Functional analysis of the RHOIII and 14-3-3 proteins of Trichoderma reesei
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Technical Research Centre of Finland , Espoo [Finland]
Trichoderma reesei -- Genetics., Proteins -- Secretion -- Regulation., G proteins -- Secretion -- Regula
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Functional analysis of the RHOIII and proteins of Trichoderma reesei VTT PUBLICATIONS Mäntylä, Vesa-Matti.
Description Functional analysis of the RHOIII and 14-3-3 proteins of Trichoderma reesei EPUB
Discrete hidden Markov models with application to isolated user-dependent hand gesture recognition. Oasmaa, Anja & Peacocke, Cordner. A guide to physical property characterisation. Vasara, Tuija. Functional analysis of the RHOIII and proteins of Trichoderma reesei. 93 p. + app.
54 p. Tala, Tuomas. Transport Barrier and Current Profile Studies. Request PDF | Trichoderma reesei rho3, a homologue of yeast RHO3, suppresses the growth defect of yeast sec mutation | The Trichoderma reesei gene, rho3, encoding the functional. The proteins are highly conserved, ubiquitously expressed proteins taking part in numerous cellular processes.
Two genes encoding proteins, ftt1 and ftt2, were isolated and characterised from the filamentous fungus Trichoderma reesei. Vasara, Tuija. Functional analysis of the RHOIII and proteins of Trichoderma reesei. 93 p. + app. 54 p. Tala, Tuomas. Transport Barrier and Current Profile Studies on.
In Trichoderma reesei light is an important factor in the regulation of glycoside hydrolase gene expression. We therefore investigated the influence of different light intensities on cellulase activity and protein secretion.
Differentially secreted proteins Cited by: 7. Trichoderma reesei. Trichoderma reesei is an efficient cell factory for protein production and also acts as a host for homologous and heterologous protein production, and hence is.
Functional analysis of the cellulase promoter cbh1 of the filamentous fungus Trichoderma reesei was carried out using the Escherichia coli lacZ gene as a reporter. An assay based on cultivation on solid medium in microtiter plates was developed that allows rapid and reliable semiquantitative analysis of β-galactosidase Cited by: Curr Genet () – DOI /s RESEARCH ARTICLE Trichoderma G protein-coupled receptors: functional characterisation of a cAMP receptor-like protein from Trichoderma.
Limited proteolysis (papain) of the cellobiohydrolase I (CBH I, 65 kDa) from Trichoderma reesei led to the seperation of two functional domains: a core protein (55 kDa) Cited by: The filamentous fungus Trichoderma reesei (T. reesei) is an excellent producer of xylanolytic enzymes [16,17].
Reports concerning AFases from T. reesei are quite limited. In previous work, we have found a complete xylanolytic enzyme system in the culture filtrate of T. reesei C by secretome analysis Author: Junyong Sun, Feng Xu, Jian Lu.
The filamentous cellulolytic fungus Trichoderma reesei is known to be an exceptionally efficient producer of cellulases and hemicellulases acting in synergy to degrade lignocellulosic materials.T.
reesei Cited by: Trichoderma reesei is the main industrial producer of cellulases and hemicellulases that are used to depolymerize biomass in a variety of biotechnical applications. Many of the production strains currently in use have been generated by classical mutagenesis.
In this study we characterized genomic alterations in high-producing mutants of T. reesei Cited by: Pakula et al. Biotechnol Biofuels DOI /s RESEARCH Genome wide analysis of protein production load in Trichoderma reesei Tiina M.
Pakula1, Heli Nygren1, Dorothee Barth1, Markus Heinonen2,3, Sandra Castillo1, Merja Penttilä1 and Mikko Arvas1* Abstract Background: The filamentous fungus Trichoderma reesei Cited by: The industrially important protein producer, the filamentous fungus Trichoderma reesei, a clonal derivative of the ascomycete Hypocrea jecorina, is adapted to growth in nutrient poor environments, where it is able to use complex plant material as carbon source.T.
reesei Cited by: Analysis of the abundance of CREI in Rut-C (a) The Trichoderma reesei wild-type strain QM6a (green bars) and Rut-C30 (yellow bars) were pre-grown on glycerol and then transferred to media supplemented with D-glucose (G), sophorose (SO) or without carbon source (NC), respectively, and incubated for 3 Cited by: BIOTECHNOLOGY- Vol III - Genetic Engineering of Fungal Cells-Margo M.
