Hadar Y

References (2)

Title : Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis - Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
Author(s) : Fernandez-Fueyo E , Ruiz-Duenas FJ , Ferreira P , Floudas D , Hibbett DS , Canessa P , Larrondo LF , James TY , Seelenfreund D , Lobos S , Polanco R , Tello M , Honda Y , Watanabe T , Ryu JS , Kubicek CP , Schmoll M , Gaskell J , Hammel KE , St John FJ , Vanden Wymelenberg A , Sabat G , Splinter BonDurant S , Syed K , Yadav JS , Doddapaneni H , Subramanian V , Lavin JL , Oguiza JA , Perez G , Pisabarro AG , Ramirez L , Santoyo F , Master E , Coutinho PM , Henrissat B , Lombard V , Magnuson JK , Kues U , Hori C , Igarashi K , Samejima M , Held BW , Barry KW , LaButti KM , Lapidus A , Lindquist EA , Lucas SM , Riley R , Salamov AA , Hoffmeister D , Schwenk D , Hadar Y , Yarden O , de Vries RP , Wiebenga A , Stenlid J , Eastwood D , Grigoriev IV , Berka RM , Blanchette RA , Kersten P , Martinez AT , Vicuna R , Cullen D
Ref : Proc Natl Acad Sci U S A , 109 :5458 , 2012
Abstract : Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn(2+). Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium.
ESTHER : Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
PubMedSearch : Fernandez-Fueyo_2012_Proc.Natl.Acad.Sci.U.S.A_109_5458
PubMedID: 22434909
Gene_locus related to this paper: cers8-m2r3x2 , cers8-m2qf37 , cers8-m2pcy7 , cers8-m2pcz3 , cers8-m2qn26 , cers8-m2r654 , cers8-m2r8g9 , cers8-m2ps90 , cers8-m2qn44 , cers8-m2q837 , cers8-m2pjy6 , cers8-m2r609 , cers8-m2qy35 , cers8-m2r1n1 , cers8-m2rl22 , cers8-m2qkx5 , cers8-m2qib7 , cers8-m2rgs8 , cers8-m2rlx6 , cers8-m2r4p3 , cers8-m2rf62 , cers8-m2qyx5 , cers8-m2pcz2 , cers8-m2rm22 , cers8-m2qwb7 , cers8-m2r9u3 , cers8-m2pp23 , cers8-m2r613 , cers8-m2rup8 , cers8-m2piv7 , cers8-m2rch3 , cers8-m2qvf7 , cers8-m2qvb7 , cers8-m2qvb2 , cers8-m2pip7 , cers8-m2rb73 , cers8-m2qgd3 , cers8-m2rcg8 , cers8-m2rb68

Title : Oxidative biodegradation of phosphorothiolates by fungal laccase - Amitai_1998_FEBS.Lett_438_195
Author(s) : Amitai G , Adani R , Sod-Moriah G , Rabinovitz I , Vincze A , Leader H , Chefetz B , Leibovitz-Persky L , Friesem D , Hadar Y
Ref : FEBS Letters , 438 :195 , 1998
Abstract : Organophosphorus (OP) insecticides and nerve agents that contain P-S bond are relatively more resistant to enzymatic hydrolysis. Purified phenol oxidase (laccase) from the white rot fungus Pleurotus ostreatus (Po) together with the mediator 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) displayed complete and rapid oxidative degradation of the nerve agents VX and Russian VX (RVX) and the insecticide analog diisopropyl-Amiton with specific activity: k(sp) = 2200, 667 and 1833 nmol min(-1) mg(-1), respectively (pH 7.4, 37 degrees C). A molar ratio of 1:20 for OP/ABTS and 0.05 M phosphate at pH 7.4 provided the highest degradation rate of VX and RVX. The thermostable laccase purified from the fungus Chaetomium thermophilium (Ct) in the presence of ABTS caused a 52-fold slower degradation of VX with k(sp) = 42 nmol min(-1) mg(-1). The enzymatic biodegradation products were identified by 31P-NMR and GC/MS analysis.
ESTHER : Amitai_1998_FEBS.Lett_438_195
PubMedSearch : Amitai_1998_FEBS.Lett_438_195
PubMedID: 9827544