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4. Constrained Catalytic Itinerary of a Retaining 3,6‐Anhydro‐D‐Galactosidase, a Key Enzyme in Red Algal Cell Wall Degradation.

Author

Wallace, Michael D., Cuxart, Irene, Roret, Thomas, Guée, Laura, Debowski, Aleksandra W., Czjzek, Mirjam, Rovira, Carme, Stubbs, Keith A., and Ficko‐Blean, Elizabeth

Subjects
ALGAL cells, POLYSACCHARIDES, ERYTHROCYTES, BIOCHEMICAL substrates, OLIGOSACCHARIDES, CARRAGEENANS
Abstract

The marine Bacteroidota Zobellia galactanivorans has a polysaccharide utilization locus dedicated to the catabolism of the red algal cell wall galactan carrageenan and its unique and industrially important α‐3,6‐anhydro‐D‐galactose (ADG) monosaccharide. Here we present the first analysis of the specific molecular interactions that the exo‐(α‐1,3)‐3,6‐anhydro‐D‐galactosidase ZgGH129 uses to cope with the strict steric restrictions imposed by its bicyclic ADG substrate — which is ring flipped relative to D‐galactose. Crystallographic snapshots of key catalytic states obtained with the natural substrate and novel chemical tools designed to mimic species along the reaction coordinate, together with quantum mechanics/molecular mechanics (QM/MM) metadynamics methods and kinetic studies, demonstrate a retaining mechanism where the second step is rate limiting. The conformational landscape of the constrained 3,6‐anhydro‐D‐galactopyranose ring proceeds through enzyme glycosylation B1,4→[E4]≠→E4/1C4 and deglycosylation E4/1C4→[E4]≠→B1,4 itineraries limited to the Southern Hemisphere of the Cremer–Pople sphere. These results demonstrate the conformational changes throughout catalysis in a non‐standard, sterically restrained, bicyclic monosaccharide, and provide a molecular framework for mechanism‐based inhibitor design for anhydro‐type carbohydrate‐processing enzymes and for future applications involving carrageenan degradation. In addition, our study provides a rare example of distinct niche‐based conformational itineraries within the same carbohydrate‐active enzyme family. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Insights into the red algae and eukaryotic evolution from the genome of Porphyra umbilicalis (Bangiophyceae, Rhodophyta)

Author

Brawley, Susan H, Blouin, Nicolas A, Ficko-Blean, Elizabeth, Wheeler, Glen L, Lohr, Martin, Goodson, Holly V, Jenkins, Jerry W, Blaby-Haas, Crysten E, Helliwell, Katherine E, Chan, Cheong Xin, Marriage, Tara N, Bhattacharya, Debashish, Klein, Anita S, Badis, Yacine, Brodie, Juliet, Cao, Yuanyu, Collén, Jonas, Dittami, Simon M, Gachon, Claire MM, Green, Beverley R, Karpowicz, Steven J, Kim, Jay W, Kudahl, Ulrich Johan, Lin, Senjie, Michel, Gurvan, Mittag, Maria, Olson, Bradley JSC, Pangilinan, Jasmyn L, Peng, Yi, Qiu, Huan, Shu, Shengqiang, Singer, John T, Smith, Alison G, Sprecher, Brittany N, Wagner, Volker, Wang, Wenfei, Wang, Zhi-Yong, Yan, Juying, Yarish, Charles, Zäuner-Riek, Simone, Zhuang, Yunyun, Zou, Yong, Lindquist, Erika A, Grimwood, Jane, Barry, Kerrie W, Rokhsar, Daniel S, Schmutz, Jeremy, Stiller, John W, Grossman, Arthur R, and Prochnik, Simon E

Subjects
Plant Biology, Biological Sciences, Genetics, 1.1 Normal biological development and functioning, Generic health relevance, Actins, Calcium Signaling, Cell Cycle, Cell Wall, Chromatin, Cytoskeleton, Evolution, Molecular, Genome, Plant, Kinesins, Phylogeny, Porphyra, cytoskeleton, calcium-signaling, carbohydrate-active enzymes, stress tolerance, vitamin B-12, vitamin B12, Kinesin
Abstract

