ArticleThe Journal of biological chemistry2015
Metal Fluoride Inhibition of a P-type H+ Pump: STABILIZATION OF THE PHOSPHOENZYME INTERMEDIATE CONTRIBUTES TO POST-TRANSLATIONAL PUMP ACTIVATION.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Priestia megaterium cells are primed for surviving lethal doses of antibiotics and chemical stress.Communications biology · 2025Article
- Gram-positive bacteria are primed for surviving lethal doses of antibiotics and chemical stress.bioRxiv : the preprint server for biology · 2024Article
- The Seed and the Metabolism Regulation.Biology · 2022Review
- STOP1 activates NRT1.1-mediated nitrate uptake to create a favorable rhizospheric pH for plant adaptation to acidity.The Plant cell · 2021Article
- Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.Science advances · 2021Article
- Plasma membrane HNature communications · 2020Article
- Fluoride contributes to the shaping of microbial community in high fluoride groundwater in Qiji County, Yuncheng City, China.Scientific reports · 2019Article
- Isolation of native plasma membrane HFEBS open bio · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plasma membrane H(+)-ATPase is a P-type ATPase responsible for establishing electrochemical gradients across the plasma membrane in fungi and plants. This essential proton pump exists in two activity states: an autoinhibited basal state with a low turnover rate and a low H(+)/ATP coupling ratio and an activated state in which ATP hydrolysis is tightly coupled to proton transport. Here we characterize metal fluorides as inhibitors of the fungal enzyme in both states. In contrast to findings for other P-type ATPases, inhibition of the plasma membrane H(+)-ATPase by metal fluorides was partly reversible, and the stability of the inhibition varied with the activation state. Thus, the stability of the ATPase inhibitor complex decreased significantly when the pump transitioned from the activated to the basal state, particularly when using beryllium fluoride, which mimics the bound phosphate in the E2P conformational state. Taken together, our results indicate that the phosphate bond of the phosphoenzyme intermediate of H(+)-ATPases is labile in the basal state, which may provide an explanation for the low H(+)/ATP coupling ratio of these pumps in the basal state.
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