title: Hybrid rotors in F1F(o) ATP synthases: subunit composition, distribution, and physiological significance.
abstract: The c ring of the Na+ F1F(o) ATP synthase from the anaerobic acetogenic bacterium Acetobacterium woodii is encoded by three different genes: atpE1, atpE2 and atpE3. Subunit c1 is similar to typical V-type c subunits and has four transmembrane helices with one ion binding site. Subunit c2 and c3 are identical at the amino acid level and are typical F-type c subunits with one ion binding site in two transmembrane helices. All three constitute a hybrid F(o)V(o) c ring, the first found in nature. To analyze whether other species may have similar hybrid rotors, we searched every genome sequence publicly available as of 23 February 2015 for F1F(o) ATPase operons that have more than one gene encoding the c subunit. This revealed no other species that has three different c subunit encoding genes but twelve species that encode one F(o)- and one V(o)-type c subunit in one operon. Their c subunits have the conserved binding motif for Na+. The organisms are all anaerobic. The advantage of hybrid c rings for the organisms in their environments is discussed.
authors.forename: Karsten
authors.initials: K
authors.lastname: Brandt
authors.forename: Volker
authors.initials: V
authors.lastname: Müller
mesh_terms: D045855:Acetobacterium / Q000201:enzymology*; D000595:Amino Acid Sequence; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D012964:Sodium / Q000737:chemistry / Q000378:metabolism
chemical_list: D021122:Protein Subunits; D012964:Sodium; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases