Cross-linking of the δ Subunit to One of the Three α Subunits Has No Effect on Functioning, as Expected if δ Is a Part of the Stator That Links the F1 and F0 Parts of the Escherichia coli ATP Synthase

Ogilvie, Isla; Aggeler, Robert; Capaldi, Roderick A.

doi:10.1074/jbc.272.26.16652

Cited by 141 publications

(121 citation statements)

References 45 publications

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“…We now can say that there is enough evidence that the structure is likely to be quite similar to models such as proposed by Duncan et al 1995 and closely to a configuration as presented by Ogilvie et al (1997) or calculated by Engelbrecht and Junge (1997). The latter models show besides a central stalk a stator comprised of b-subunits as a second connecting mass between F 1 and F 0 .…”

Section: Introductionmentioning

confidence: 86%

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Boekema¹,

Ubbink-Kok

Lolkema

et al. 1998

Photosynthesis Research

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F-type and V-type ATPases couple synthesis or hydrolysis of ATP to the translocation of H + or Na + across biological membranes and have similarities in structure and mechanism. In both types of enzymes three main parts can be distinguished: headpiece, membrane-bound piece and stalk region. We report on structural details of the membrane sector and stalk region, including the stator, of V-type ATPase from Clostridium fervidus, as determined by electron microscopy. Besides visualization of the stator structure, one of the main findings is that in certain projections the central stalk connecting V 1 and V 0 makes an angle of about 70 • with the membrane. Implications for the subunit arrangement in V-type and F-type ATPase are discussed.

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Section: Introductionmentioning

confidence: 86%

Untitled

Boekema¹,

Ubbink-Kok

Lolkema

et al. 1998

Photosynthesis Research

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“…Electron microscopic analysis of the V-ATPase from Clostridium fervidus (25) and from clathrincoated vesicles 2 indicates that the peripheral V 1 domain is attached to the integral V 0 domain both by a central stalk and by a peripheral stalk, as has been observed for the F-ATPases (20). In the case of the F-ATPases, the central stalk is composed of the ␥ and ⑀ subunits while the peripheral stalk is composed of the ␦ subunit and the soluble domains of subunit b (21). Because the D subunit, like ␥ of F 1 , is predicted to have a very high ␣-helical content (50), we suggest that subunit D is the V-ATPase homolog to ␥, placing subunit D, and subunit F with which it interacts, in the central stalk.…”

Section: Subunits H F and G And The 45-kda Glycoprotein In The V-atmentioning

confidence: 93%

“…We have suggested, based on mutagenesis studies (30,45), that the 100-kDa subunit corresponds to the V-ATPase homolog of the F-ATPase a subunit, which functions not only in proton translocation (12,46,47) but as part of the stator that is held rigid relative to the ␣ 3 ␤ 3 hexamer (21). Most recently we have demonstrated that the large amino-terminal domain of the 100-kDa subunit is oriented toward the cytoplasmic side of the membrane (35), making it a likely candidate for forming part of the stator structure in the V-ATPases.…”

Section: Discussionmentioning

confidence: 99%

“…The structure of the peripheral F 1 domain of the mitochondrial F-ATPase has been determined by x-ray crystallography and shown to consist of a hexamer of alternating ␣ and ␤ subunits surrounding a central cavity containing the highly ␣-helical ␥ subunit (18,19). F 1 appears to be attached to the F 0 domain via both a central stalk (believed to include both the ␥ and ⑀ subunits) and a peripheral stalk (composed of the ␦ subunit and the soluble portions of subunit b) (20,21). The F 0 domain contains a ring of c subunits with the a and b subunits to one side (12,23).…”

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confidence: 99%

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Subunit Interactions in the Clathrin-coated Vesicle Vacuolar (H+)-ATPase Complex

