References of "Vandenbol, Micheline"
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See detailInteraction network of antimicrobial peptides of Arabidopsis thaliana, based on hith-throughput yeast two-hybrid screening
Damon, Coralie ULg; Dmitrieva, Joelia Borisnova; Muhovski, Yordan et al

in Plant Physiology & Biochemistry (2012)

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See detailChanges in termites feeding diets for gut micro-organisms selection and further cultivation
Bauwens, Julien ULg; Brasseur, Catherine ULg; Matteotti, Christel ULg et al

Poster (2011, October 02)

Termites gut may overcome important dietary perturbations, initial diversity acting as key point buffering effects on host, although termites possess their own enzymatic system. Some artificial diets ... [more ▼]

Termites gut may overcome important dietary perturbations, initial diversity acting as key point buffering effects on host, although termites possess their own enzymatic system. Some artificial diets permitted a simplification of the lower termites gut symbiotic system, which could be used as first step in symbionts isolation and cultivation. Preliminary assay of cultivation actually gave encouraging results. Proteomic proved to be suitable tool to investigate such a complex system. Nevertheless, for some symbionts very few genes are sequenced, which should lead to more targeted proteomic studies. Protein chromatography will allow to split up the proteome and more accurate analysis. [less ▲]

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See detailScreening of a soil metatranscriptomic library by functional complementation of Saccharomyces cerevisiae mutants.
Kellner, Harald ULg; Luis, Patricia; Portetelle, Daniel ULg et al

in Microbiological Research (2011), 166(5), 360368

Metatranscriptomics applied to environmental transcripts provides unique opportunities to reveal microbial activity in the environment and to discover novel enzymes of potential use in biotechnological ... [more ▼]

Metatranscriptomics applied to environmental transcripts provides unique opportunities to reveal microbial activity in the environment and to discover novel enzymes of potential use in biotechnological applications. Here, by functional complementation of a pho5(-) mutation (affecting a repressible acid phosphatase) and a his3(-) mutation in Saccharomyces cerevisiae, we identified fungal genes encoding an acid phosphatase and an imidazoleglycerol-phosphate dehydratase in a metatranscriptomic library, which was obtained by reverse-transcribed polyA fraction of total RNA extracted from the organic layer of a sugar maple forest soil, constructed in the modified yeast secretion vector pTEF-MF-SfiI A/B. Yeast transformants exhibiting phosphatase activity were identified in a colony-staining assay and transformants with his3(-)-complementing genes were detected by plating on histidine-deficient medium. In each screen one DNA insert was found and sequenced. The sequenced his3(-)-complementing gene showed strong similarity to a basidiomycete imidazoleglycerol-phosphate dehydratase (76% identity to a Phaffia rhodozyma enzyme). The candidate showing phosphatase activity was found to produce phosphatase extracellularly, the enzyme showing highest activity at pH 4 and between 40 and 50°C when 4-nitrophenyl phosphate was used as substrate. The sequenced insert showed strong similarity to a basidiomycete acid phosphatase (60% identity to Postia placenta). [less ▲]

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See detailFunctional suppression of the yeast msb3- mutation
Biver, Sophie ULg; Vandenbol, Micheline ULg

Poster (2010, September)

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See detailFungal gene expression in a forest soil
Kellner, Harald ULg; Portetelle, Daniel ULg; Vandenbol, Micheline ULg

Poster (2010, August)

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See detailCaractérisation de la diversité des organismes symbiotiques et des activités glycosyl hydrolases dans le tube digestif de Reticulitermes santonensis (Feytaud) par une approche multidisciplinaire
Bauwens, Julien ULg; Matteotti, Christel ULg; Brognaux, Alison ULg et al

Scientific conference (2010, July 08)

Le bioéthanol cellulosique pourrait être une solution pour satisfaire le besoin croissant en énergie renouvelable. Actuellement, l’efficience de la transformation de la cellulose en sucres fermentescibles ... [more ▼]

Le bioéthanol cellulosique pourrait être une solution pour satisfaire le besoin croissant en énergie renouvelable. Actuellement, l’efficience de la transformation de la cellulose en sucres fermentescibles reste le principal facteur limitant. La recherche de nouvelles glycosyl hydrolases constitue une voie potentielle d’amélioration de la valorisation des composés ligno-cellulosiques. Trois types de glycosyl hydrolases sont généralement produites par les organismes capables d’utiliser efficacement ces composés : les endoglucanases, les exoglucanases/cellobiohydrolases, et les β-glucosidases. Dans les processus de digestion de la cellulose par les animaux, des organismes symbiotiques tels que des bactéries, des protistes et/ou des champignons sont fréquemment observés. Ces organismes contribuent en grande partie voir totalement à la production des complexes enzymatiques nécessaires. Chez les termites inférieures, comme notre modèle Reticulitermes santonensis (Feytaud), des protistes et des bactéries sont impliqués dans un système symbiotique complexe. Une étude multidisciplinaire est menée afin d’approfondir les rôles respectifs des différents groupes de symbiontes, via des approches « omiques », à savoir la protéomique (ESI-LC-MS-MS, 2D-SDS-PAGE couplée avec une analyse en spectrométrie de masse du type MALDI-TOF pour l’identification des protéines), la génomique (avec une approche métagénomique basée sur la construction d’une large banque de cDNA), la métabolomique (caractérisation des produits de dégradation de carbohydrates via une strategie LC-MS). De plus, l’isolation de microorganismes a également été employée dans la caractérisation de la diversité et de l’activité des glycosyl hydrolases chez R. santonensis. [less ▲]

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See detailFungi Unearthed: Transcripts Encoding Lignocellulolytic and Chitinolytic Enzymes in Forest Soil
Kellner, Harald ULg; Zak, Don; Vandenbol, Micheline ULg

in PLoS ONE (2010), 5(Issue 6), 10971-7

Detailed reference viewed: 33 (6 ULg)