title: ATP synthases with novel rotor subunits: new insights into structure, function and evolution of ATPases.
abstract: ATPases with unusual membrane-embedded rotor subunits were found in both F(1)F(0) and A(1)A(0) ATP synthases. The rotor subunit c of A(1)A(0) ATPases is, in most cases, similar to subunit c from F(0). Surprisingly, multiplied c subunits with four, six, or even 26 transmembrane spans have been found in some archaea and these multiplication events were sometimes accompanied by loss of the ion-translocating group. Nevertheless, these enzymes are still active as ATP synthases. A duplicated c subunit with only one ion-translocating group was found along with "normal" F(0) c subunits in the Na(+) F(1)F(0) ATP synthase of the bacterium Acetobacterium woodii. These extraordinary features and exceptional structural and functional variability in the rotor of ATP synthases may have arisen as an adaptation to different cellular needs and the extreme physicochemical conditions in the early history of life.
authors.affiliation: Molecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University, Frankfurt, Germany. vmueller@em.uni-frankfurt.de
authors.forename: Volker
authors.initials: V
authors.lastname: Müller
authors.forename: Astrid
authors.initials: A
authors.lastname: Lingl
authors.forename: Kim
authors.initials: K
authors.lastname: Lewalter
authors.forename: Michael
authors.initials: M
authors.lastname: Fritz
mesh_terms: D045855:Acetobacterium / Q000201:enzymology; D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D025243:Bacterial Proton-Translocating ATPases; D019143:Evolution, Molecular; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D020409:Molecular Motor Proteins
chemical_list: D020409:Molecular Motor Proteins; D000251:Adenosine Triphosphatases; D025243:Bacterial Proton-Translocating ATPases; D025261:Mitochondrial Proton-Translocating ATPases