ATP-dependent Ca2+ transport in wheat root plasma membrane vesicles

Olbe, Malin; Sommarin, Marianne

doi:10.1034/j.1399-3054.1991.830401.x

Cited by 10 publications

(13 citation statements)

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“…As reported for native plant PM Ca 2+ -ATPase (RasiCaldogno et al 1987(RasiCaldogno et al , 1989Williams et al 1990;Olbe and Sommarin 1991;De Michelis et al 1993), D74-At-ACA8 expressed in yeast was highly sensitive to inhibition by fluorescein derivatives such as erythrosin B (EB) and eosin Y (EY): in the presence of 0.5 mM MgATP half-inhibition of the hydrolytic activity was observed in the presence of inhibitor concentrations of 25 and 7 nM, respectively (Fig. 9).…”

Section: Resultsmentioning

confidence: 53%

“…Table 2 shows the substrate specificity of D74-At-ACA8 and 794 HE fi KK D74-At-ACA8. As the native PM Ca 2+ -ATPase (Rasi-Caldogno et al 1989;Williams et al 1990;Olbe and Sommarin 1991;Carnelli et al 1992;Bonza et al 1998), D74-At-ACA8 expressed in yeast used MgITP or MgGTP about as well as MgATP, when the nucleoside triphosphates were supplied in the millimolar range, and this holds true also for the 794 HE fi KK D74-At-ACA8 mutant. Analysis of Ca 2+ uptake as a function of nucleoside triphosphate concentration (data not reported) showed that the 794 HE fi KK mutation slightly increased the K m of D74-At-ACA8 for both MgATP and MgITP: Ca 2+ uptake during the first minute was semi-saturated by 6 lM ATP or 25 lM ITP when driven by D74-At-ACA8 and by 8 lM ATP or 31 lM ITP when driven by the 794 HE fi KK D74-At-ACA8 mutant.…”

Section: Resultsmentioning

confidence: 82%

“…Plant type-IIB Ca 2+ -ATPases show some peculiar characteristics, which distinguish them from other members of type-II P-type ATPases. In particular, they share the unique property of using MgITP or MgGTP as substrates nearly as well as MgATP and they are extremely sensitive to inhibition by fluorescein derivatives such as EB and EY (Rasi-Caldogno et al 1987, 1989Williams et al 1990;Olbe and Sommarin 1991;Carnelli et al 1992;De Michelis et al 1993;Askerlund and Sommarin 1996;Bonza et al 1998;Geisler et al 2000a;Sze et al 2000). The effect of fluorescein derivatives on plant PM Ca 2+ -ATPase activity has been shown to be competitive with the nucleoside triphosphate substrate (De Michelis et al 1993), in agreement with ATP-protectable labeling of a conserved Lys residue in the conserved KGAXE motif of different P-type ATPases (Møller et al 1996;Brandt and Vanaman 1998;Palmgren 2001;Jorgensen et al 2003).…”

Section: Discussionmentioning

confidence: 99%

“…The type-IIB Ca 2+ -ATPases of plant cells share some common peculiar characteristics: (i) the autoinhibitory CaM-binding domain is localized in an extended cytosolic N-terminus rather than in the C-terminus as in animal PM Ca 2+ -ATPase; (ii) they are all able to use ITP or GTP as alternative substrates to ATP; (iii) they are extremely sensitive to inhibition by fluorescein and its derivatives which are known to bind at, or close to, the nucleotide-binding domain (RasiCaldogno et al 1987(RasiCaldogno et al , 1989Williams et al 1990;Olbe and Sommarin 1991;De Michelis et al 1993;Askerlund and Sommarin 1996;Bonza et al 1998;Geisler et al 2000a;Sze et al 2000).…”

Section: Introductionmentioning

confidence: 97%

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Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant

Bonza

Luoni

Michelis

2003

Planta

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A constitutively active form of At-ACA8, a plasma membrane Ca(2+)-ATPase from Arabidopsis thaliana (L.) Heynh., from which the first 74 amino acids containing the calmodulin-binding domain (delta74- At-ACA8) had been deleted, was expressed in Saccharomyces cerevisiae strain K616, which lacks the main endogenous active Ca(2+) transport systems. Delta74- At-ACA8 complemented the K616 phenotype, making it able to grow in a calcium-depleted medium. Delta74- At-ACA8 protein, which co-migrated with the endoplasmic reticulum marker BiP in a sucrose-density gradient, catalyzed MgATP-dependent Ca(2+) uptake and Ca(2+)-dependent MgATP hydrolysis, and retained the biochemical characteristics of the native plant plasma membrane Ca(2+)-ATPase (low specificity for nucleoside triphosphate, high sensitivity to inhibition by the fluorescein derivatives erythrosin B and eosin Y), thus confirming that it is correctly folded and functional. Substitution of the (794)HE residues (numbers refer to full-length At-ACA8) following the highly conserved TGDG(TV)NDP(AS)L motif in the cytoplasmic headpiece with two lysine residues generated an hyperactive protein, with a catalytic activity 2-fold higher than that of delta74- At-ACA8. The (794)HE-->KK mutant was also about 6-fold more sensitive than delta74- At-ACA8 to inhibition by vanadate, indicating that the mutation determines an increase in the proportion of enzyme in the E(2) state during the catalytic cycle.

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Section: Resultsmentioning

confidence: 53%

Section: Resultsmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

See 2 more Smart Citations

Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant

Bonza

Luoni

Michelis

2003

Planta

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“…4. Active efflux pumps are existing for example for Na + in maize (Schubert and Läu-chli 1990) and for Ca 2+ in wheat roots (Olbe and Sommarin 1991). They prevent the development of too-high concentrations in root cells.…”

Section: Mechanisms Of Toxicity and Tolerance In Higher Plantsmentioning

confidence: 99%

Essential and Toxic Effects of Macro‐, Trace and Ultratrace Elements for Higher Plants, Interactions and Requirement

Schilling¹

2004

Elements and Their Compounds in the Environment

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Calcium efflux of plasma membrane vesicles exposed to ELF magnetic fields—test of a nuclear magnetic resonance interaction model

Sun

Mogadam

Sommarin

et al. 2012

Bioelectromagnetics

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The question whether very weak, low frequency magnetic fields can affect biological matter is still under debate. The theoretical possibility of such an interaction is often questioned and the site of interaction in the cell is unknown. In the present study, the influence of extremely weak 60 Hz magnetic fields on the transport of Ca(2+) was studied in a biological system consisting of highly purified plasma membrane vesicles. We tested a newly proposed quantum mechanical model postulates that polarization of hydrogen nuclei can elicit a biological effect. Vesicles were exposed for half an hour at 32 °C and the calcium efflux was studied using radioactive (45) Ca(2+) as a tracer. A static magnetic field of 26 µT and time-varying magnetic fields with a frequency of 60 Hz and amplitudes between 0.6 and 6.3 µT were used. The predictions of the model, proposed by Lednev, that at a frequency of 60 Hz the biological effect under investigation would significantly be altered at the amplitudes of 1.3 and 3.9 µT could not be confirmed.

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ATP-dependent Ca2+ transport in wheat root plasma membrane vesicles

Cited by 10 publications

References 0 publications

Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant

Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant

Essential and Toxic Effects of Macro‐, Trace and Ultratrace Elements for Higher Plants, Interactions and Requirement

Calcium efflux of plasma membrane vesicles exposed to ELF magnetic fields—test of a nuclear magnetic resonance interaction model

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