivos de Aminoácidos , Substituição de Aminoácidos , Animais , Sítios de Ligação , Proteínas de Transporte de Cátions/genética , Proteínas de Transporte de Cátions/metabolismo , Clonagem Molecular , Transporte de Íons , Cinética , Modelos Moleculares , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Brotos de Planta/genética , Ligação Proteica , Domínios e Motivos de Interação entre Proteínas , Isoformas de Proteínas/química , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Estrutura Secundária de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/metabolismo , Relação Estrutura-Atividade , Simportadores/genética , Simportadores/metabolismo , Termodinâmica , Triticum/genética , Xenopus laevis/genética , Xenopus laevis/metabolismo
17.
Int J Mol Sci ; 18(11)2017 Nov 03.
Artigo em Inglês | MEDLINE | ID: mdl-29099773

RESUMO

Aquaporins (AQPs) are known to facilitate water and solute fluxes across barrier membranes. An increasing number of AQPs are being found to serve as ion channels. Ion and water permeability of selected plant and animal AQPs (plant Arabidopsis thaliana AtPIP2;1, AtPIP2;2, AtPIP2;7, human Homo sapiens HsAQP1, rat Rattus norvegicus RnAQP4, RnAQP5, and fly Drosophilamelanogaster DmBIB) were expressed in Xenopus oocytes and examined in chelator-buffered salines to evaluate the effects of divalent cations (Ca2+, Mg2+, Ba2+ and Cd2+) on ionic conductances. AtPIP2;1, AtPIP2;2, HsAQP1 and DmBIB expressing oocytes had ionic conductances, and showed differential sensitivity to block by external Ca2+. The order of potency of inhibition by Ca2+ was AtPIP2;2 > AtPIP2;1 > DmBIB > HsAQP1. Blockage of the AQP cation channels by Ba2+ and Cd2+ caused voltage-sensitive outward rectification. The channels with the highest sensitivity to Ca2+ (AtPIP2;1 and AtPIP2;2) showed a distinctive relief of the Ca2+ block by co-application of excess Ba2+, suggesting that divalent ions act at the same site. Recognizing the regulatory role of divalent cations may enable the discovery of other classes of AQP ion channels, and facilitate the development of tools for modulating AQP ion channels. Modulators of AQPs have potential value for diverse applications including improving salinity tolerance in plants, controlling vector-borne diseases, and intervening in serious clinical conditions involving AQPs, such as cancer metastasis, cardiovascular or renal dysfunction.


Assuntos
Aquaporinas/metabolismo , Cátions Bivalentes/metabolismo , Animais , Arabidopsis/metabolismo , Proteínas de Arabidopsis/metabolismo , Bário/metabolismo , Cádmio/metabolismo , Cálcio/metabolismo , Drosophila , Humanos , Transporte de Íons , Magnésio/metabolismo , Xenopus
18.
Plant Cell Environ ; 40(5): 658-671, 2017 May.
Artigo em Inglês | MEDLINE | ID: mdl-27987209

RESUMO

Excessive soil salinity diminishes crop yield and quality. In a previous study in tomato, we identified two closely linked genes encoding HKT1-like transporters, HKT1;1 and HKT1;2, as candidate genes for a major quantitative trait locus (kc7.1) related to shoot Na+ /K+ homeostasis - a major salt tolerance trait - using two populations of recombinant inbred lines (RILs). Here, we determine the effectiveness of these genes in conferring improved salt tolerance by using two near-isogenic lines (NILs) that were homozygous for either the Solanum lycopersicum allele (NIL17) or for the Solanum cheesmaniae allele (NIL14) at both HKT1 loci; transgenic lines derived from these NILs in which each HKT1;1 and HKT1;2 had been silenced by stable transformation were also used. Silencing of ScHKT1;2 and SlHKT1;2 altered the leaf Na+ /K+ ratio and caused hypersensitivity to salinity in plants cultivated under transpiring conditions, whereas silencing SlHKT1;1/ScHKT1;1 had a lesser effect. These results indicate that HKT1;2 has the more significant role in Na+ homeostasis and salinity tolerance in tomato.


