{Reference Type}: Journal Article

{Author}: Claire Veneault-Fourrey；Carine Commun；Annegret Kohler；Emmanuelle Morin；Raffaella Balestrini；Jonathan Plett；Etienne Danchin；Pedro Coutinho；Ad Wiebenga；Ronald P de Vries；Bernard Henrissat；Francis Martin

{Year}: 2014

{Title}:Genomic and transcriptomic analysis of Laccaria bicolor CAZome reveals insights into polysaccharides remodelling during symbiosis establishment

{Tag}: 0

{Star}: 0

{Volume}: 72

{Issue}: 0

{Pages}: 168-181

{DOL}:http://dx.doi.org/10.1016/j.fgb.2014.08.007

{ISBN/ISSN}:1087-1845

{Keywords}: Ectomycorrhiza；Symbiosis；Carbohydrate Active enZymes；Transcriptome profiling

{Abstract}: Ectomycorrhizal fungi, living in soil forests, are required microorganisms to sustain tree growth and productivity. The establishment of mutualistic interaction with roots to form ectomycorrhiza (ECM) is not well known at the molecular level. In particular, how fungal and plant cell walls are rearranged to establish a fully functional ectomycorrhiza is poorly understood. Nevertheless, it is likely that Carbohydrate Active enZymes (CAZyme) produced by the fungus participate in this process.

         Genome-wide transcriptome profiling during ECM development was used to examine how the CAZome of Laccaria bicolor is regulated during symbiosis establishment.

         CAZymes active on fungal cell wall were upregulated during ECM development in particular after 4 weeks of contact when the hyphae are surrounding the root cells and start to colonize the apoplast. We demonstrated that one expansin-like protein, whose expression is specific to symbiotic tissues, localizes within fungal cell wall.

         Whereas L. bicolor genome contained a constricted repertoire of CAZymes active on cellulose and hemicellulose, these CAZymes were expressed during the first steps of root cells colonization. L. bicolor retained the ability to use homogalacturonan, a pectin-derived substrate, as carbon source. CAZymes likely involved in pectin hydrolysis were mainly expressed at the stage of a fully mature ECM.

           All together, our data suggest an active remodelling of fungal cell wall with a possible involvement of expansin during ECM development. By contrast, a soft remodelling of the plant cell wall likely occurs through the loosening of the cellulose microfibrils by AA9 or GH12 CAZymes and middle lamella smooth remodelling through pectin (homogalacturonan) hydrolysis likely by GH28, GH12 CAZymes.

{Author Address}:   http://www.sciencedirect.com

{Language}: English

{Reference Type}: Journal Article

{Author}: Jin jing Zhang；Liang Shi；Hui Chen；Yun qi Sun；Ming wen Zhao；Ang Ren；Ming jie Chen；Hong Wang；Zhi yong Feng

{Year}: 2014

{Title}:An efficient Agrobacterium-mediated transformation method for the edible mushroom Hypsizygus

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{Star}: 0

{Volume}: 169

{Issue}: 9-10

{Pages}: 741-748

{DOL}: http://dx.doi.org/10.1016/j.micres.2014.01.004

{ISBN/ISSN}:0944-5013

{Keywords}: Agrobacterium-mediated transformation；Hypsizygus marmoreus；gpd；Promoter

{Abstract}:

Hypsizygus marmoreus is one of the major edible mushrooms in East Asia. As no efficient transformation method, the molecular and genetics studies were hindered. The glyceraldehyde-3-phosphate dehydrogenase (GPD) gene of H. marmoreus was isolated and its promoter was used to drive the hygromycin B phosphotransferase (HPH) and enhanced green fluorescent protein (EGFP) in H. marmoreus. Agrobacterium tumefaciens-mediated transformation (ATMT) was successfully applied in H. marmoreus. The transformation parameters were optimized, and it was found that co-cultivation of bacteria with protoplast at a ratio of 1000:1 at a temperature of 26 °C in medium containing 0.3 mM acetosyringone resulted in the highest transformation efficiency for Agrobacterium strain. Besides, three plasmids, each carrying a different promoter (from H. marmoreus, Ganoderma lucidum and Lentinula edodes) driving the expression of an antibiotic resistance marker, were also tested. The construct carrying the H. marmoreus gpd promoter produced more transformants than other constructs. Our analysis showed that over 85% of the transformants tested remained mitotically stable even after five successive rounds of subculturing. Putative transformants were analyzed for the presence of hph gene by PCR and Southern blot. Meanwhile, the expression of EGFP in H. marmoreus transformants was detected by fluorescence imaging. This ATMT system increases the transformation efficiency of H. marmoreus and may represent a useful tool for molecular genetic studies in this mushroom spec

{Author Address}:   http://www.sciencedirect.com

{Language}: English

{Reference Type}: Journal Article

{Author}: Fhernanda R Smiderle；Guilherme L Sassaki；Leo J L   D Van Griensven；Marcello Iacomini

{Year}: 2013

{Title}:Isolation and chemical characterization of a glucogalactomannan of the medicinal mushroom Cordyceps militaris

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{Star}: 0

{Volume}: 97

{Issue}: 1

{Pages}: 74-80

{DOL}: http://dx.doi.org/10.1016/j.carbpol.2013.04.049

{ISBN/ISSN}:0144-8617

{Keywords}: Cordyceps militaris；Glucogalactomannan；Ascomycete；NMR spectrometry

{Abstract}: Cordyceps militaris dried fruiting bodies were extracted with 5% KOH solution. The extract was purified by freeze-thawing treatment, and dialysis (100 kDa), giving rise to a homogeneous polysaccharide (Mw 23,000 Da). Its monosaccharide composition was mannose (56.7%), galactose (34.5%), and glucose (8.8%). The anomeric configurations were determined by their coupling constants. A complex polysaccharide was identified by NMR and methylation analysis. The HSQC spectrum showed signals at δ 107.7/5.06 and 106.1/5.14; 105.9/5.12 relative to β-d-Galf, and O-2-substituted β-d-Galf units, respectively. The sign at δ 104.4/5.21 corresponded to α-d-Galf. Other signals corresponded to α-d-Manp O-6- and O-2-substituted (δ 100.2/4.94; 100.5/5.27; 100.6/5.23; 100.7/5.16), and α-d-Manp 2,6-di-O-substituted (from δ 99.3 to 99.9). The main linkages, confirmed by methylation analysis, showed the derivatives: 2,3,4-Me3-Manp (11.9%) and 3,4,6-Me3-Manp (28.6%). The branches were (1 → 6)-linked-α-d-Manp or (1 → 2)-linked-β-d-Galf, terminating with β-d-Galf, α-d-Galf, α-d-Galp, or α-d-Manp. 42.7% of the partially hydrolyzed product consisted of 3,4,6-Me3-Manp, suggesting a (1 → 2)-linked backbone.

{Author Address}:   http://www.sciencedirect.com

{Language}: English