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A new benthic freshwater diatom, Fragilaria rinoi Almeida & C.Delgado sp. nov., is described from river periphyton samples in Portugal. Fragilaria rinoi sp. nov. is illustrated and discussed based on populations collected from the Vouga, Mondego and Lis river basins in central Portugal and compared with the type material of Fragilaria vaucheriae (Kütz.) J.B.Petersen. The morphological features of the new diatom species are documented through light and scanning electron micrographs, including a comparative analysis with related species of the genus (F. candidagilae Almeida, C.Delgado, Novais & S.Blanco, F. intermedia Grunow in Van Heurck, F. neointermedia Tuji & D.M.Williams, F. recapitellata Lange-Bert. & Metzeltin, F. perminuta (Grunow) Lange-Bert., F. vaucheriae and F. microvaucheriae C.E.Wetzel & Ector). Fragilaria rinoi sp. nov. is characterized by solitary cells without spines, lanceolate valves with slightly rostrate apices, a narrow, linear axial area, and a large, unilateral central area. Fragilaria rinoi sp. nov. may be confused with F. microvaucheriae in terms of length, striae density and outline, although a morphometric analysis revealed that F. rinoi sp. nov. is significantly wider. Fragilaria rinoi sp. nov. is present in rivers with high dissolved oxygen concentrations, medium to high conductivity, neutral to slightly alkaline pH and high mean values of nitrates and ammonium.
Fucoxanthin chlorophyll proteins (Fcps), the light-harvesting antennas of heterokont algae, are encoded by a multigene family and are highly similar with respect to their molecular masses as well as to their pigmentation, making it difficult to purify single Fcps. In this study, a hexa-histidine tag was genetically added to the C-terminus of the FcpA protein of the pennate diatom Phaeodactylum tricornutum. A transgenic strain expressing the recombinant His-tagged FcpA protein in addition to the endogenous wild type Fcps was created. This strategy allowed, for the first time, the purification of a specific, stable trimeric Fcp complex. In addition, a pool of various trimeric Fcps was also purified from the wild-type cells using sucrose density gradient ultracentrifugation and gel filtration. In both the His-tagged and the wild-type Fcps, excitation energy coupling between fucoxanthin and chlorophyll a was intact and the existence of a chlorophyll a/fucoxanthin excitonic dimer was demonstrated using circular dichroism spectroscopy. Mass spectrometric analyses of the trimeric His-tagged complex indicated that it is composed of FcpA and FcpE polypeptides. It is confirmed here that a trimer is the basic organizational unit of Fcps in P. tricornutum. From circular dichroism spectra, it is proposed that the organization of the pigments on the polypeptide backbone of Fcps is a conserved feature in the case of chlorophyll a/c containing algae.