Paper · 1996 · New Phytologist

Regulatory effects of zinc on corn root plasma membrane H+‐ATPase

VERENA KASTRUP; SABINE STEIGER; ULRICH LÜTTGE; et al.

14
claims
28
verbatim quotes
12
citations
1
research areas
✓
Open access

Abstract

summary Effects of divalent metal ions (Zn, Mg, Mn), metal‐ATP complexes, and pH on the activity of the plasma membrane H + ‐ATPase were investigated. Both native vesicles, isolated by sucrose gradient centrifugation, and solubilized H + ‐ATPase, purified by linear glycerol gradient centrifugation were used. Zn, as well as Mg and Mn, stimulates the activity of H + ‐ATPase. Computer calculations of equilibrium concentrations have been used to separate the effects of individual ion complexes and free ionic forms on the enzyme activity. The calculations indicated that Zn as ZnATP + serves as a substrate of the plasma membrane H + ‐ATPase. The possibility of serving as substrate depends on the Zn/ATP ratio and the pH of the medium. The native H + ‐ATPase was activated by divalent metal ions in the order of Mg > Mn > Zn at pH 6.5 and in the order of Zn > Mn > Mg at pH 5.5 for total metal ion concentrations not higher than 3.0 mM. A Zn: ATP ratio of 0.6 at pH 5.5 gave more than 100% of the Mg‐dependent ATPase activity (Mg: ATP ratio of 1, pH 5.5). By contrast, free Zn 2+ is an effective inhibitor of ATP hydrolysis and H + transport with a strong dependence upon the pH of the medium. At pH 55 a total ZnSO 4 concentration of 1 mM induced no inhibition of ATP hydrolysis, whereas at pH 6.5 the same Zn concentration decreased the activity of the native and purified H + ‐ATPase to 49% and 34% (control activity: Mg: ATP ratio of 1, no ZnSO 4 ), respectively. We show that both activation by ZnATP 2− and inhibition by free Zn 2+ of the native plasma membrane H + ‐ATPase and the partially purified enzyme were strongly affected by the pH of the medium. The results provide evidence that Zn, in combination with the pH of the cytoplasm could play a role in regulating the plasma membrane H + ‐ATPase and thus in nutrient uptake of plant systems.

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Claims 14

Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Zn stimulated H+-ATPase activity.

Treatment
Zne0
Outcome
activity of H + ‐ATPasee0
Direction
stimulatese0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“Zn, as well as Mg and Mn, stimulates the activity of H + ‐ATPase.”

✓ located verbatim in the source · abstract, characters 310–375 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Mg stimulated H+-ATPase activity.

Treatment
Mge0
Outcome
activity of H + ‐ATPasee0
Direction
stimulatese0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“Zn, as well as Mg and Mn, stimulates the activity of H + ‐ATPase.”

✓ located verbatim in the source · abstract, characters 310–375 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Mn stimulated H+-ATPase activity.

Treatment
Mne0
Outcome
activity of H + ‐ATPasee0
Direction
stimulatese0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“Zn, as well as Mg and Mn, stimulates the activity of H + ‐ATPase.”

✓ located verbatim in the source · abstract, characters 310–375 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Mechanismobservedoriginal resultsimulated

Claim · model-written summary

Calculations indicated ZnATP+ serves as a substrate for the enzyme.

Gene
plasma membrane H + ‐ATPasee0
Compound
ZnATP +e0
Outcome
serves as a substratee0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“The calculations indicated that Zn as ZnATP + serves as a substrate of the plasma membrane H + ‐ATPase.”

✓ located verbatim in the source · abstract, characters 540–643 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

At pH 6.5 native enzyme activation ranked Mg > Mn > Zn.

Outcome
Mg > Mn > Zne0
Direction
activatede0
Qualifier
pH 6.5e0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“The native H + ‐ATPase was activated by divalent metal ions in the order of Mg > Mn > Zn at pH 6.5”

✓ located verbatim in the source · abstract, characters 738–836 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

At pH 5.5 native enzyme activation ranked Zn > Mn > Mg.

Outcome
Zn > Mn > Mge0
Qualifier
pH 5.5e0

Not reportedDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“in the order of Zn > Mn > Mg at pH 5.5 for total metal ion concentrations not higher than 3.0 mM”

✓ located verbatim in the source · abstract, characters 841–937 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

A Zn: ATP ratio of 0.6 at pH 5.5 yielded over 100% of Mg-dependent ATPase activity.

