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1.
New Phytol ; 2024 Jul 26.
Artículo en Inglés | MEDLINE | ID: mdl-39060950

RESUMEN

The ALMT1 transporter aids malate secretion, chelating Al3+ ions to form nontoxic Al-malate complexes, believed to exclude Al from the roots. However, the extent to which malate secreted by ALMT1 is solely used for the exclusion of Al3+ or can be reutilized by plant roots for internal Al tolerance remains uncertain. In our investigation, we explored the impact of malate secretion on both external and internal Al resistance in Arabidopsis thaliana. Additionally, we delved into the mechanism by which the tonoplast-localized bacterial-type ATP-binding cassette (ABC) transporter complex STAR1/ALS3 promotes the degradation of the Al resistance transcription factor STOP1 to regulate ALMT1 expression. Our study demonstrates that the level of secreted malate influences whether the Al-malate complex is excluded from the roots or transported into root cells. The nodulin 26-like intrinsic protein (NIP) subfamily members NIP1;1 and NIP1;2, located in the plasma membrane, coordinate with STAR1/ALS3 to facilitate Al-malate transport from root apoplasm to the symplasm and eventually to the vacuoles for the internal Al detoxification. ALS3-dependent STAR1 interacts with and promotes the degradation of STOP1, regulating malate exudation. Our findings demonstrate the dual roles of malate exudation in external Al exclusion and Al absorption for internal Al detoxification.

2.
Plant Cell ; 36(3): 688-708, 2024 Feb 26.
Artículo en Inglés | MEDLINE | ID: mdl-37936326

RESUMEN

Aluminum (Al) stress triggers the accumulation of hydrogen peroxide (H2O2) in roots. However, whether H2O2 plays a regulatory role in aluminum resistance remains unclear. In this study, we show that H2O2 plays a crucial role in regulation of Al resistance, which is modulated by the mitochondrion-localized pentatricopeptide repeat protein REGULATION OF ALMT1 EXPRESSION 6 (RAE6). Mutation in RAE6 impairs the activity of complex I of the mitochondrial electron transport chain, resulting in the accumulation of H2O2 and increased sensitivity to Al. Our results suggest that higher H2O2 concentrations promote the oxidation of SENSITIVE TO PROTON RHIZOTOXICITY 1 (STOP1), an essential transcription factor that promotes Al resistance, thereby promoting its degradation by enhancing the interaction between STOP1 and the F-box protein RAE1. Conversely, decreasing H2O2 levels or blocking the oxidation of STOP1 leads to greater STOP1 stability and increased Al resistance. Moreover, we show that the thioredoxin TRX1 interacts with STOP1 to catalyze its chemical reduction. Thus, our results highlight the importance of H2O2 in Al resistance and regulation of STOP1 stability in Arabidopsis (Arabidopsis thaliana).


Asunto(s)
Proteínas de Arabidopsis , Arabidopsis , Factores de Transcripción/genética , Factores de Transcripción/metabolismo , Peróxido de Hidrógeno/metabolismo , Proteínas de Arabidopsis/metabolismo , Aluminio/toxicidad , Aluminio/metabolismo , Regulación de la Expresión Génica de las Plantas/genética , Arabidopsis/metabolismo , Raíces de Plantas/genética , Raíces de Plantas/metabolismo
3.
Plant Physiol ; 192(2): 1498-1516, 2023 05 31.
Artículo en Inglés | MEDLINE | ID: mdl-36823690

RESUMEN

Aluminum (Al) toxicity represents a primary constraint for crop production in acidic soils. Rice (Oryza sativa) is a highly Al-resistant species; however, the molecular mechanisms underlying its high Al resistance are still not fully understood. Here, we identified SAL1 (SENSITIVE TO ALUMINUM 1), which encodes a plasma membrane (PM)-localized PP2C.D phosphatase, as a crucial regulator of Al resistance using a forward genetic screen. SAL1 was found to interact with and inhibit the activity of PM H+-ATPases, and mutation of SAL1 increased PM H+-ATPase activity and Al uptake, causing hypersensitivity to internal Al toxicity. Furthermore, knockout of NRAT1 (NRAMP ALUMINUM TRANSPORTER 1) encoding an Al uptake transporter in a sal1 background rescued the Al-sensitive phenotype of sal1, revealing that coordination of Al accumulation in the cell, wall and symplasm is critical for Al resistance in rice. By contrast, we found that mutations of PP2C.D phosphatase-encoding genes in Arabidopsis (Arabidopsis thaliana) enhanced Al resistance, which was attributed to increased malate secretion. Our results reveal the importance of PP2C.D phosphatases in Al resistance and the different strategies used by rice and Arabidopsis to defend against Al toxicity.