Porphyra umbilicalis (laver) belongs to an ancient group of red algae (Bangiophyceae), is harvested for human food, and thrives in the harsh conditions of the upper intertidal zone. Here we present the 87.7-Mbp haploid Porphyra genome (65.8% G + C content, 13,125 gene loci) and elucidate traits that inform our understanding of the biology of red algae as one of the few multicellular eukaryotic lineages. Novel features of the Porphyra genome shared by other red algae relate to the cytoskeleton, calcium signaling, the cell cycle, and stress-tolerance mechanisms including photoprotection. Cytoskeletal motor proteins in Porphyra are restricted to a small set of kinesins that appear to be the only universal cytoskeletal motors within the red algae. Dynein motors are absent, and most red algae, including Porphyra, lack myosin. This surprisingly minimal cytoskeleton offers a potential explanation for why red algal cells and multicellular structures are more limited in size than in most multicellular lineages. Additional discoveries further relating to the stress tolerance of bangiophytes include ancestral enzymes for sulfation of the hydrophilic galactan-rich cell wall, evidence for mannan synthesis that originated before the divergence of green and red algae, and a high capacity for nutrient uptake. Our analyses provide a comprehensive understanding of the red algae, which are both commercially important and have played a major role in the evolution of other algal groups through secondary endosymbioses.

Published
2017

6. Unveiling the role of novel carbohydrate‐binding modules in laminarin interaction of multimodular proteins from marine Bacteroidota during phytoplankton blooms.

Author

Zühlke, Marie‐Katherin, Ficko‐Blean, Elizabeth, Bartosik, Daniel, Terrapon, Nicolas, Jeudy, Alexandra, Jam, Murielle, Wang, Fengqing, Welsch, Norma, Dürwald, Alexandra, Martin, Laura Torres, Larocque, Robert, Jouanneau, Diane, Eisenack, Tom, Thomas, François, Trautwein‐Schult, Anke, Teeling, Hanno, Becher, Dörte, Schweder, Thomas, and Czjzek, Mirjam

Subjects
*ALGAL blooms, *PROTEIN-protein interactions, *MARINE bacteria, *PHAEODACTYLUM tricornutum, *BACTERIAL cell surfaces, *BACTERIAL genomes, *PHYTOPLANKTON
Abstract

Laminarin, a β(1,3)‐glucan, serves as a storage polysaccharide in marine microalgae such as diatoms. Its abundance, water solubility and simple structure make it an appealing substrate for marine bacteria. Consequently, many marine bacteria have evolved strategies to scavenge and decompose laminarin, employing carbohydrate‐binding modules (CBMs) as crucial components. In this study, we characterized two previously unassigned domains as laminarin‐binding CBMs in multimodular proteins from the marine bacterium Christiangramia forsetii KT0803T, thereby introducing the new laminarin‐binding CBM families CBM102 and CBM103. We identified four CBM102s in a surface glycan‐binding protein (SGBP) and a single CBM103 linked to a glycoside hydrolase module from family 16 (GH16_3). Our analysis revealed that both modular proteins have an elongated shape, with GH16_3 exhibiting greater flexibility than SGBP. This flexibility may aid in the recognition and/or degradation of laminarin, while the constraints in SGBP could facilitate the docking of laminarin onto the bacterial surface. Exploration of bacterial metagenome‐assembled genomes (MAGs) from phytoplankton blooms in the North Sea showed that both laminarin‐binding CBM families are widespread among marine Bacteroidota. The high protein abundance of CBM102‐ and CBM103‐containing proteins during phytoplankton blooms further emphasizes their significance in marine laminarin utilization. [ABSTRACT FROM AUTHOR]

Published
2024
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8. The Rhodoexplorer Platform for Red Algal Genomics and Whole-Genome Assemblies for Several Gracilaria Species

Author

Lipinska, Agnieszka P, primary, Krueger-Hadfield, Stacy A, additional, Godfroy, Olivier, additional, Dittami, Simon M, additional, Ayres-Ostrock, Lígia, additional, Bonthond, Guido, additional, Brillet-Guéguen, Loraine, additional, Coelho, Susana, additional, Corre, Erwan, additional, Cossard, Guillaume, additional, Destombe, Christophe, additional, Epperlein, Paul, additional, Faugeron, Sylvain, additional, Ficko-Blean, Elizabeth, additional, Beltrán, Jessica, additional, Lavaut, Emma, additional, Le Bars, Arthur, additional, Marchi, Fabiana, additional, Mauger, Stéphane, additional, Michel, Gurvan, additional, Potin, Philippe, additional, Scornet, Delphine, additional, Sotka, Erik E, additional, Weinberger, Florian, additional, Cabral de Oliveira, Mariana, additional, Guillemin, Marie-Laure, additional, Plastino, Estela M, additional, and Valero, Myriam, additional

Published
2023
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11. The Rhodoexplorer Platform for Red Algal Genomics and Whole Genome Assemblies for Several Gracilaria Species

Author

Lipinska, Agnieszka P., Krueger-Hadfield, Stacy A., Godfroy, Olivier, Dittami, Simon, Ayres-Ostrock, Lígia, Bonthond, Guido, Brillet-Guéguen, Loraine, Coelho, Susana, Corre, Erwan, Cossard, Guillaume, Destombe, Christophe, Epperlein, Paul, Faugeron, Sylvain, Ficko-Blean, Elizabeth, Beltrán, Jessica, Lavaut, Emma, Le Bars, Arthur, Marchi, Fabiana, Mauger, Stéphane, Michel, Gurvan, Potin, Philippe, Scornet, Delphine, Sotka, Erik E., Weinberger, Florian, de Oliveira, Mariana Cabral, Guillemin, Marie-Laure, Plastino, Estela M, Valero, Myriam, Castric, Vincent, Lipinska, Agnieszka P., Krueger-Hadfield, Stacy A., Godfroy, Olivier, Dittami, Simon, Ayres-Ostrock, Lígia, Bonthond, Guido, Brillet-Guéguen, Loraine, Coelho, Susana, Corre, Erwan, Cossard, Guillaume, Destombe, Christophe, Epperlein, Paul, Faugeron, Sylvain, Ficko-Blean, Elizabeth, Beltrán, Jessica, Lavaut, Emma, Le Bars, Arthur, Marchi, Fabiana, Mauger, Stéphane, Michel, Gurvan, Potin, Philippe, Scornet, Delphine, Sotka, Erik E., Weinberger, Florian, de Oliveira, Mariana Cabral, Guillemin, Marie-Laure, Plastino, Estela M, Valero, Myriam, and Castric, Vincent

Abstract

Macroalgal (seaweed) genomic resources are generally lacking as compared to other eukaryotic taxa, and this is particularly true in the red algae (Rhodophyta). Understanding red algal genomes is critical to understanding eukaryotic evolution given that red algal genes are spread across eukaryotic lineages from secondary endosymbiosis and red algae diverged early in the Archaeplastids. The Gracilariales is a highly diverse and widely distributed order including species that can serve as ecosystem engineers in intertidal habitats and several notorious introduced species. The genus Gracilaria is cultivated worldwide, in part for its production of agar and other bioactive compounds with downstream pharmaceutical and industrial applications. This genus is also emerging as a model for algal evolutionary ecology. Here, we report new whole genome assemblies for two species (G. chilensis and G. gracilis), a draft genome assembly of G. caudata, and genome annotation of the previously published G. vermiculophylla genome. To facilitate accessibility and comparative analysis, we integrated these data in a newly created web-based portal dedicated to red algal genomics (https://rhodoexplorer.sb-roscoff.fr). These genomes will provide a resource for understanding algal biology and, more broadly, eukaryotic evolution.

Published
2023
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12. Specificity of a β-porphyranase produced by the carrageenophyte red alga Chondrus crispus and implications of this unexpected activity on red algal biology

Author

Manat, Guillaume, primary, Fanuel, Mathieu, additional, Jouanneau, Diane, additional, Jam, Murielle, additional, Mac-Bear, Jessica, additional, Rogniaux, Hélène, additional, Mora, Théo, additional, Larocque, Robert, additional, Lipinska, Agnieszka, additional, Czjzek, Mirjam, additional, Ropartz, David, additional, and Ficko-Blean, Elizabeth, additional

Published
2022
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14. Systematic comparison of eight methods for preparation of high purity sulfated fucans extracted from the brown alga Pelvetia canaliculata

Author

Nikolić Chenais, Jasna, primary, Marion, Léry, additional, Larocque, Robert, additional, Jam, Murielle, additional, Jouanneau, Diane, additional, Cladiere, Lionel, additional, Le Gall, Sophie, additional, Fanuel, Mathieu, additional, Desban, Nathalie, additional, Rogniaux, Hélène, additional, Ropartz, David, additional, Ficko-Blean, Elizabeth, additional, and Michel, Gurvan, additional

Published
2022
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18. Chondrus crispus – A Present and Historical Model Organism for Red Seaweeds

Author

Collén, Jonas, primary, Cornish, M. Lynn, additional, Craigie, James, additional, Ficko-Blean, Elizabeth, additional, Hervé, Cécile, additional, Krueger-Hadfield, Stacy A., additional, Leblanc, Catherine, additional, Michel, Gurvan, additional, Potin, Philippe, additional, Tonon, Thierry, additional, and Boyen, Catherine, additional

Published
2014
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22. Characterisation of an exo-(α-1,3)-3,6-anhydro-d-galactosidase produced by the marine bacterium Zobellia galactanivorans DsijT: Insight into enzyme preference for natural carrageenan oligosaccharides and kinetic characterisation on a novel chromogenic substrate

Author

Wallace, Michael D., primary, Guée, Laura, additional, Ropartz, David, additional, Fanuel, Mathieu, additional, Lannuzel, Guillaume, additional, Correc, Gaëlle, additional, Stubbs, Keith A., additional, and Ficko-Blean, Elizabeth, additional

Published
2020
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23. In-depth structural characterization of oligosaccharides released by GH107 endofucanase MfFcnA reveals enzyme subsite specificity and sulfated fucan substructural features.

Author

Ropartz, David, Marion, Lery, Fanuel, Mathieu, Nikolic, Jasna, Jam, Murielle, Larocque, Robert, Ficko-Blean, Elizabeth, Michel, Gurvan, and Rogniaux, Helene

Subjects
LIQUID chromatography-mass spectrometry, OLIGOSACCHARIDES, ENZYME specificity, MONOSACCHARIDES, BROWN algae, CHARGE transfer
Abstract

The extracellular matrix of brown algae represents an abundant source of fucose-containing sulfated polysaccharides (FCSPs). FCSPs include sulfated fucans, essentially composed of fucose, and highly heterogeneous fucoidans, comprising various monosaccharides. Despite a range of potentially valuable biological activities, the structures of FCSPs are only partially characterized and enzymatic tools leading to their deconstruction are rare. Previously, the enzyme Mf FcnA was isolated from the marine bacterium Mariniflexile fucanivorans and biochemically characterized as an endo-α-1 → 4- l -fucanase, the first member of glycoside hydrolase family 107. Here, Mf FcnA was used as an enzymatic tool to deconstruct the structure of the sulfated fucans from Pelvetia canaliculata (Fucales brown alga). Oligofucans released by Mf FcnA at different time points were characterized using mass spectrometry coupled with liquid chromatography and tandem mass spectrometry through Charge Transfer Dissociation. This approach highlights a large diversity in the structures released. In particular, the analyses show the presence of species with less than three sulfates per two fucose residues. They also reveal species with monosaccharides other than fucose and the occurrence of laterally branched residues. Precisely, the lateral branching is either in the form of a hexose accompanied by a trisulfated fucose nearby, or of a side chain of fucoses with a pentose as the branching point on the polymer. Overall, the results indicate that the structure of sulfated fucans from P. canaliculata is more complex than expected. They also reveal the interesting capacity of Mf FcnA to accommodate different substrates, leading to structurally diverse oligofucan products that potentially could be screened for bioactivities. [ABSTRACT FROM AUTHOR]

