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pyrophosphatase/oryza sativa
Врската е зачувана во таблата со исечоци
Страница 1 од 18 резултати
Isolation and characterization of cDNAs encoding vacuolar H(+)-pyrophosphatase isoforms from rice (Oryza sativa L.).
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The vacuolar H(+)-pyrophosphatase (V-PPase) is an electrogenic H+ pump, which was found in the plant vacuolar membrane. Two cDNA clones (OVP1 and OVP2) encoding the V-PPase were isolated from cultured rice (Oryza sativa L.) cells and subsequently sequenced. The sequence analysis has revealed that
Identification of the gene structure and promoter region of H+-translocating inorganic pyrophosphatase in rice (Oryza sativa L. ).
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In order to determine the gene structure and promoter region of vacuolar H+-translocating inorganic pyrophosphatase (V-PPase), we isolated the genomic clones using a rice BAC library and probes derived from rice V-PPase cDNA (OVP1). The entire OVP1 gene is approx. 5.4 kb in length, and seven introns
Silicon regulates the expression of vacuolar H+-pyrophosphatase 1 and decreases cadmium accumulation in rice (Oryza sativa L.).
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Deciphering the mechanism of Cd accumulation in crops is imperative for minimizing soil-to-plant transfer of Cd to improve safe food production. Hydroponic experiments were performed examining Cd accumulation, growth performance and protein characteristics of two rice genotypes, Xiushui817 and
Vacuolar H(+)-translocating pyrophosphatase is induced by anoxia or chilling in seedlings of rice.
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The present study was undertaken to determine whether vacuolar H(+)-pyrophosphatase (V-PPase) might replace vacuolar H(+)-ATPase under energy stress due to anoxia or chilling in anoxia-tolerant species such as rice (Oryza sativa L.) and corn (Zea mays L.). The relative transcript level of V-PPase in
Rice plastidial N-glycosylated nucleotide pyrophosphatase/phosphodiesterase is transported from the ER-golgi to the chloroplast through the secretory pathway.
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A nucleotide pyrophosphatase/phosphodiesterase (NPP) activity that catalyzes the hydrolytic breakdown of ADP-glucose (ADPG) has been shown to occur in the plastidial compartment of both mono- and dicotyledonous plants. To learn more about this enzyme, we purified two NPPs from rice (Oryza sativa)
OVP1, a vacuolar H+-translocating inorganic pyrophosphatase (V-PPase), overexpression improved rice cold tolerance.
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Vacuolar H(+)-translocating inorganic pyrophosphatase (V-PPase, EC 3.6.1.1) is an electrogenic proton pump and has been studied in many plants. Here we report characterization of the OVP1 gene from rice (Oryza sativa L.). Quantitative reverse transcriptase-polymerase chain reaction analysis
Rapid reconstitution of tonoplast H(+)-translocating pyrophosphatase from cultured rice cells into liposomes.
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We report the rapid and functional reconstitution of H(+)-pyrophosphatase (H(+)-PPase) from the tonoplast of cultured rice (Oryza sativa L.) cells to proteoliposomes. The CHAPS-solubilized H(+)-PPase was incorporated into liposomes by gel-filtration. Both the activities of PPi-hydrolysis and
N-Glycomic and Microscopic Subcellular Localization Analyses of NPP1, 2 and 6 Strongly Indicate that trans-Golgi Compartments Participate in the Golgi to Plastid Traffic of Nucleotide Pyrophosphatase/Phosphodiesterases in Rice.
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Nucleotide pyrophosphatase/phosphodiesterases (NPPs) are widely distributed N-glycosylated enzymes that catalyze the hydrolytic breakdown of numerous nucleotides and nucleotide sugars. In many plant species, NPPs are encoded by a small multigene family, which in rice are referred to NPP1-NPP6
Apoplasmic loading in the rice phloem supported by the presence of sucrose synthase and plasma membrane-localized proton pyrophosphatase.
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OBJECTIVE
Although Oryza sativa (rice) is one of the most important cereal crops, the mechanism by which sucrose, the major photosynthate, is loaded into its phloem is still a matter of debate. Current opinion holds that the phloem loading pathway in rice could involve either a symplasmic or an
Expression of vacuolar H+-pyrophosphatase (OVP3) is under control of an anoxia-inducible promoter in rice.
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Vacuolar H(+)-pyrophosphatase (V-PPase) expression increases in a number of abiotic stresses and is thought to play a role in adaptation to abiotic stresses. This paper reports on the regulation of six V-PPase genes in rice (Oryza sativa L.) coleoptiles under anoxia, using flood tolerant and
Comparative proteomic and physiological characterisation of two closely related rice genotypes with contrasting responses to salt stress
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Salinity is a limiting factor affecting crop growth. We evaluated the responses of a salt-tolerant recombinant inbred rice (Oryza sativa L.) line, FL478, and the salt-sensitive IR29. Seedlings were exposed to salt stress and the growth rate was monitored to decipher the effect of long-term stress.
Transcriptomic adaptations in rice suspension cells under sucrose starvation.
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Sugar is an important resource for energy generation and developmental regulation in plants, and sucrose starvation causes enormous changes in cellular morphology, enzyme activities and gene expression. Genome-wide gene expression profiling provides a comprehensive knowledge of gene expression under
Mutagenesis Reveals That the OsPPa6 Gene Is Required for Enhancing the Alkaline Tolerance in Rice.
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Alkaline stress (AS) is one of the abiotic stressful factors limiting plant's growth and development. Inorganic pyrophosphatase is usually involved in a variety of biological processes in plant in response to the abiotic stresses. Here, to clarify the responsive regulation of inorganic
Stress response of plant H+-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae: a potentially useful mechanism for the development of stress-tolerant organisms.
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The simple proton-translocating inorganic pyrophosphatase (H(+)-PPase) found in plants and protists is an evolutionally conserved, essential enzyme that catalyzes the hydrolysis of pyrophosphate (PPi). Little is known about the functional contribution of H(+)-PPase to the cellular response to
Isolation and characterization of a Na+/H+ antiporter gene from the halophyte Atriplex gmelini.
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With a homologous gene region we successfully isolated a Na+/H+ antiporter gene from a halophytic plant, Atriplex gmelini, and named it AgNHX1. The isolated cDNA is 2607 bp in length and contains one open reading frame, which comprises 555 amino acid residues with a predicted molecular mass of 61.9
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