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Registros recuperados: 7
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Alpha-agarases define a new family of glycoside hydrolases, distinct from beta-agarase families ArchiMer
Flament, Didier; Barbeyron, Tristan; Jam, Murielle; Potin, Philippe; Czjzek, Mirjam; Kloareg, Bernard; Michel, Gurvan.
The gene encoding the alpha-agarase from "Alteromonas agarilytica" (proposed name) has been cloned and sequenced. The gene product (154 kDa) is unrelated to Beta-agarases and instead belongs to a new family of glycoside hydrolases (GH96). The -agarase also displays a complex modularity, with the presence of five thrombospondin type 3 repeats and three carbohydrate-binding modules.
Tipo: Text
Ano: 2007 URL: http://archimer.ifremer.fr/doc/2007/publication-2826.pdf
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Alterocin, an antibiofilm protein secreted by Pseudoalteromonas sp. 3J6 ArchiMer
Jouault, Albane; Gobet, Angelique; Simon, Marjolaine; Portier, Emilie; Perennou, Morgan; Corre, Erwan; Gaillard, Fanny; Vallenet, David; Michel, Gurvan; Fleury, Yannick; Bazire, Alexis; Dufour, Alain.
The aim was to identify and study the antibiofilm protein secreted by the marine bacterium Pseudoalteromonas sp. 3J6. The latter is active against marine and terrestrial bacteria, including Pseudomonas aeruginosa clinical strains forming different biofilm types. Several amino acid sequences were obtained from the partially purified antibiofilm protein, named alterocin. The Pseudoalteromonas sp. 3J6 genome was sequenced and a candidate alt gene was identified by comparing the genome-encoded proteins to the sequences from purified alterocin. Expressing the alt gene in another non-active Pseudoalteromonas sp. strain, 3J3, demonstrated that it is responsible for the antibiofilm activity. Alterocin is a 139-residue protein including a predicted 20-residue...
Tipo: Text Palavras-chave: Antibiofilm protein; Pseudoalteromonas; Pseudomonas aeruginosa; Biofilm.
Ano: 2020 URL: https://archimer.ifremer.fr/doc/00643/75517/76405.pdf
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Evolutionary Evidence of Algal Polysaccharide Degradation Acquisition by Pseudoalteromonas carrageenovora 9(T) to Adapt to Macroalgal Niches ArchiMer
Gobet, Angelique; Barbeyron, Tristan; Matard-mann, Maria; Magdelenat, Ghislaine; Vallenet, David; Duchaud, Eric; Michel, Gurvan.
About half of seaweed biomass is composed of polysaccharides. Most of these complex polymers have a marked polyanionic character. For instance, the red algal cell wall is mainly composed of sulfated galactans, agars and carrageenans, while brown algae contain alginate and fucose-containing sulfated polysaccharides (FCSP) as cell wall polysaccharides. Some marine heterotrophic bacteria have developed abilities to grow on such macroalgal polysaccharides. This is the case of Pseudoalteromonas carrageenovora 9(T) (ATCC 43555(T)), a marine gammaproteobacterium isolated in 1955 and which was an early model organism for studying carrageenan catabolism. We present here the genomic analysis of P. carrageenovora. Its genome is composed of two chromosomes and of a...
Tipo: Text Palavras-chave: Carrageenan; CAZymes; Alginate; Gammaproteobacteria; Pseudoalteromonas; Marine bacteria; Algal holobiont; Biofilm.
Ano: 2018 URL: https://archimer.ifremer.fr/doc/00489/60070/63377.pdf
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Genome and metabolic network of "Candidatus Phaeomarinobacter ectocarpi" Ec32, a new candidate genus of Alphaproteobacteria frequently associated with brown algae ArchiMer
Dittami, Simon M.; Barbeyron, Tristan; Boyen, Catherine; Cambefort, Jeanne; Collet, Guillaume; Delage, Ludovic; Gobet, Angelique; Groisillier, Agnes; Leblanc, Catherine; Michel, Gurvan; Scornet, Delphine; Siegel, Anne; Tapia, Javier E.; Tonon, Thierry.
