ArticleJournal of bioenergetics and biomembranes2008
Cloning and sequencing of V-ATPase subunit d from mung bean and its function in passive proton transport.
Article in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023Review
- CRISPR/Cas9-mediated gene editing ofFrontiers in plant science · 2023Article
- The Plant V-ATPase.Frontiers in plant science · 2022Review
- The tether connecting cytosolic (N terminus) and membrane (C terminus) domains of yeast V-ATPase subunit a (Vph1) is required for assembly of V0 subunit d.The Journal of biological chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that vacuolar H+-ATPase subcomplex V(o) from mung bean contains subunit d, however, its sequence and function were unknown. In the present study, we report the cloning and recombinant over expression of subunit d from mung bean in E. coli. To study the function of subunit d, two vacuolar H+-ATPase subcomplexes V(o) from mung bean were purified-one containing subunits a and c(c',c") and the other containing subunits a, c(c',c") and d. After reconstitution of the purified V(o) subcomplexes into liposomes, the proton translocation was studied. Our results show that the V(o) subcomplex in the absence of subunit d is a passive proton channel, while the V(o) subcomplex in the presence of the subunit d is not. Taken together, our data supports the conclusion that the subunit d of the plant vacuolar H(+)-ATPase from mung bean is positioned at the central stalk and involved in the proton translocation across the tonoplast membrane.
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Registered trials
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