Published
2022
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27. Carrageenan catabolism is encoded by a complex regulon in marine heterotrophic bacteria

Author

Ficko-Blean, Elizabeth, Prechoux, Aurelie, Thomas, François, Rochat, Tatiana, Larocque, Robert, Zhu, Yongtao, Stam, Mark, Génicot, Sabine, Jam, Murielle, Calteau, Alexandra, Viart, Benjamin, Ropartz, David, Pérez-Pascual, David, Correc, Gaëlle, Matard-Mann, Maria, Stubbs, Keith, Rogniaux, Hélène, Jeudy, Alexandra, Barbeyron, Tristan, Médigue, Claudine, Czjzek, Mirjam, Vallenet, David, Mcbride, Mark, Duchaud, Éric, Michel, Gurvan, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche Virologie et Immunologie Moléculaires (VIM), Institut National de la Recherche Agronomique (INRA), University of Wisconsin - Milwaukee, Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), School of Molecular and Microbial Sciences, University of Queensland [Brisbane], Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Fédération de recherche de Roscoff (FR2424), Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), INRA MIGALE bioinformatics platform, Agence National de la Recherche (ANR) [ANR-14-CE19-0020-01], ANR [ANR-10-BTBR-04], National Science Foundation [MCB-1516990], Australian Research Council [FT100100291], Centre for Microscopy, Characterisation and Analysis at The University of Western Australia, and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)

Subjects
Models, Molecular, Bacteroidetes, Protein Conformation, Sequence Analysis, RNA, Science, Carrageenan, Crystallography, X-Ray, Regulon, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Article, Galactosidases, Evolution, Molecular, carbohydrates (lipids), RNA, Bacterial, Bacterial Proteins, Species Specificity, Genes, Bacterial, Multigene Family, lcsh:Q, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, lcsh:Science, Flavobacteriaceae, Metabolic Networks and Pathways, Phylogeny
Abstract

Macroalgae contribute substantially to primary production in coastal ecosystems. Their biomass, mainly consisting of polysaccharides, is cycled into the environment by marine heterotrophic bacteria using largely uncharacterized mechanisms. Here we describe the complete catabolic pathway for carrageenans, major cell wall polysaccharides of red macroalgae, in the marine heterotrophic bacterium Zobellia galactanivorans. Carrageenan catabolism relies on a multifaceted carrageenan-induced regulon, including a non-canonical polysaccharide utilization locus (PUL) and genes distal to the PUL, including a susCD-like pair. The carrageenan utilization system is well conserved in marine Bacteroidetes but modified in other phyla of marine heterotrophic bacteria. The core system is completed by additional functions that might be assumed by non-orthologous genes in different species. This complex genetic structure may be the result of multiple evolutionary events including gene duplications and horizontal gene transfers. These results allow for an extension on the definition of bacterial PUL-mediated polysaccharide digestion., Carrageenans, major cell wall polysaccharides of red macroalgae, are metabolised by marine heterotrophic bacteria through unclear mechanisms. Here, the authors identify an unusual polysaccharide-utilization locus encoding carrageenan catabolism in a marine bacterium, and characterise the complete pathway.

Published
2017

28. Analysis of the structural and functional diversity of plant cell wall specific family 6 carbohydrate binding modules

Author

Abbott, D. Wade, Ficko-Blean, Elizabeth, Bueren, Alicia Lammerts van, Rogowski, Artur, Cartmell, Alan, Coutinho, Pedro M., Henrissat, Bernard, Gilbert, Harry J., and Boraston, Alisdair B.

