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Müller, Volker; Ruppert, Claudia; Lemker, Thorsten

doi:10.1023/a:1005451311009

Cited by 50 publications

(24 citation statements)

References 62 publications

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“…Duplicated proteolipids were, for a long time, seen as an exclusive feature of eucaryal V 1 V 0 -ATPases (28). In archaea, duplication and triplication of proteolipid-encoding genes with subsequent fusion of the genes was described very recently (16,29). With the experiments described here we add another argument, now derived from a bacterial species, that multiplied and fused proteolipid-encoding genes are not exclusively present in eucarya, but also in the other domains of life.…”

Section: Discussionmentioning

confidence: 51%

Identification of Subunits a, b, andc 1 from Acetobacterium woodiiNa+-F1F0-ATPase

Aufurth¹,

Müller²

2000

Journal of Biological Chemistry

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The Na ؉ -F 1 F 0 -ATPase operon of Acetobacterium woodii was recently shown to contain, among eleven atp genes, those genes that encode subunit a and b, a gene encoding a 16-kDa proteolipid (subunit c 1 ), and two genes encoding 8-kDa proteolipids (subunits c 2 and c 3 ). Because subunits a, b, and c 1 were not found in previous enzyme preparations, we re-determined the subunit composition of the enzyme. The genes were overproduced, and specific antibodies were raised. Western blots revealed that subunits a, b, and c 1 are produced and localized in the cytoplasmic membrane. Membrane protein complexes were solubilized by dodecylmaltoside and separated by blue native-polyacrylamide gel electrophoresis, and the ATPase subunits were resolved by SDS-polyacrylamide gel electrophoresis. N-terminal sequence analyses revealed the presence of subunits a, c 2 , c 3 , b, ␦, ␣, ␥, ␤, and ⑀. Biochemical and immunological analyses revealed that subunits c 1 , c 2 , and c 3 are all part of the c-oligomer, the first of a F 1 F 0 -ATPase that contains 8-and 16-kDa proteolipids.

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Section: Discussionmentioning

confidence: 51%

Identification of Subunits a, b, andc 1 from Acetobacterium woodiiNa+-F1F0-ATPase

Aufurth¹,

Müller²

2000

Journal of Biological Chemistry

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“…It is important to determine whether the membranebound enzyme uses the same electron transfer pathway. If the physiologically relevant order of electron flow is indeed HPhenH 2 3 [Fe 4 S 4 ] H 3 [heme b] L , the high potential cluster is expected to be located near the subunit interface. This is because the large subunit containing the clusters is cytoplasmic and the heme is in the membrane-associated subunit (16).…”

Section: Discussionmentioning

confidence: 99%

“…What is the intramolecular electron transfer pathway? Based on our results, we propose that the physiological electron transfer pathway from methanophenazine to the heterodisulfide is: MPhenH 2 3 [Fe 4 S 4 ] high 3 heme low 3 CoB-S-S-CoM. * This work was supported by Department of Energy Grant ER20053 (to S. W. R.).…”

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confidence: 96%

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Characterization of the Intramolecular Electron Transfer Pathway from 2-Hydroxyphenazine to the Heterodisulfide Reductase fromMethanosarcina thermophila

Murakami¹,

Deppenmeier²,

Ragsdale³

2001

Journal of Biological Chemistry

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“…The A-type ATP synthases are more closely related to vacuolar (V-type) ATPase, which, however, is functionally different and acts as an ATPdriven ion pump (1). Some bacteria also harbor A-type ATP synthases, probably acquired by horizontal gene transfer (2,3).…”

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confidence: 99%

Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron Microscopy

Vonck

Pisa

Morgner

et al. 2009

Journal of Biological Chemistry

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The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A 1 part and a transmembrane, ion translocation domain A 0 . The A 1 A 0 complex from the hyperthermophile Pyrococcus furiosus was isolated. Mass analysis of the complex by laser-induced liquid bead ion desorption (LILBID) indicated a size of 730 ؎ 10 kDa. A three-dimensional map was generated by electron microscopy from negatively stained images. The map at a resolution of 2.3 nm shows the A 1 and A 0 domain, connected by a central stalk and two peripheral stalks, one of which is connected to A 0 , and both connected to A 1 via prominent knobs. X-ray structures of subunits from related proteins were fitted to the map. On the basis of the fitting and the LILBID analysis, a structural model is presented with the stoichiometry A 3 B 3 CDE 2 FH 2 ac 10 .Archaea produce ATP by an ATP synthase that is distinct from the well known F 1 F 0 -type ATP synthase occurring in bacteria, mitochondria, and chloroplasts. The A-type ATP synthases are more closely related to vacuolar (V-type) ATPase, which, however, is functionally different and acts as an ATPdriven ion pump (1). Some bacteria also harbor A-type ATP synthases, probably acquired by horizontal gene transfer (2, 3).Like F 1 F 0 ATP synthases and V 1 V 0 ATPases, A 1 A 0 ATP synthases consist of a soluble enzymatic head in the cytoplasm and a transmembrane ion-translocating domain, forming a pair of coupled rotary motors. There is clear homology in the main catalytic subunits of all types, showing a common evolutionary origin, but many of the peripheral subunits are unique for the distinct groups. The A-and V-type enzymes are considerably larger than the F-type (1).The catalytic heads are made up of three A and three B subunits, where A is the catalytic subunit equivalent to F-type ␤. The A subunit contains a 90-amino acid insert near the N terminus, known as the non-homologous region, which makes this subunit with Ϸ66 kDa considerably larger than its homologues (4 -7). The central stalk consists of the C, D, and F subunits, and the D subunit is thought to be the equivalent of the ␥ subunit, responsible for conformational changes in the nucleotide-binding pockets upon rotation (8, 9). The transmembrane domain contains a rotor of a number of identical c-subunits and part of the a-subunit. The a-subunit is large, comprising a transmembrane domain with seven to eight predicted transmembrane helices and a soluble domain, which probably forms part of the stator. In addition, the A-type ATP synthases contain subunits H and E (10).Structural information on the A-type and V-type ATPases has been forthcoming in recent years. For several subunits, x-ray structures have been determined, including isolated archaeal A (11) and B (12) subunits, the E subunit (13), and a bacterial A-type C subunit (14, 15). The archaeal F subunit has been solved by NMR spectroscopy (16), and the shape of an H subunit dimer is known from small angle x-ray scattering (17). Information about the whole complex has been pro...

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Cited by 50 publications

References 62 publications

Identification of Subunits a, b, andc 1 from Acetobacterium woodiiNa+-F1F0-ATPase

Identification of Subunits a, b, andc 1 from Acetobacterium woodiiNa+-F1F0-ATPase

Characterization of the Intramolecular Electron Transfer Pathway from 2-Hydroxyphenazine to the Heterodisulfide Reductase fromMethanosarcina thermophila

Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron Microscopy

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