105,117 research outputs found

    Plant Physiology, Development and Metabolism

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    Water is one of the most important constituents of life. Chemically, water is the hydride of oxygen. Oxygen, being more electronegative, exerts a strong attractive pull on its electrons. This unequal attraction results in small positive charge on twohydrogenmoleculesandasmallnegativechargeontheoxygenmolecule.The two lone pairs of electrons of the oxygen molecule result in bending of water molecule. The partial charges on oxygen and hydrogen molecules result in high electric dipole moment and polarity of water molecule

    Fungal glycoside hydrolase family 44 xyloglucanases are restricted to the phylum Basidiomycota and show a distinct xyloglucan cleavage pattern

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    Xyloglucan is a prominent matrix heteropolysaccharide binding to cellulose microfibrils in primary plant cellwalls. Hence, the hydrolysis of xyloglucan facilitates the overall lignocellulosic biomass degradation. Xyloglucanases (XEGs) are key enzymes classified in several glycoside hydrolase (GH) families. So far, family GH44 has been shown to contain bacterial XEGs only. Detailed genome analysis revealed GH44 members in fungal species from the phylum Basidiomycota, but not in other fungi, which we hypothesized to also be XEGs. Two GH44 enzymes from Dichomitus squalens and Pleurotus ostreatus were heterologously produced and characterized. They exhibited XEG activity and displayed a hydrolytic cleavage pattern different fromthat observed in fungal XEGs from other GH families. Specifically, the fungal GH44 XEGs were not hindered by substitution of neighboring glucosyl units and generated various," "XXXG- type,'' "GXXX(G)-type,'' and "XXX-type'' oligosaccharides. Overall, these fungal GH44 XEGs represent a novel class of enzymes for plant biomass conversion and valorization.Peer reviewe

    Temporal transcriptome analysis of the white-rot fungus Obba rivulosa shows expression of a constitutive set of plant cell wall degradation targeted genes during growth on solid spruce wood

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    The basidiomycete white-rot fungus Obba rivulosa, a close relative of Gelatoporia (Ceriporiopsis) subvermispora, is an efficient degrader of softwood. The dikaryotic O. rivulosa strain T241i (FBCC949) has been shown to selectively remove lignin from spruce wood prior to depolymerization of plant cell wall polysaccharides, thus possessing potential in biotechnological applications such as pretreatment of wood in pulp and paper industry. In this work, we studied the time-course of the conversion of spruce by the genome-sequenced monokaryotic O. rivulosa strain 3A-2, which is derived from the dikaryon T241i, to get insight into transcriptome level changes during prolonged solid state cultivation. During 8-week cultivation, O. rivulosa expressed a constitutive set of genes encoding putative plant cell wall degrading enzymes. High level of expression of the genes targeted towards all plant cell wall polymers was detected at 2-week time point, after which majority of the genes showed reduced expression. This implicated non-selective degradation of lignin by the O. rivulosa monokaryon and suggests high variation between mono- and dikaryotic strains of the white-rot fungi with respect to their abilities to convert plant cell wall polymers.Peer reviewe

    JUNGBRUNNEN1 confers drought tolerance downstream of the HD-Zip I Transcription factor AtHB13

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    Low water availability is the major environmental factor limiting growth and productivity of plants and crops and is therefore considered of high importance for agriculture affected by climate change. Identifying regulatory components controlling the response and tolerance to drought stress is thus of major importance. The NAC transcription factor (TF) JUNGBRUNNEN1 (JUB1) from Arabidopsis thaliana extends leaf longevity under non-stress growth conditions, lowers cellular hydrogen peroxide (H2O2) level, and enhances tolerance against heat stress and salinity. Here, we additionally find that JUB1 strongly increases tolerance to drought stress in Arabidopsis when expressed from both, a constitutive (CaMV 35S) and an abiotic stress-induced (RD29A) promoter. Employing a yeast one-hybrid screen we identified HD-Zip class I TF AtHB13 as an upstream regulator of JUB1. AtHB13 has previously been reported to act as a positive regulator of drought tolerance. AtHB13 and JUB1 thereby establish a joint drought stress control module.Fil: Ebrahimian Motlagh, Saghar. University of Potsdam; Alemania. Max Planck Institute of Molecular Plant Physiology; AlemaniaFil: Ribone, Pamela AnahĂ­. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - Santa Fe. Instituto de AgrobiotecnologĂ­a del Litoral. Universidad Nacional del Litoral. Instituto de AgrobiotecnologĂ­a del Litoral; ArgentinaFil: Thirumalaikumar, Venkatesh P.. Max Planck Institute of Molecular Plant Physiology; Alemania. University of Potsdam; AlemaniaFil: Allu, Annapurna D.. Max Planck Institute of Molecular Plant Physiology; Alemania. University of Potsdam; AlemaniaFil: Chan, Raquel Lia. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - Santa Fe. Instituto de AgrobiotecnologĂ­a del Litoral. Universidad Nacional del Litoral. Instituto de AgrobiotecnologĂ­a del Litoral; ArgentinaFil: Mueller Roeber, Bernd. University of Potsdam; Alemania. Max Planck Institute of Molecular Plant Physiology; AlemaniaFil: Balazadeh, Salma. University of Potsdam; Alemania. Max Planck Institute of Molecular Plant Physiology; Alemani