Subjects
Ligand binding (Biochemistry) -- Analysis, Carbohydrates -- Chemical properties, Cladistic analysis -- Usage, Clostridium -- Physiological aspects, Clostridium -- Genetic aspects, Biological sciences, Chemistry
Abstract

A predictive model for family 6 carbohydrate binding modules (CBMs) (CBM6) that is based upon several factors, including phylogenetic relatedness, and structural and functional evidence is presented. The mechanism, by which the CBM recognizes xylose but not glucose, a specificity not known earlier in family 6 CBM supported the predictive model that holds that variation in region E plays a key role in the diverse ligand selection evident in CBM6.

Published
2009

29. Carbohydrate recognition by a large sialidase toxin from clostridium perfringens

Author

Boraston, Alisdair B., Ficko-Blean, Elizabeth, and Healey, Michael

Subjects
Carbohydrates -- Structure, Clostridium -- Physiological aspects, Gel permeation chromatography -- Analysis, Protein binding -- Analysis, Biological sciences, Chemistry
Abstract

The carbohydrate binding activity of the family of 32 and 40 carbohydrate binding module (CBM) isolated from sialidase secreted Clostridium perfringens is reported. The results suggest that NanJ, the largest sialidases contains carbohydrate specific binding modules that target the enzyme bearing mixed populations of glycans that terminate in either galactose/N-acetylgalactosamine or sialic acid.

Published
2007

30. Chondrus crispus – A Present and Historical Model Organism for Red Seaweeds

Author

Porcel, B., Carre, W., Ball, S., Chaparro, C., Barbeyron, T., Noel, B., Valentin, K., Elias, M., Artiguenave, François, Arun, A., Aury, J.-M., Barbosa-Neto, J., Bothwell, J., Bouget, F.-Y., Brillet, L., Cabello-Hurtado, F., Capella-Gutierrez, S., Charrier, B., Cladière, L., Cock, J., Coelho, S., Colleoni, C., Czjzek, M., Da Silva, C., Delage, L., Denoeud, France, Deschamps, P., Dittami, S., Gabaldón, T., Gachon, C., Groisillier, A., Jabbari, K., Katinka, M., Kloareg, B., Kowalczyk, N., Labadie, K., Lopez, P., Mclachlan, D., Meslet-Cladiere, L., Moustafa, A., Nehr, Z., Nyvall Collen, P., Panaud, O., Partensky, F., Poulain, J., Rensing, S., Rousvoal, S., Samson, G., Symeonidi, A., Weissenbach, J., Zambounis, A., Wincker, P., Collen, Jonas, Cornish, M. Lynn, Craigie, James, Ficko-Blean, Elizabeth, Hervé, Cécile, Krueger-Hadfield, Stacy, Leblanc, Catherine, Michel, Gurvan, Potin, Philippe, Tonon, Thierry, Boyen, Catherine, Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire Génome et développement des plantes (LGDP), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), inconnu, Inconnu, Centre d'étude spatiale des rayonnements (CESR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Observatoire Midi-Pyrénées (OMP), Institut de Recherche pour le Développement (IRD)-Centre National de la Recherche Scientifique (CNRS)-Université Fédérale Toulouse Midi-Pyrénées-Centre National d'Études Spatiales [Toulouse] (CNES)-Météo France-Institut de Recherche pour le Développement (IRD)-Centre National de la Recherche Scientifique (CNRS)-Centre National d'Études Spatiales [Toulouse] (CNES)-Météo France, Structure et évolution des génomes (SEG), CNS-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Ecosystèmes, biodiversité, évolution [Rennes] (ECOBIO), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut Ecologie et Environnement (INEE), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Observatoire des Sciences de l'Univers de Rennes (OSUR)-Centre National de la Recherche Scientifique (CNRS), Sylvadour, IUT des Pays de l'Adour, Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire des plantes (IBMP), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Centre européen de recherche et d'enseignement des géosciences de l'environnement (CEREGE), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Collège de France (CdF (institution))-Institut national des sciences de l'Univers (INSU - CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Institut de Génomique Fonctionnelle de Lyon (IGFL), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut de Génomique d'Evry (IG), Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Centre d'études d'océanographie et de biologie marine (CEOBM), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Unité de Recherche Clinique, Hospices Civils de Lyon (HCL), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Bordeaux 2 Laboratoire de Psychologie EA «Santé et qualité de vie», Université Bordeaux Segalen - Bordeaux 2, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut national des sciences de l'Univers (INSU - CNRS)-Observatoire Midi-Pyrénées (OMP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Collège de France (CdF)-Institut national des sciences de l'Univers (INSU - CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), and École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
biology, Ecology, Ecology (disciplines), [SDV]Life Sciences [q-bio], Population structure, Genomics, biology.organism_classification, Moss, Rocky shore, Algae, Chondrus crispus, Botany, 14. Life underwater, Organism, ComputingMilieux_MISCELLANEOUS
Abstract

