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Phylogenetic characterization of transporter proteins in the cnidarian-dinoflagellate symbiosis.
Sproles, Ashley E; Kirk, Nathan L; Kitchen, Sheila A; Oakley, Clinton A; Grossman, Arthur R; Weis, Virginia M; Davy, Simon K.
Afiliación
  • Sproles AE; School of Biological Sciences, Victoria University of Wellington, Wellington 6012, New Zealand.
  • Kirk NL; Department of Integrative Biology, Oregon State University, Corvallis, OR 97331, USA.
  • Kitchen SA; Department of Integrative Biology, Oregon State University, Corvallis, OR 97331, USA.
  • Oakley CA; School of Biological Sciences, Victoria University of Wellington, Wellington 6012, New Zealand.
  • Grossman AR; Department of Plant Biology, The Carnegie Institution for Science, Stanford, CA 94305, USA.
  • Weis VM; Department of Integrative Biology, Oregon State University, Corvallis, OR 97331, USA.
  • Davy SK; School of Biological Sciences, Victoria University of Wellington, Wellington 6012, New Zealand. Electronic address: simon.davy@vuw.ac.nz.
Mol Phylogenet Evol ; 120: 307-320, 2018 03.
Article en En | MEDLINE | ID: mdl-29233707
ABSTRACT
Metabolic exchange between cnidarians and their symbiotic dinoflagellates is central to maintaining their mutualistic relationship. Sugars are translocated to the host, while ammonium and nitrate are utilized by the dinoflagellates (Symbiodinium spp.). We investigated membrane protein sequences of each partner to identify potential transporter proteins that move sugars into cnidarian cells and nitrogen products into Symbiodinium cells. We examined the facilitated glucose transporters (GLUT), sodium/glucose cotransporters (SGLT), and aquaporin (AQP) channels in the cnidarian host as mechanisms for sugar uptake, and the ammonium and high-affinity nitrate transporters (AMT and NRT2, respectively) in the algal symbiont as mechanisms for nitrogen uptake. Homologous protein sequences were used for phylogenetic analysis and tertiary structure deductions. In cnidarians, we identified putative glucose transporters of the GLUT family and glycerol transporting AQP proteins, as well as sodium monocarboxylate transporters and sodium myo-inositol cotransporters homologous to SGLT proteins. We hypothesize that cnidarians use GLUT proteins as the primary mechanism for glucose uptake, while glycerol moves into cells by passive diffusion. We also identified putative AMT proteins in several Symbiodinium clades and putative NRT2 proteins only in a single clade. We further observed an upregulation of expressed putative AMT proteins in Symbiodinium, which may have emerged as an adaptation to conditions experienced inside the host cell. This study is the first to identify transporter sequences from a diversity of cnidarian species and Symbiodinium clades, which will be useful for future experimental analyses of the host-symbiont proteome and the nutritional exchange of Symbiodinium cells in hospite.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Filogenia / Dinoflagelados / Cnidarios Límite: Animals Idioma: En Año: 2018 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Filogenia / Dinoflagelados / Cnidarios Límite: Animals Idioma: En Año: 2018 Tipo del documento: Article