Rhizobiales and related orders of Alphaproteobacteria comprise several genera of nodule-inducing symbiotic bacteria associated with plant roots. Here we describe the genome and the metabolic network of "Candidatus Phaeomarinobacter ectocarpi" Ec32, a member of a new candidate genus closely related to Rhizobiales and found in association with cultures of the filamentous brown algal model Ectocarpus. The "Ca. P. ectocarpi" genome encodes numerous metabolic pathways that may be relevant for this bacterium to interact with algae. Notably, it possesses a large set of glycoside hydrolases and transporters, which may serve to process and assimilate algal metabolites. It also harbors several proteins likely to be involved in the synthesis of algal hormones such as...
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Ano: 2014 URL: https://archimer.ifremer.fr/doc/00488/59944/63183.pdf
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MARINE-EXPRESS: taking advantage of high throughput cloning and expression strategies for the post-genomic analysis of marine organisms ArchiMer
Groisillier, Agnes; Herve, Christiane; Jeudy, Alexandra; Rebuffet, Etienne; Pluchon, Pierre Francois; Chevolot, Yann; Flament, Didier; Geslin, Claire; Morgado, Isabel M.; Power, Deborah; Branno, Margherita; Moreau, Herve; Michel, Gurvan; Boyen, Catherine; Czjzek, Mirjam.
Background: The production of stable and soluble proteins is one of the most important steps prior to structural and functional studies of biological importance. We investigated the parallel production in a medium throughput strategy of genes coding for proteins from various marine organisms, using protocols that involved recombinatorial cloning, protein expression screening and batch purification. This strategy was applied in order to respond to the need for post-genomic validation of the recent success of a large number of marine genomic projects. Indeed, the upcoming challenge is to go beyond the bioinformatic data, since the bias introduced through the genomes of the so called model organisms leads to numerous proteins of unknown function in the still...
Tipo: Text
Ano: 2010 URL: http://archimer.ifremer.fr/doc/00011/12219/9003.pdf
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Seasonal and algal diet-driven patterns of the digestive microbiota of the European abalone Haliotis tuberculata, a generalist marine herbivore ArchiMer
Gobet, Angelique; Mest, Laetitia; Perennou, Morgan; Dittami, Simon M.; Caralp, Claire; Coulombet, Celine; Huchette, Sylvain; Roussel, Sabine; Michel, Gurvan; Leblanc, Catherine.
Background: Holobionts have a digestive microbiota with catabolic abilities allowing the degradation of complex dietary compounds for the host. In terrestrial herbivores, the digestive microbiota is known to degrade complex polysaccharides from land plants while in marine herbivores, the digestive microbiota is poorly characterized. Most of the latter are generalists and consume red, green, and brown macroalgae, three distinct lineages characterized by a specific composition in complex polysaccharides, which represent half of their biomass. Subsequently, each macroalga features a specific epiphytic microbiota, and the digestive microbiota of marine herbivores is expected to vary with a monospecific algal diet. We investigated the effect of four...
Tipo: Text Palavras-chave: Microbe-host interactions; Digestive microbiota; Abalone; Macroalgae; Holobiont.
Ano: 2018 URL: https://archimer.ifremer.fr/doc/00489/60071/63368.pdf
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The Complete Genome Sequence of the Fish Pathogen Tenacibaculum maritimum Provides Insights into Virulence Mechanisms ArchiMer
Perez-pascual, David; Lunazzi, Aurelie; Magdelenat, Ghislaine; Rouy, Zoe; Roulet, Alain; Lopez-roques, Celine; Larocque, Robert; Barbeyron, Tristan; Gobet, Angelique; Michel, Gurvan; Bernardet, Jean-francois; Duchaud, Eric.
Tenacibaculum maritimum is a devastating bacterial pathogen of wild and farmed marine fish with a broad host range and a worldwide distribution. We report here the complete genome sequence of the T. maritimum type strain NCIMB 2154(T). The genome consists of a 3,435,971-base pair circular chromosome with 2,866 predicted protein-coding genes. Genes encoding the biosynthesis of exopolysaccharides, the type IX secretion system, iron uptake systems, adhesins, hemolysins, proteases, and glycoside hydrolases were identified. They are likely involved in the virulence process including immune escape, invasion, colonization, destruction of host tissues, and nutrient scavenging. Among the predicted virulence factors, type IX secretion-mediated and cell-surface...
Tipo: Text Palavras-chave: Tenacibaculum maritimum; Fish pathogen; Virulence factors; Genome; Toxins.
Ano: 2017 URL: https://archimer.ifremer.fr/doc/00488/59939/63150.pdf
Registros recuperados: 7
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