Chondrus crispus, or Irish moss, is a common edible red seaweed that can be found on rocky shores in the Northern Atlantic. The cell wall contains carrageenan and C. crispus is the original source of this commercially used thickener. Because of the ecological and economic importance of this red alga a relatively important research literature exists and one of the recent achievements in C. crispus research is the sequencing of its genome. In this chapter we review some of the literature with the aim to promote C. crispus as a model organism for florideophyte red seaweeds. We consider subjects like commercial and historical uses, ecology, genetics, population structure, mating systems, physiology, cell wall biology and genomics. © 2014 Elsevier Ltd.

Published
2014

34. Tampering with Cell Division by Using Small-Molecule Inhibitors of CDK-CKS Protein Interactions

Author

Hamdi, Amel, primary, Lesnard, Aurélien, additional, Suzanne, Peggy, additional, Robert, Thomas, additional, Miteva, Maria A., additional, Pellerano, Morgan, additional, Didier, Bruno, additional, Ficko‐Blean, Elizabeth, additional, Lobstein, Annelise, additional, Hibert, Marcel, additional, Rault, Sylvain, additional, Morris, May C., additional, and Colas, Pierre, additional

Published
2015
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42. The Conformation and Function of a Multimodular Glycogen-Degrading Pneumococcal Virulence Factor

Author

Lammerts van Bueren, Alicia, primary, Ficko-Blean, Elizabeth, additional, Pluvinage, Benjamin, additional, Hehemann, Jan-Hendrik, additional, Higgins, Melanie A., additional, Deng, Lehua, additional, Ogunniyi, A. David, additional, Stroeher, Uwe H., additional, El Warry, Nahida, additional, Burke, Robert D., additional, Czjzek, Mirjam, additional, Paton, James C., additional, Vocadlo, David J., additional, and Boraston, Alisdair B., additional

Published
2011
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46. Biochemical and structural investigation of two paralogous glycoside hydrolases from Zobellia galactanivorans: novel insights into the evolution, dimerization plasticity and catalytic mechanism of the GH117 family.

Author

Ficko-Blean, Elizabeth, Duffieux, Delphine, Rebuffet, Étienne, Larocque, Robert, Groisillier, Agnes, Michel, Gurvan, and Czjzek, Mirjam

Subjects
*GLYCOSIDASES, *DIMERIZATION, *MATERIAL plasticity, *PHYLOGENY, *CHEMICAL reduction
Abstract

The family 117 glycoside hydrolase (GH117) enzymes have exo-α-1,3-(3,6-anhydro)-L-galactosidase activity, removing terminal nonreducing α-1,3-linked 3,6-anhydro-L-galactose residues from their red algal neoagarose substrate. These enzymes have previously been phylogenetically divided into clades, and only the clade A enzymes have been experimentally studied to date. The investigation of two GH117 enzymes, Zg3615 and Zg3597, produced by the marine bacterium Zobellia galactanivorans reveals structural, biochemical and further phylogenetic diversity between clades. A product complex with the unusual β-3,6-anhydro-L-galactose residue sheds light on the inverting catalytic mechanism of the GH117 enzymes as well as the structure of this unique sugar produced by hydrolysis of the agarophyte red algal cell wall. [ABSTRACT FROM AUTHOR]

Published
2015
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