Treatment
Zn: ATP ratio of 0.6e0
Outcome
ATPase activitye0
Direction
more thane0
Value
100%e0
Comparator
Mg: ATP ratio of 1e0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“A Zn: ATP ratio of 0.6 at pH 5.5 gave more than 100% of the Mg‐dependent ATPase activity (Mg: ATP ratio of 1, pH 5.5)”

✓ located verbatim in the source · abstract, characters 939–1056 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Free Zn2+ inhibited ATP hydrolysis.

Treatment
free Zn 2+e0
Outcome
ATP hydrolysise0
Direction
inhibitore0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“free Zn 2+ is an effective inhibitor of ATP hydrolysis and H + transport”

✓ located verbatim in the source · abstract, characters 1071–1143 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Free Zn2+ inhibited H+ transport.

Treatment
free Zn 2+e0
Outcome
H + transporte0
Direction
inhibitore0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“free Zn 2+ is an effective inhibitor of ATP hydrolysis and H + transport”

✓ located verbatim in the source · abstract, characters 1071–1143 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultno effectmeasured

Claim · model-written summary

At pH 55, 1 mM ZnSO4 did not inhibit ATP hydrolysis.

Treatment
ZnSO 4 concentration of 1 mMe0
Outcome
ATP hydrolysise0
Direction
no inhibitione0
Qualifier
pH 55e0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“At pH 55 a total ZnSO 4 concentration of 1 mM induced no inhibition of ATP hydrolysis”

✓ located verbatim in the source · abstract, characters 1196–1281 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

At pH 6.5, 1 mM zinc lowered native enzyme activity to 49% of control.

Treatment
Zn concentratione0
Outcome
activity of the native and purified H + ‐ATPasee0
Direction
decreasede0
Value
49%e0
Comparator
control activity: Mg: ATP ratio of 1, no ZnSO 4e0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“at pH 6.5 the same Zn concentration decreased the activity of the native and purified H + ‐ATPase to 49% and 34% (control activity: Mg: ATP ratio of 1, no ZnSO 4 )”

✓ located verbatim in the source · abstract, characters 1291–1454 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

At pH 6.5, 1 mM zinc lowered purified enzyme activity to 34% of control.

Treatment
Zn concentratione0
Outcome
activity of the native and purified H + ‐ATPasee0
Direction
decreasede0
Value
34%e0
Comparator
control activity: Mg: ATP ratio of 1, no ZnSO 4e0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“at pH 6.5 the same Zn concentration decreased the activity of the native and purified H + ‐ATPase to 49% and 34% (control activity: Mg: ATP ratio of 1, no ZnSO 4 )”

✓ located verbatim in the source · abstract, characters 1291–1454 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

pH strongly affected zinc-complex activation of native and partly purified H+-ATPase.

Outcome
activation by ZnATP 2−e0
Setting
pH of the mediume0

Not reportedDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“activation by ZnATP 2− and inhibition by free Zn 2+ of the native plasma membrane H + ‐ATPase and the partially purified enzyme were strongly affected by the pH of the medium”

✓ located verbatim in the source · abstract, characters 1488–1662 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

pH strongly affected free-zinc inhibition of native and partly purified H+-ATPase.

Outcome
inhibition by free Zn 2+e0
Setting
pH of the mediume0

Not reportedDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Zea mays subsp. mays
Zea mays subsp. mays · TaxonDominicus Johannes Bergsma · CC BY-SA 4.0 · Wikimedia Commons ↗

Verbatim

e0

“activation by ZnATP 2− and inhibition by free Zn 2+ of the native plasma membrane H + ‐ATPase and the partially purified enzyme were strongly affected by the pH of the medium”

✓ located verbatim in the source · abstract, characters 1488–1662 · show in text ↑
t0

“corn root”

✓ located verbatim in the source · title, characters 30–39 · show in text ↑

zinc sulfate · molecular: metabolites · Zea mays (maize)Positive and negative results

10 papers: 7 positive, 3 negative or no effect

2 papers in the same direction as this paper · 7 in the opposite direction

  1. positive
  2. positive
  3. positive

6 papers more in this group

See all 10 papers →

Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.