2 edition of H-ATPase (ATP synthase)--structure, function, biogenesis: The FF complex of coupling membranes (ICSU Press symposium series) found in the catalog.
H-ATPase (ATP synthase)--structure, function, biogenesis: The FF complex of coupling membranes (ICSU Press symposium series)
by Published on behalf of the ICSU Press by Adriatica Editrice
Written in English
|The Physical Object|
|Number of Pages||454|
Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal and environmental cues, including auxin, blue light, and fungal elicitors. However, little is known about the signaling components that mediate this regulation. Here, we report that an Arabidopsis thaliana Ser/Thr protein kinase, PKS5, is a negative regulator of the . The Arabidopsis PM H -ATPase AHA2 interacts with VAMP7C. The longin domain of VAMP interacts with AHA2 to inhibit PM H+-ATPase activity on the plasma membrane. The alkaline phenotype of vamp and vamp vamp vamp triple mutants suggested that VAMP7C was functionally redundant in regulating PM H+-ATPase activity in response to high.
An H +-ATPase gene, HA1, has been identified in Medicago truncatula that is expressed specifically in arbuscule-containing cells of mycorrhizal roots (Krajinski et al., ). To test the hypothesis that HA1 is required to energize phosphate transport to the plant, we isolated an ha mutant of M. truncatula and compared its symbiotic. The vacuolar (H+)-ATPases (V-ATPases) are a family of ATP-driven proton pumps and they have been associated with cancer invasion, metastasis, and drug resistance. Despite the clear involvement of V-ATPases in cancer, the therapeutic use of V-ATPase-targeting small molecules has not reached human clinical trials to date. Thus, V-ATPases are emerging as important .
Abstract. Approximately 30%–40% of hydrogen ion transport in the proximal tubule, and most or all of proton transport in the distal nephron, is generated by proton pumps belonging to the vacuolar class of H + WATPases. This ubiquitous type of proton pump is found in all eukaryotic cells, where it serves to acidify intracellular compartments, such as endosomes, lysosomes, . This lesson explores how the Na/K-ATPase or Na-pump uses ATP to transport sodium out of the cell and potassium into the cells. In particular, the various conformational states of the Na/K-ATPase.
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Handbook of H+-ATPases - Kindle edition by Nakamura, Suguru. Download it once and read it on your Kindle device, PC, phones or tablets. Use features like bookmarks, note taking and highlighting while reading Handbook of H+cturer: Pan Stanford.
The proton-pumping ATPase (H +-ATPase) of the plant plasma membrane generates the proton motive force across the plasma membrane that is necessary to activate most of the ion and metabolite recent years, important progress has been made concerning the identification and organization of H +-ATPase genes, their expression, and Cited by: Since multiple ATPase cycles (i.e., AAA1, AAA3, and AAA4 cycles) simultaneously run in a single motor domain, it is necessary to identify which ATPase cycle is responsible for the linker swing.
To dissect the coupling of the linker swing and ATPase cycles, the Walker A mutation was introduced into AAA1, AAA3, or AAA4. 34,40 Pre-steady-state kinetic measurements of ATP.
The H +-ATPase (proton pump) is a hetero-oligomeric protein assembly consisting of a proteolipid (V0) and a catalytic part (V1) with exchangeable SUs.
The V0 and V1 part are connected by a stalk containing an a-SU, but the V1 H-ATPase book can dissociate, thus leaving behind the V0 channel part (Boesen and Nissen, ) to which a role in membrane.
Theodor Burdyga, Richard J. Paul, in Muscle, Plasma Membrane Ca H-ATPase book ATPase. PMCA, a calmodulin-dependent calcium ATPase, is a ubiquitous transport protein that acts to extrude Ca 2+ across the plasmalemma (for review see 38).It also has been reported to counter-transport a proton, which in turn might affect its activity.
The plasma membrane H + ‐ATPase of fungi and plants is a single polypeptide of fewer than 1, residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi‐subunit F O F 1 ATPase of mitochondria, which is also a proton pump, but.
In book: An Innovative Approach to Understanding and Treating Cancer: Targeting pH, pp This protein shares high sequence homology to the yeast vacuolar H(+)-ATPase.
Saline-alkali soil is a major environmental constraint impairing plant growth and crop productivity. In this study, we identified a Ca2+ sensor/kinase/plasma membrane (PM) H+-ATPase module as a central component conferring alkali tolerance in Arabidopsis (Arabidopsis thaliana).
We report that the SCaBP3 (SOS3-LIKE CALCIUM BINDING PROTEIN3)/CBL7 (CALCINEURIN B. This H +-ATPase may account for up to 60% of the ATP hydrolysis in the cell.