Details Functional analysis of the RHOIII and 14-3-3 proteins of Trichoderma reesei EPUB
Moore ©Encyclopedia of Life Support Systems (EOLSS) reesei and a description of the utility of the cbh1 promoter to drive protein. Trichoderma reesei is well-known for its excellent cellu-lase producing ability. Cre1 and ACEI are the two transcription factors that repress expression of cellulase genes (Strauss et al.
; Ilmen et al. ; Saloheimo et al. ; Aro et al.
Download Functional analysis of the RHOIII and 14-3-3 proteins of Trichoderma reesei FB2
Disruption of cre1 or ace1 can improve cellulase production in T. reesei. Functional analyses of Trichoderma reesei LAE1 reveal conserved and contrasting roles of this regulator. Karimi-Aghcheh R(1), Bok JW, Phatale PA, Smith KM, Baker SE, Lichius A, Omann Cited by: Swollenin, a protein first characterized in the saprophytic fungus Trichoderma reesei, contains an N-terminal carbohydrate-binding module family 1 domain (CBD) with cellulose-binding function and a C-terminal expansin-like domain.
This protein was identified by liquid chromatography-mass spectrometry among many other cellulolytic proteins. Proteomic Analysis of pH and Strains Dependent Protein Secretion of Trichoderma reesei. Journal of Proteome Research10 (10), DOI: /prt. Cited by: Functional characterization of Rho GTPases in Aspergillus niger uncovers conserved and diverged roles of Rho proteins within filamentous fungi Min Jin Kwon Department Molecular Cited by: Functional analysis of the RHOIII and proteins of Trichoderma reesei / Tuija Vasara.
Espoo [Finland]: Technical Research Centre of Finland, T1.V no Transport. "Trichoderma reesei prs12 encodes a stress- and unfolded-protein-response-inducible regulatory subunit of the fungal 26S proteasome.
Current Genetics, 33 (), - S.P. Trichoderma reesei is an industrially important cellulolytic filamentous light of of T. reesei's capacity to secrete large amounts of cellulases and hemi cellulases, the DOE is funding research into developing T.
reesei. system of the filamentous fungus Trichoderma reesei has been found to be one of the most effective for hydrolysis of cellulosic materials. reesei produces an extracellular, stable, and efficient cellulase enzyme system (Tengborg et al.
; Lynd et al. reesei. Media, Growth Conditions, and Metabolite Analysis. reesei, strain QMwas obtained from the American Type Culture Collection (ATCC ).A liter inoculum. Overall asparagine and cysteine are the two most over represented amino acids (43 and 37 % more, respectively) when comparing the relative amino acid contents of sequences of T.
reesei proteins found to be secreted based on 2D-gel analysis and other T. reesei proteins. More fundamentally Cited by: Trichoderma reesei is the best-known cellulase producer among filamentous fungi, and the preferred organism for the production of industrial cellulases [23,24].
The cellulolytic system of T. reesei Cited by: The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The 3-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus T.
reesei [T. longibrachiatum] reveals an α-β protein Cited by:. The effect of induction of protein production was studied in bioreactor cultures of T. reesei strain Rut-C30 and its transformant expressing endoglucanase I core domain (EGI, Cel7B) fused with a hydrophobic peptide tag.
The tag was previously designed for efficient purification of the fusion protein .Fungal-derived, copper-dependent polysaccharide monooxygenases (PMOs), formerly known as GH61 proteins, have recently been shown to catalyze the O2-dependent oxidative cleavage.
Alamethicin is a membrane-active peptide isolated from the beneficial root-colonising fungus Trichoderma viride. This peptide can insert into membranes to form voltage Cited by:
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