pyrophosphatase/arabidopsis

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Overexpression of the halophyte Kalidium foliatum H⁺-pyrophosphatase gene confers salt and drought tolerance in Arabidopsis thaliana.

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According to sequences of H(+)-pyrophosphatase genes from GenBank, a new H(+)-pyrophosphatase gene (KfVP1) from the halophyte Kalidium foliatum, a very salt-tolerant shrub that is highly succulent, was obtained by using reverse transcription PCR and rapid amplification of cDNA ends methods. The

N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast.

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Expression of heterologous multispanning membrane proteins in Saccharomyces cerevisiae is a difficult task. Quite often, the use of multicopy plasmids where the foreign gene is under the control of a strong promoter does not guarantee efficient production of the corresponding protein. In the present

A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast.

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V-ATPases (vacuolar H+-ATPases) are a specific class of multi-subunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. Another simpler proton pump that co-localizes with the V-ATPase occurs in plants and many protists: the single-subunit

Identification and characterization of an ecto-pyrophosphatase activity in intact epimastigotes of Trypanosoma rangeli.

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In this study, we performed the molecular and biochemical characterization of an ecto-enzyme present in Trypanosoma rangeli that is involved with the hydrolysis of extracellular inorganic pyrophosphate. PCR analysis identified a putative proton-pyrophosphatase (H(+)-PPase) in the epimastigote forms

Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport.

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The membrane bounding the vacuole of plant cells contains two electrogenic proton pumps. These are the vacuolar H(+)-ATPase (EC 3.6.1.3), an enzyme common to all eukaryotes, and a vacuolar H(+)-translocating pyrophosphatase (EC 3.6.1.1), which is ubiquitous in plants but otherwise known in only a

Molecular cloning, characterization and expression analysis of isoforms encoding tonoplast-bound proton-translocating inorganic pyrophosphatase in tobacco.

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The tonoplast-bound proton-translocating inorganic pyrophosphatase (V-type PPase) and the proton ATPase (V-type ATPase) are electrogenic proton pumps guaranteeing the energization of solute transport across the tonoplast. Using an Arabidopsis thaliana PCR cDNA fragment corresponding to clone ATAVP3

Amino acid sequence similarities between the vacuolar proton-pumping inorganic pyrophosphatase and the c-subunit of F0F1-ATPases.

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Comparison of the Arabidopsis thaliana vacuolar proton-pumping inorganic pyrophosphatase with three F0F1-ATPase c-subunits revealed a strong similarity between a stretch containing amino acids 227-245 of the H(+)-PPase and a transmembrane alpha-helix of the c-subunits which contains the glutamate

Isolation and characterization of cDNAs encoding the vacuolar H(+)-pyrophosphatase of Beta vulgaris.

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The H(+)-pyrophosphatase (V-PPase) of plant vacuolar membranes catalyzes the electrogenic translocation of H+ from the cytosol to vacuole lumen and, in parallel with the vacuolar H(+)-ATPase located in the same membrane, establishes the inside-acid, inside-positive H(+)-electrochemical potential

Acidic residues necessary for pyrophosphate-energized pumping and inhibition of the vacuolar H+-pyrophosphatase by N,N'-dicyclohexylcarbodiimide.

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On the basis of a revised topological model of the vacuolar H+-pyrophosphatase (V-PPase; EC 3.6.1.1) derived from the analysis of four published sequences using two structure-predicting programs, TopPred II and MEMSAT, eight acidic amino acid residues located near or within transmembrane

Lack of H(+)-pyrophosphatase Prompts Developmental Damage in Arabidopsis Leaves on Ammonia-Free Culture Medium.

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The plant vacuolar H(+)-pyrophosphatase (H(+)-PPase) functions as a proton pump coupled with the hydrolysis of pyrophosphate (PPi). Loss-of-function mutants (fugu5s and vhp1) of the H(+)-PPase of Arabidopsis thaliana show clear morphological phenotypes in the cotyledons, caused by inhibition of

Lack of Vacuolar H ⁺ -Pyrophosphatase and Cytosolic Pyrophosphatases Causes Fatal Developmental Defects in Arabidopsis thaliana

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The cytosolic level of inorganic pyrophosphate (PPi) is finely regulated, with PPi hydrolyzed primarily by the vacuolar H⁺-pyrophosphatase (H⁺-PPase, VHP1/FUGU5/AVP1) and secondarily by five cytosolic soluble pyrophosphatases (sPPases; PPa1-PPa5) in Arabidopsis thaliana.