Vasilyeva

Forgac

1999

Journal of Biological Chemistry

130

177

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The vacuolar (H ؉ )-ATPases (or V-ATPases) are structurally related to the F 1 F 0 ATP synthases of mitochondria, chloroplasts and bacteria, being composed of a peripheral (V 1 ) and an integral (V 0 ) domain. To further investigate the arrangement of subunits in the V-ATPase complex, covalent cross-linking has been carried out on the V-ATPase from clathrin-coated vesicles using three different cross-linking reagents. Crosslinked products were identified by molecular weight and by Western blot analysis using polyclonal antibodies raised against individual V-ATPase subunits. In the intact V 1 V 0 complex, evidence for cross-linking of subunits C and E, D and F, as well as E and G by disuccinimidyl glutarate was obtained, while in the free V 1 domain, cross-linking of subunits H and E was also observed. Subunits C and E as well as D and E could be cross-linked by 1-ethyl-3-(dimethylaminopropyl)carbodiimide, while subunits a and E could be cross-linked by 4-(N-maleimido)benzophenone. It was further demonstrated that it is possible to treat the V-ATPase with potassium iodide and MgATP in such a way that while subunits A, B, and H are nearly quantitatively removed, significant amounts of subunits C, D, E, and F remain attached to the membrane, suggesting that one or more of these latter subunits are in contact with the V 0 domain. In addition, treatment of the V-ATPase with cystine, which modifies Cys-254 of the catalytic A subunit, results in dissociation of subunit H, suggesting communication between the catalytic nucleotide binding site and subunit H. Finally, the stoichiometry of subunits F, G, and H were determined by quantitative amino acid analysis. Based on these and previous observations, a new structural model of the V-ATPase from clathrincoated vesicles is proposed.The vacuolar (H ϩ )-ATPases (or V-ATPases) 1 are a family of ATP-dependent proton pumps that carry out proton transport across both intracellular membranes and, in some cases, the plasma membrane (1-6). Acidification of intracellular compartments is important for such processes as protein degradation, intracellular protein targeting, and receptor-mediated endocytosis (1-6), while V-ATPases in the plasma membrane function in renal acidification, bone resorption, and tumor metastasis (7-9).The V-ATPase is a heteroligomeric complex of molecular mass approximately 800 kDa composed of at least 13 different subunits arranged into two separate domains (1-6). The peripheral V 1 domain has a molecular mass of about 570 kDa and contains eight different subunits of molecular mass 70 (A), 60 (B), 57 (H), 40 (C), 34 (D), 33 (E), 14 (F), and 16 (G) kDa. The integral V 0 domain has a molecular mass of 260 kDa and contains five different subunits of molecular mass 100 (a), 38 (d), 19 (cЉ), and 17 (c, cЈ) kDa. Functional studies indicate that the V 1 domain is responsible for ATP hydrolysis while the V 0 domain carries out proton transport (1-6). We have previously demonstrated that each V-ATPase complex contains three copies each of the A and B subunits, six co...

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“…However, not until the first atomic-level (0.28 • A) resolution structure of bovine mitochondria F 1 was obtained (Abrahams et al, 1994), as well as a great deal of related Fig. 1 Schematic of F 1 -ATPase motor, whose propeller is nickel nanowire fabricated by electrochemical deposition studies (Duncan et al, 1995;Ogilvie et al, 1997;Engelbrecht and Junge, 1997;Groth and Walker, 1997), the understanding of the mechanism of F 1 motor was turned from the 'cartoon' stage to detailed calculations (Noji et al, 1997;Oster and Wang, 2003). Now, the prevailing and accepted mechanism for isolated F 1 -ATPase is that the central γ subunit rotates against the surrounding α 3 β 3 subunits during the hydrolysis of ATP in the three catalytic β subunits of the F 1 -ATPase.…”

Section: Introductionmentioning

confidence: 99%

Biological application of multi-component nanowires in hybrid devices powered by F1-ATPase motors

Ren

Zhao

Yue

et al. 2006

Biomed Microdevices

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In this paper, construction of hybrid device by integrating nanowires with F 1 -ATPase motors is described. The nickel nanowires and multi-segment nanowires, including gold and nickel, were fabricated by electrochemical deposition in nanoporous templates. The nickel nanowires functionalized by biotinylated peptide can be assembled directly onto F 1 -ATPase motors to act as the propellers. If the multicomponent nanowires, including gold and nickel, were selectively functionalized by the thiol group modified ssDNA and the synthetic peptide, respectively, the biotinylated F 1 -ATPase motors can be attached to the biotinylated peptide on nickel segment of the nanowires. Then, the multi-component nanowires can also be used as the propellers, and one may observe the rotations of the multi-component nanowires driven by F 1 -ATPase motors. Therefore, introduction of multiple segments along the length of a nanowire can lead to a variety of multiple chemical functionalities, which can be selectively bound to cells and special biomolecules. This method provides an insight for the construction of other hybrid devices with its controlling arrangement of different biomolecule on designed nanometer scale structures.

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Cross-linking of the δ Subunit to One of the Three α Subunits Has No Effect on Functioning, as Expected if δ Is a Part of the Stator That Links the F1 and F0 Parts of the Escherichia coli ATP Synthase

Cited by 141 publications

References 45 publications

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Subunit Interactions in the Clathrin-coated Vesicle Vacuolar (H+)-ATPase Complex

Biological application of multi-component nanowires in hybrid devices powered by F1-ATPase motors

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