1999
DOI: 10.1074/jbc.274.36.25281
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The Proteolipid of the A1A0ATP Synthase from Methanococcus jannaschii Has Six Predicted Transmembrane Helices but Only Two Proton-translocating Carboxyl Groups

Abstract: The proteolipid, a hydrophobic ATPase subunit essential for ion translocation, was purified from membranes of Methanococcus jannaschii by chloroform/methanol extraction and gel chromatography and was studied using molecular and biochemical techniques. Its apparent molecular mass as determined in SDS-polyacrylamide gel electrophoresis varied considerably with the conditions applied. The N-terminal sequence analysis made it possible to define the open reading frame and revealed that the gene is a triplication of… Show more

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Cited by 31 publications
(25 citation statements)
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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: 66%
See 1 more Smart Citation
“…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: 66%
“…Therefore, subunit c 1 of A. woodii is similar to the so-called 16-kDa proteolipids of V 1 V 0 -ATPases, which also arose by gene duplication accompanied by loss of the protonbinding residue in hair pin one. The loss of the proton-binding residue was believed to be the reason for the apparent inability of V 1 V 0 -ATPases to function as ATP synthases under in vivo conditions (16). Western blot analyses verified that atpE 1 was expressed and that the product was not posttranslationally split into two 8-kDa proteolipids (11).…”
mentioning
confidence: 87%
“…Although the stoichiometry of c-subunit gene products in the assembled c-ring is not known [21], an H þ /ATP ratio of 10/3 or 8/3 would be achieved if they assemble as five or four repeats of c/c-cx, respectively. Similarly, a triple-c fusion with loss of the N-terminal carboxylate, as found in synthases from the methanogenic archaea Methanococcus maripaludis (GenBank Accession member NC_005791) and M. jannaschii [22], would give a coupling ratio of 10/3 or 8/3 depending on whether five or four of the cx-c-c's assemble to form a ring.…”
Section: Fine Tuning the H þ /Atp Coupling Ratio In Atp Synthasesmentioning
confidence: 99%
“…In recent years, however, the determination of the genome sequences of several archaea have revealed an unexpected feature of A 1 A O ATP synthases: the gene encoding for subunit c underwent duplication (12,13), triplication (14), and even greater multiplication, so far up to 13-fold (15-17). Moreover, in some species the sequence motif characteristic of the ionbinding site is absent in one hairpin, which would result in c subunits with one ion-binding site within four transmembrane helices or two within six transmembrane helices (10,18).…”
mentioning
confidence: 99%