Roles of basic residues and salt-bridge interaction in a vacuolar H+-pumping pyrophosphatase (AVP1) from Arabidopsis thaliana.

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To investigate the possible role of basic residues in H+ translocation through vacuolar-type H+-pumping pyrophosphatases (V-PPases), conserved arginine and lysine residues predicted to reside within or close to transmembrane domains of an Arabidopsis thaliana V-PPase (AVP1) were subjected to

Evidence for a non-overlapping subcellular localization of the family I isoforms of soluble inorganic pyrophosphatase in Arabidopsis thaliana.

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Pyrophosphate is a byproduct of macromolecular biosynthesis and its degradation gives a thermodynamic impulse to cell growth. Soluble inorganic pyrophosphatases (PPa) are present in all living cells, but in plants and other Eukaryotes membrane-bound H+-pumping pyrophosphatases may compete with these

The H ⁺-Translocating Inorganic Pyrophosphatase From Arabidopsis thaliana Is More Sensitive to Sodium Than Its Na ⁺-Translocating Counterpart From Methanosarcina mazei

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Overexpression of membrane-bound K⁺-dependent H⁺-translocating inorganic pyrophosphatases (H⁺-PPases) from higher plants has been widely used to alleviate the sensitivity toward NaCl in these organisms, a strategy that had been previously tested in Saccharomyces

Co-expression of Pennisetum glaucum vacuolar Na⁺/H⁺ antiporter and Arabidopsis H⁺-pyrophosphatase enhances salt tolerance in transgenic tomato.
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Salinity is one of the major abiotic stresses affecting plant productivity. Tomato (Solanum lycopersicum L.), an important and widespread crop in the world, is sensitive to moderate levels of salt in the soil. To generate tomato plants that can adapt to saline soil, AVP1, a vacuolar

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pyrophosphatase/arabidopsis

Overexpression of the halophyte Kalidium foliatum H⁺-pyrophosphatase gene confers salt and drought tolerance in Arabidopsis thaliana.

N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast.

A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast.

Identification and characterization of an ecto-pyrophosphatase activity in intact epimastigotes of Trypanosoma rangeli.

Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport.

Molecular cloning, characterization and expression analysis of isoforms encoding tonoplast-bound proton-translocating inorganic pyrophosphatase in tobacco.

Amino acid sequence similarities between the vacuolar proton-pumping inorganic pyrophosphatase and the c-subunit of F0F1-ATPases.

Isolation and characterization of cDNAs encoding the vacuolar H(+)-pyrophosphatase of Beta vulgaris.

Acidic residues necessary for pyrophosphate-energized pumping and inhibition of the vacuolar H+-pyrophosphatase by N,N'-dicyclohexylcarbodiimide.

Lack of H(+)-pyrophosphatase Prompts Developmental Damage in Arabidopsis Leaves on Ammonia-Free Culture Medium.

Lack of Vacuolar H + -Pyrophosphatase and Cytosolic Pyrophosphatases Causes Fatal Developmental Defects in Arabidopsis thaliana

Roles of basic residues and salt-bridge interaction in a vacuolar H+-pumping pyrophosphatase (AVP1) from Arabidopsis thaliana.

Evidence for a non-overlapping subcellular localization of the family I isoforms of soluble inorganic pyrophosphatase in Arabidopsis thaliana.

The H +-Translocating Inorganic Pyrophosphatase From Arabidopsis thaliana Is More Sensitive to Sodium Than Its Na +-Translocating Counterpart From Methanosarcina mazei

Co-expression of Pennisetum glaucum vacuolar Na⁺/H⁺ antiporter and Arabidopsis H⁺-pyrophosphatase enhances salt tolerance in transgenic tomato.

Najkompletnejšia databáza liečivých bylín podporovaná vedou

Lack of Vacuolar H ⁺ -Pyrophosphatase and Cytosolic Pyrophosphatases Causes Fatal Developmental Defects in Arabidopsis thaliana

The H ⁺-Translocating Inorganic Pyrophosphatase From Arabidopsis thaliana Is More Sensitive to Sodium Than Its Na ⁺-Translocating Counterpart From Methanosarcina mazei