    Selective cleavage of lignin β-O-4 aryl ether bond by β-etherase of the white-rot fungus Dichomitus squalens.

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    Production of value-added compounds from a renewable aromatic polymer, lignin, has proven to be challenging. Chemical procedures, involving harsh reaction conditions, are costly and often result in nonselective degradation of lignin linkages. Therefore, enzymatic catalysis with selective cleavage of lignin bonds provides a sustainable option for lignin valorization. In this study, we describe the first functionally characterized fungal intracellular beta-etherase from the wood-degrading white-rot basidiomycete Dichomitus squalens. This enzyme, Ds-GST1, from the glutathione-Stransferase superfamily selectively cleaved the beta-O-4 aryl ether bond of a dimeric lignin model compound in a glutathionedependent reaction. Ds-GST1 also demonstrated activity on polymeric synthetic lignin fractions, shown by a decrease in molecular weight distribution of the lactase -oxidized guaiacyl dehydrogenation polymer. In addition to a possible role of DsGST1 in intracellular catabolism of lignin-derived aromatic compounds, the cleavage of the most abundant linkages in lignin under mild reaction conditions makes this biocatalyst an attractive green alternative in biotechnological applications.Peer reviewe

    Plant Physiology

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    Exam paper for second semester: Plant Physiolog

    Plant Physiology

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    Exam paper for second semester: Plant Physiolog

    Identification of a gene encoding the last step of the L-rhamnose catabolic pathway in Aspergillus niger revealed the inducer of the pathway regulator

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    In fungi, L-rhamnose (Rha) is converted via four enzymatic steps into pyruvate and L-lactaldehyde, which enter central carbon metabolism. In Aspergillus niger, only the genes involved in the first three steps of the Rha catabolic pathway have been identified and characterized, and the inducer of the pathway regulator RhaR remained unknown. In this study, we identified the gene (lkaA) involved in the conversion of L-2-keto-3-deoxyrhamnonate (L-KDR) into pyruvate and L-lactaldehyde, which is the last step of the Rha pathway. Deletion of lkaA resulted in impaired growth on L-rhamnose, and potentially in accumulation of L-KDR. Contrary to Delta lraA, Delta lrlA and Delta lrdA, the expression of the Rha-responsive genes that are under control of RhaR, were at the same levels in Delta lkaA and the reference strain, indicating the role of L-KDR as the inducer of the Rha pathway regulator.Peer reviewe

    Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism

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    How organisms integrate metabolism with the external environment is a central question in biology. Here, we describe a novel regulatory small molecule, a proteogenic dipeptide Tyr-Asp, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Specifically, Tyr-Asp inhibits the activity of a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPC), and redirects glucose toward pentose phosphate pathway (PPP) and NADPH production. In line with the metabolic data, Tyr-Asp supplementation improved the growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. Moreover, inhibition of Arabidopsis phosphoenolpyruvate carboxykinase (PEPCK) activity by a group of branched-chain amino acid-containing dipeptides, but not by Tyr-Asp, points to a multisite regulation of glycolytic/gluconeogenic pathway by dipeptides. In summary, our results open the intriguing possibility that proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism.Fil: Moreno, Juan C.. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Rojas, Bruno Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Vicente, Rubén. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Gorka, Michal. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Matz, Timon. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Chodasiewicz, Monika. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Peralta?Ariza, Juan S.. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Zhang, Youjun. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Alseekh, Saleh. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Childs, Dorothee. European Molecular Biology Laboratory; AlemaniaFil: Luzarowski, Marcin. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Nikoloski, Zoran. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Zarivach, Raz. Ben Gurion University of the Negev; IsraelFil: Walther, Dirk. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Hartman, Matias Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Fernie, Alisdair R.. Max Planck Institute Of Molecular Plant Physiology; AlemaniaFil: Skirycz, Aleksandra. Max Planck Institute Of Molecular Plant Physiology; Alemani
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