ArticleThe Journal of biological chemistry2012
Reconstitution of vacuolar-type rotary H+-ATPase/synthase from Thermus thermophilus.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structures of multisubunit membrane complexes with the CRYO ARM 200.Microscopy (Oxford, England) · 2022Article
- Mechanical inhibition of isolated VeLife · 2020Article
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Cryo EM structure of intact rotary HNature communications · 2018Article
- The ingenious structure of central rotor apparatus in VoV1; key for both complex disassembly and energy coupling between V1 and Vo.PloS one · 2015Article
- Molecular basis of ADP inhibition of vacuolar (V)-type ATPase/synthase.The Journal of biological chemistry · 2014Article
- Evaluation of Immune Response and Protection Induced by V-ATPase Subunit F as DNA Vaccine AgainstAvicenna journal of medical biotechnologyArticle
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Authors and funding
2 authors.
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Abstract
Vacuolar-type rotary H(+)-ATPase/synthase (V(o)V(1)) from Thermus thermophilus, composed of nine subunits, A, B, D, F, C, E, G, I, and L, has been reconstituted from individually isolated V(1) (A(3)B(3)D(1)F(1)) and V(o) (C(1)E(2)G(2)I(1)L(12)) subcomplexes in vitro. A(3)B(3)D and A(3)B(3) also reconstituted with V(o), resulting in a holoenzyme-like complexes. However, A(3)B(3)D-V(o) and A(3)B(3)-V(o) did not show ATP synthesis and dicyclohexylcarbodiimide-sensitive ATPase activity. The reconstitution process was monitored in real time by fluorescence resonance energy transfer (FRET) between an acceptor dye attached to subunit F or D in V(1) or A(3)B(3)D and a donor dye attached to subunit C in V(o). The estimated dissociation constants K(d) for V(o)V(1) and A(3)B(3)D-V(o) were ∼0.3 and ∼1 nm at 25 °C, respectively. These results suggest that the A(3)B(3) domain tightly associated with the two EG peripheral stalks of V(o), even in the absence of the central shaft subunits. In addition, F subunit is essential for coupling of ATP hydrolysis and proton translocation and has a key role in the stability of whole complex. However, the contribution of the F subunit to the association of A(3)B(3) with V(o) is much lower than that of the EG peripheral stalks.
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