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Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers.

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Τίτλος: Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers.
Συγγραφείς: Malysenko E; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany., Günther Pomorski T; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany.; Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark., Justesen BH; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany. bo.justesen@ruhr-uni-bochum.de.
Πηγή: Scientific reports [Sci Rep] 2026 Sep 15; Vol. 16 (1). Date of Electronic Publication: 2026 Sep 15.
Τύπος έκδοσης: Journal Article; Research Support, Non-U.S. Gov't
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
Imprint Name(s): Original Publication: London : Nature Publishing Group, copyright 2011-
Ιατρικοί όροι (MeSH): Proton-Translocating ATPases*/chemistry , Proton-Translocating ATPases*/isolation & purification , Proton-Translocating ATPases*/metabolism , Cell Membrane*/enzymology , Arabidopsis Proteins*/chemistry , Arabidopsis Proteins*/metabolism , Arabidopsis Proteins*/isolation & purification , Arabidopsis*/enzymology , Protein Multimerization*, Liposomes/metabolism ; Chromatography, Gel
Περίληψη: Plant H⁺-ATPases are activated through tightly regulated hexameric assembly, relieving autoinhibition via displacement of a regulatory domain during the oligomerization process. Sub-hexameric assembly states also exist but their role in activity regulation remains elusive. To characterize sub-hexameric plant H⁺-ATPases, we isolated homo-oligomers of the H⁺-ATPases AHA2 and determined their sizes with size exclusion chromatography multi-angle light scattering. AHA2 predominantly presented as a monomer but also assembled into stable dimers and larger complexes. Activity assays on solubilized and liposome-reconstituted AHA2 monomers and dimers revealed that dimerization did not affect enzymatic activity, suggesting that AHA2 dimerization does not represent a separate regulatory pathway. Instead, AHA2 dimers may serve as reservoirs for rapid hexamer assembly, facilitating the dynamic regulation of protein activity.
(© 2026. The Author(s).)
Competing Interests: Declarations. Competing interests: The authors declare no competing interests.
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Contributed Indexing: Keywords: Dimers; H+-ATPase; Membrane reconstitution; Oligomers; Proton pumping; SEC-MALS
Substance Nomenclature: EC 3.6.3.14 (Proton-Translocating ATPases)
0 (Arabidopsis Proteins)
0 (Liposomes)
EC 7.1.2.1 (AHA2 protein, Arabidopsis)
Entry Date(s): Date Created: 20260916 Date Completed: 20260916 Latest Revision: 20260918
Update Code: 20260918
PubMed Central ID: PMC13578685
DOI: 10.1038/s41598-026-70970-z
PMID: 42744987
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:2045-2322
DOI:10.1038/s41598-026-70970-z