To investigate whether other inhibitors of the plasma membrane H + -ATPase could affect the oscillations, we tested the effect of omeprazole, which is a strong inhibitor of the H + -K + -ATPase of the gastric mucosa (40). The structure and function of the gastric H,K-ATPase.
The primary structure of the gastric H,K-ATPase α subunits containing the catalytic site was first elucidated in the rat  and then in the hog , rabbit , dog , and human .This catalytic subunit consists of 1, or 1, amino acids in length in all species.
Abstract. Plant plasma membrane H +-ATPase acts as a primary transporter via proton pumping and regulates diverse physiological responses by controlling secondary solute transport, pH homeostasis, and membrane orylation of the penultimate threonine and the subsequent binding of proteins in the carboxyl terminus of the enzyme are required for H +-ATPase.
Structure and Mechanism of a Rotary Motor. The V-ATPases are large multi-subunit complexes that hydrolyze ATP to pump protons across biological membranes [1, 3].The subunit model of the yeast V-ATPase is shown in Figure enzyme is composed of two functional domains, termed V 1 and V kDa membrane peripheral V 1 domain is.
The removal of the auto-inhibitory domain of H + ATPase is characterized by (a) a higher degree of stimulation in H +-pumping than in hydrolytic ATPase activity, (b) an increase in V max and a decrease inK m, (c) a shift of pH optimum toward more alkaline values, and (d) sensitivity of the enzyme to vanadate remains unchanged (Palmgren et al.
VAMP Interacts with PM H +-ATPase AHA1. ABA inhibits PM H +-ATPase activity (Merlot et al., ; Planes et al., ).To identify components involved in this inhibition, we first confirmed this result. Four-week-old Arabidopsis Col-0 plants were treated with m m NaHCO 3 for 2 d to induce PM H +-ATPase activity and then treated with or without 10 µ m of ABA for 1 d.
The H +-ATPase has N- and C-terminal segments, which emerge into the cytoplasm (Duby & Boutry, ). The structure of plasma membrane H +-ATPase consists of domains A, M, P, N, and R. The A-domain (actuator) consists of the N-terminal segment and small loop.
The M-domain (membrane) corresponds to a transmembrane domain with ten helices, M1 to M PM H +-ATPase. A key function of the PM H +-ATPase is to generate a proton electrochemical gradient, thereby providing the driving force for the uptake and efflux of ions and metabolites across the plasma ial nutrients, such as nitrate and sulfate, are taken into cells against concentration and electrical gradients by H +-coupled anion symporters (Figure 1.
Introduction. The plasma membrane (PM) H +-ATPase is an electrogenic pump that exports cellular addition to generating a transmembrane chemical gradient of H + (ΔpH; acidic on the outside), it also establishes an electrical gradient (the membrane potential; negative on the inside).
As almost all other transport proteins in the plant PM are energized by. The Plasma Membrane H +-ATPase. The major ion pumps in plants and fungi are plasma membrane H +r pumps are not found in animals, in which the equivalent enzyme is the Na + /K +-ATPase, which in turn is absent from r, both types of pumps are evolutionarily related and belong to the superfamily of P-type ATPases (Axelsen and.
The emission wavelength was recorded at nm. The H +-ATPase activity was determined as the initial rate of pH i recovery (dpH i /dt, pH/min) from an acid load induced by NH 3 / NH 4 + withdrawal in an Na +-free solution. The dpH i /dtwas calculated by fitting to a linear equation the first 3 min of the time course of pH i recovery.
Increased metabolic acid production and upregulation of net acid extrusion render pH homeostasis profoundly dysregulated in many cancers. Plasma membrane activity of vacuolar H+ ATPases (V-ATPases) has been implicated in acid extrusion and invasiveness of some cancers, yet often on the basis of unspecific inhibitors.
Serving as a membrane anchor directing V. In eukaryotic cells, compartments of the highly dynamic endomembrane system are acidified to varying degrees by the activity of vacuolar H+-ATPases (V-ATPases). In the Arabidopsis thaliana genome, most V-ATPase subunits are encoded by small gene families, thus offering potential for a multitude of enzyme complexes with different kinetic properties and localizations.Yeast Plasma‐Membrane H + ‐ATPase: Model System for Studies of Structure, Function, Biogenesis, and Regulation (Pages: ) Silvia Lecchi Carolyn W.
Slayman.P-type proton ATPase (or plasma membrane H +-ATPase) is found in the plasma membranes of eubacteria, archaea, protozoa, fungi and it serves as a functional equivalent to the Na + /K + ATPase of animal cells; i.e.
it energizes the plasma membrane by forming an electrochemical gradient of protons (Na + in animal cells), that in turn drives secondary active .