Anthozoa from the northern Mid-Atlantic Ridge and Charlie-Gibbs Fracture Zone

An annotated list of deep-sea Anthozoa of the orders Actiniaria, Antipatharia, Scleractinia, Alcyonacea and Pennatulacea collected on the G.O. Sars MAR-ECO cruise to the Mid-Atlantic Ridge between the Azores and the southern tip of the Reykjanes Ridge is given. A total of 33 species is reported of which 32 were identified to species or genus level. The groups most rich in species were Actiniaria (nine species), Scleractinia (eight species) and Pennatulacea (eight species). Scleractinia, Antipatharia and Pennatulacea were mainly represented by species with a wide or cosmopolitan geographical distribution. In contrast, most of the actiniarians had been rarely recorded in the North Atlantic. Three species, Schizopathes affinis Brook, 1889 (Antipatharia), Dendrobrachia multispina Opresko & Bayer, 1991 and Heteropolypus cf. insolitus Tixier-Durivault, 1964 (Alcyonacea) are reported from the North Atlantic for the first time.     

Highly Divergent Mitochondrial ATP Synthase Complexes in Tetrahymena thermophila

The F-type ATP synthase complex is a rotary nano-motor driven by proton motive force to synthesize ATP. Its F₁ sector catalyzes ATP synthesis, whereas the F_o sector conducts the protons and provides a stator for the rotary action of the complex. Components of both F₁ and F_o sectors are highly conserved across prokaryotes and eukaryotes. Therefore, it was a surprise that genes encoding the a and b subunits as well as other components of the F_o sector were undetectable in the sequenced genomes of a variety of apicomplexan parasites. While the parasitic existence of these organisms could explain the apparent incomplete nature of ATP synthase in Apicomplexa, genes for these essential components were absent even in Tetrahymena thermophila, a free-living ciliate belonging to a sister clade of Apicomplexa, which demonstrates robust oxidative phosphorylation. This observation raises the possibility that the entire clade of Alveolata may have invented novel means to operate ATP synthase complexes. To assess this remarkable possibility, we have carried out an investigation of the ATP synthase from T. thermophila. Blue native polyacrylamide gel electrophoresis (BN-PAGE) revealed the ATP synthase to be present as a large complex. Structural study based on single particle electron microscopy analysis suggested the complex to be a dimer with several unique structures including an unusually large domain on the intermembrane side of the ATP synthase and novel domains flanking the c subunit rings. The two monomers were in a parallel configuration rather than the angled configuration previously observed in other organisms. Proteomic analyses of well-resolved ATP synthase complexes from 2-D BN/BN-PAGE identified orthologs of seven canonical ATP synthase subunits, and at least 13 novel proteins that constitute subunits apparently limited to the ciliate lineage. A mitochondrially encoded protein, Ymf66, with predicted eight transmembrane domains could be a substitute for the subunit a of the F_o sector. The absence of genes encoding orthologs of the novel subunits even in apicomplexans suggests that the Tetrahymena ATP synthase, despite core similarities, is a unique enzyme exhibiting dramatic differences compared to the conventional complexes found in metazoan, fungal, and plant mitochondria, as well as in prokaryotes. These findings have significant implications for the origins and evolution of a central player in bioenergetics.