Asunto(s)
Arabidopsis , Oryza , Monoéster Fosfórico Hidrolasas/metabolismo , Oryza/metabolismo , Arabidopsis/genética , Arabidopsis/metabolismo , Aluminio/toxicidad , Aluminio/metabolismo , Transporte Biológico , Proteínas de Transporte de Membrana/metabolismo , ATPasas de Translocación de Protón/genética , ATPasas de Translocación de Protón/metabolismo , Raíces de Plantas/metabolismo
4.
New Phytol ; 231(6): 2200-2214, 2021 09.
Artículo en Inglés | MEDLINE | ID: mdl-33454966

RESUMEN

Golgi is a critical compartment for both the reutilisation of the essential micronutrient manganese (Mn) and its detoxification. However, whether Mn plays a role in the Golgi remains to be demonstrated in plants. We characterised the function of PML3, a member of the Unknown Protein Family UPF0016, in Mn transport and the regulation of plant growth, Golgi glycosylation and cell wall biosynthesis in Arabidopsis. We also investigated the relationship of PML3 with NRAMP2, a trans-Golgi network localised Mn transporter. PML3-GFP is preferentially localised in the cis-Golgi. PML3 can transport Mn to rescue the hypersensitivity of yeast mutant Δpmr1 to excess Mn. Two mutant alleles of PML3 displayed reduced plant growth and impaired seed development under Mn-deficient conditions. The pml3 mutants also showed impaired Golgi glycosylation and cell wall biosynthesis under Mn deficiency. Double mutations of PML3 and NRAMP2 showed improved plant growth compared with that of single mutants under Mn deficiency, implying that PML3 and NRAMP2 play opposite roles in the regulation of Golgi Mn levels. Our results suggest that PML3 mediates Mn uptake into the Golgi compartments, which is required for proper protein glycosylation and cell wall biosynthesis under Mn-deficient conditions.


Asunto(s)
Proteínas de Arabidopsis , Arabidopsis , Proteínas de Transporte de Catión , Arabidopsis/genética , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Proteínas de Transporte de Catión/metabolismo , Pared Celular/metabolismo , Glicosilación , Aparato de Golgi/metabolismo , Manganeso/metabolismo
5.
Nanoscale ; 12(44): 22518-22526, 2020 Nov 19.
Artículo en Inglés | MEDLINE | ID: mdl-32996521

RESUMEN

Toxic and corrosive solutions are widely used in the preparation of abrasives and chemical mechanical polishing (CMP) of sapphire wafers, resulting in potential environmental pollution. Developing a novel green CMP technique to achieve light-emitting diode sapphire wafers is a significant challenge. In this study, a novel green CMP slurry, consisting of silica, sorbitol, aminomethyl propanol, and deionized water was developed for sapphire wafers. After CMP, the sapphire wafers were cleaned with deionized water and dried with compressed air, which is a green process. After CMP, the surface roughness Ra of the sapphire wafer surface with an area of 5 × 5 µm2 was 0.098 nm, which is the lowest surface roughness reported to date for sapphire wafers. Tetrahydroxy-coordinated Al(OH)4- ions were produced in the alkaline CMP slurry, and chelation occurred between sorbitol and these ions. The proposed green CMP has potential applications in the semiconductor and microelectronics industries.

6.
Adv Sci (Weinh) ; 7(4): 1903239, 2020 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-32099768

RESUMEN

Friction and wear remain the primary modes for energy dissipation in moving mechanical components. Superlubricity is highly desirable for energy saving and environmental benefits. Macroscale superlubricity was previously performed under special environments or on curved nanoscale surfaces. Nevertheless, macroscale superlubricity has not yet been demonstrated under ambient conditions on macroscale surfaces, except in humid air produced by purging water vapor into a tribometer chamber. In this study, a tribological system is fabricated using a graphene-coated plate (GCP), graphene-coated microsphere (GCS), and graphene-coated ball (GCB). The friction coefficient of 0.006 is achieved in air under 35 mN at a sliding speed of 0.2 mm s-1 for 1200 s in the developed GCB/GCS/GCP system. To the best of the knowledge, for the first time, macroscale superlubricity on macroscale surfaces under ambient conditions is reported. The mechanism of macroscale superlubricity is due to the combination of exfoliated graphene flakes and the swinging and sliding of the GCS, which is demonstrated by the experimental measurements, ab initio, and molecular dynamics simulations. These findings help to bridge macroscale superlubricity to real world applications, potentially dramatically contributing to energy savings and reducing the emission of carbon dioxide to the environment.

7.
Proc Natl Acad Sci U S A ; 115(42): E9962-E9970, 2018 10 16.
Artículo en Inglés | MEDLINE | ID: mdl-30266793

RESUMEN

Genomic imprinting is a form of epigenetic regulation resulting in differential gene expression that reflects the parent of origin. In plants, imprinted gene expression predominantly occurs in the seed endosperm. Maternal-specific DNA demethylation by the DNA demethylase DME frequently underlies genomic imprinting in endosperm. Whether other more ubiquitously expressed DNA demethylases regulate imprinting is unknown. Here, we found that the DNA demethylase ROS1 regulates the imprinting of DOGL4DOGL4 is expressed from the maternal allele in endosperm and displays preferential methylation and suppression of the paternal allele. We found that ROS1 negatively regulates imprinting by demethylating the paternal allele, preventing its hypermethylation and complete silencing. Furthermore, we found that DOGL4 negatively affects seed dormancy and response to the phytohormone abscisic acid and that ROS1 controls these processes by regulating DOGL4 Our results reveal roles for ROS1 in mitigating imprinted gene expression and regulating seed dormancy.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/fisiología , Metilación de ADN , Proteínas de Unión al ADN/metabolismo , Impresión Genómica , Proteínas Nucleares/metabolismo , Latencia en las Plantas , Semillas/fisiología , Factores de Transcripción/metabolismo , Proteínas de Arabidopsis/genética , ADN de Plantas/genética , Proteínas de Unión al ADN/genética , Epigénesis Genética , Regulación de la Expresión Génica de las Plantas , Proteínas Nucleares/genética , Factores de Transcripción/genética
8.
New Phytol ; 217(1): 179-193, 2018 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-28913895

RESUMEN

To cope with manganese (Mn) deficiency, plants have evolved an efficient transport system to uptake and redistribute Mn. However, the underlying molecular mechanisms remain to be demonstrated. We carried out a forward genetic screen in a root high-affinity Mn transporter nramp1 mutant background in Arabidopsis thaliana and identified an uncharacterized Mn transport NRAMP2. We investigated the effect of nramp2 mutation on root growth and reactive oxygen species (ROS) accumulation and we also examined the NRAMP2 expression pattern, and the subcellular localization and transport activity of NRAMP2. Mutation of NRAMP2 impaired plant growth, while overexpression of NRAMP2 improved plant growth under low Mn conditions. In the nramp2-1nramp1 double mutant, Mn deficiency inhibited root cell elongation and root hair development, which was associated with increased hydrogen peroxide (H2 O2 ) accumulation. NRAMP2 is preferentially localized to the trans-Golgi network. NRAMP2 has Mn influx transport activity in yeast, and mutation of NRAMP2 led to greater Mn retention in roots. Our results suggest that under Mn-deficient conditions, increased accumulation of H2 O2 is partially responsible for the root growth inhibition and NRAMP2 is involved in remobilization of Mn in Golgi for root growth.


Asunto(s)
Proteínas de Arabidopsis/metabolismo , Arabidopsis/genética , Proteínas de Transporte de Catión/metabolismo , Manganeso/metabolismo , Arabidopsis/crecimiento & desarrollo , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , Transporte Biológico , Proteínas de Transporte de Catión/genética , Aparato de Golgi/metabolismo , Peróxido de Hidrógeno/metabolismo , Mutación , Raíces de Plantas/metabolismo , Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/metabolismo , Red trans-Golgi/metabolismo
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