Assuntos
Proteínas de Transporte de Cátions/genética , Homeostase , Proteínas de Plantas/genética , Brotos de Planta/metabolismo , Potássio/metabolismo , Salinidade , Sódio/metabolismo , Solanum lycopersicum/genética , Solanum lycopersicum/metabolismo , Simportadores/genética , Alelos , Proteínas de Transporte de Cátions/metabolismo , Regulação da Expressão Gênica de Plantas/efeitos dos fármacos , Inativação Gênica/efeitos dos fármacos , Genes de Plantas , Loci Gênicos , Homeostase/efeitos dos fármacos , Homeostase/genética , Endogamia , Solanum lycopersicum/efeitos dos fármacos , Solanum lycopersicum/crescimento & desenvolvimento , Fenótipo , Folhas de Planta/efeitos dos fármacos , Folhas de Planta/metabolismo , Proteínas de Plantas/metabolismo , Brotos de Planta/efeitos dos fármacos , Análise de Componente Principal , Interferência de RNA , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Cloreto de Sódio/farmacologia , Simportadores/metabolismo
19.
Plant Cell Environ ; 40(6): 802-815, 2017 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-27620834

RESUMO

The aquaporin AtPIP2;1 is an abundant plasma membrane intrinsic protein in Arabidopsis thaliana that is implicated in stomatal closure, and is highly expressed in plasma membranes of root epidermal cells. When expressed in Xenopus laevis oocytes, AtPIP2;1 increased water permeability and induced a non-selective cation conductance mainly associated with Na+ . A mutation in the water pore, G103W, prevented both the ionic conductance and water permeability of PIP2;1. Co-expression of AtPIP2;1 with AtPIP1;2 increased water permeability but abolished the ionic conductance. AtPIP2;2 (93% identical to AtPIP2;1) similarly increased water permeability but not ionic conductance. The ionic conductance was inhibited by the application of extracellular Ca2+ and Cd2+ , with Ca2+ giving a biphasic dose-response with a prominent IC50 of 0.32 mм comparable with a previous report of Ca2+ sensitivity of a non-selective cation channel (NSCC) in Arabidopsis root protoplasts. Low external pH also inhibited ionic conductance (IC50 pH 6.8). Xenopus oocytes and Saccharomyces cerevisiae expressing AtPIP2;1 accumulated more Na+ than controls. Establishing whether AtPIP2;1 has dual ion and water permeability in planta will be important in understanding the roles of this aquaporin and if AtPIP2;1 is a candidate for a previously reported NSCC responsible for Ca2+ and pH sensitive Na+ entry into roots.


Assuntos
Aquaporinas/metabolismo , Proteínas de Arabidopsis/metabolismo , Cálcio/metabolismo , Substituição de Aminoácidos , Animais , Aquaporinas/genética , Proteínas de Arabidopsis/genética , Cádmio/farmacologia , Cálcio/farmacologia , Regulação da Expressão Gênica de Plantas , Glicina/genética , Concentração de Íons de Hidrogênio , Oócitos/efeitos dos fármacos , Oócitos/fisiologia , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Saccharomyces cerevisiae/genética , Sódio/metabolismo , Triptofano/genética , Água/metabolismo , Xenopus laevis
20.
Front Plant Sci ; 7: 1815, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-28018372

RESUMO

Setaria viridis is a C4 grass used as a model for bioenergy feedstocks. The elongating internodes in developing S. viridis stems grow from an intercalary meristem at the base, and progress acropetally toward fully expanded cells that store sugar. During stem development and maturation, water flow is a driver of cell expansion and sugar delivery. As aquaporin proteins are implicated in regulating water flow, we analyzed elongating and mature internode transcriptomes to identify putative aquaporin encoding genes that had particularly high transcript levels during the distinct stages of internode cell expansion and maturation. We observed that SvPIP2;1 was highly expressed in internode regions undergoing cell expansion, and SvNIP2;2 was highly expressed in mature sugar accumulating regions. Gene co-expression analysis revealed SvNIP2;2 expression was highly correlated with the expression of five putative sugar transporters expressed in the S. viridis internode. To explore the function of the proteins encoded by SvPIP2;1 and SvNIP2;2, we expressed them in Xenopus laevis oocytes and tested their permeability to water. SvPIP2;1 and SvNIP2;2 functioned as water channels in X. laevis oocytes and their permeability was gated by pH. Our results indicate that SvPIP2;1 may function as a water channel in developing stems undergoing cell expansion and SvNIP2;2 is a candidate for retrieving water and possibly a yet to be determined solute from mature internodes. Future research will investigate whether changing the function of these proteins influences stem growth and sugar yield in S. viridis.

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