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Akira Isogai - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:The crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:Abstract The crystal structure of endo-β-(1→4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical β-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1–II′.
Merja Penttila - One of the best experts on this subject based on the ideXlab platform.
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visualization of cellobiohydrolase i from Trichoderma reesei moving on crystalline cellulose using high speed atomic force microscopy
Methods in Enzymology, 2012Co-Authors: Kiyohiko Igarashi, Takayuki Uchihashi, Anu Koivula, Masahisa Wada, Satoshi Kimura, Toshio Ando, Merja Penttila, Masahiro SamejimaAbstract:Cellulases hydrolyze β-1,4-glucosidic linkages of insoluble cellulose at the solid/liquid interface, generating soluble cellooligosaccharides. We describe here our method for real-time observation of the behavior of cellulase molecules on the substrate, using high-speed atomic force microscopy (HS-AFM). When glycoside hydrolase family 7 cellobiohydrolase from Trichoderma reesei (TrCel7A) was incubated with crystalline cellulose, many enzyme molecules were observed to move unidirectionally on the surface of the substrate by HS-AFM. The velocity of the moving molecules of TrCel7A on cellulose I crystals was estimated by means of image analysis.
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expression of Trichoderma reesei cellulases cbhi and egi in ashbya gossypii
Applied Microbiology and Biotechnology, 2010Co-Authors: Orquidea Ribeiro, Lucília Domingues, Marilyn G Wiebe, Marja Ilmen, Merja PenttilaAbstract:To explore the potential of Ashbya gossypii as a host for the expression of recombinant proteins and to assess whether protein secretion would be more similar to the closely related Saccharomyces cerevisiae or to other filamentous fungi, endoglucanase I (EGI) and cellobiohydrolase I (CBHI) from the fungus Trichoderma reesei were successfully expressed in A. gossypii from plasmids containing the two micron sequences from S. cerevisiae, under the S. cerevisiae PGK1 promoter. The native signal sequences of EGI and CBHI were able to direct the secretion of EGI and CBHI into the culture medium in A. gossypii. Although CBHI activity was not detected using 4-methylumbelliferyl-β-d-lactoside as substrate, the protein was detected by Western blot using monoclonal antibodies. EGI activity was detectable, the specific activity being comparable to that produced by a similar EGI producing S. cerevisiae construct. More EGI was secreted than CBHI, or more active protein was produced. Partial characterization of CBHI and EGI expressed in A. gossypii revealed overglycosylation when compared with the native T. reesei proteins, but the glycosylation was less extensive than on cellulases expressed in S. cerevisiae.
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the Trichoderma reesei hydrophobin genes hfb1 and hfb2 have diverse functions in fungal development
Fems Microbiology Letters, 2005Co-Authors: Sanna Askolin, Han A B Wosten, Merja Penttila, Tiina NakarisetalaAbstract:Hydrophobins are fungal self-assembling proteins. Here, the hydrophobin genes hfb1 and hfb2 were deleted in Trichoderma reesei and their biological roles studied. Our results suggest that HFBI has a role in hyphal development and HFBII in sporulation. Sporulating colonies of the Δhfb2 strain were wettable and sporulation was only 50% of the parent strain. Colonies of Δhfb1 showed wettable and fluffy phenotype. In shaken liquid cultures, the hyphae of Δhfb1 were thinner and biomass formation was slower compared to the parent strain while in static liquid cultures no aerial hyphae were formed. Expressing the Schizophyllum commune hydrophobin SC3 in the Δhfb1 strain restored the formation of aerial hyphae.
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the Trichoderma reesei hydrophobin genes hfb1 and hfb2 have diverse functions in fungal development
Fems Microbiology Letters, 2005Co-Authors: Sanna Askolin, Han A B Wosten, Merja Penttila, Tiina NakarisetalaAbstract:Hydrophobins are fungal self-assembling proteins. Here, the hydrophobin genes hfb1 and hfb2 were deleted in Trichoderma reesei and their biological roles studied. Our results suggest that HFBI has a role in hyphal development and HFBII in sporulation. Sporulating colonies of the Deltahfb2 strain were wettable and sporulation was only 50% of the parent strain. Colonies of Deltahfb1 showed wettable and fluffy phenotype. In shaken liquid cultures, the hyphae of Deltahfb1 were thinner and biomass formation was slower compared to the parent strain while in static liquid cultures no aerial hyphae were formed. Expressing the Schizophyllum commune hydrophobin SC3 in the Deltahfb1 strain restored the formation of aerial hyphae.
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genetic and biochemical characterization of the Trichoderma reesei hydrophobin hfbi
FEBS Journal, 1996Co-Authors: Tiina Nakarisetala, Nina Aro, Nisse Kalkkinen, Edward Alatalo, Merja PenttilaAbstract:The hfb1 gene of the filamentous fungus Trichoderma reesei, previously cloned as a gene which was abundantly expressed when the fungus was grown on glucose-containing medium, was shown to encode a novel fungal hydrophobin. The encoded 97-amino-acid protein is cysteine-rich and has a typical signal sequence for secretion. Signal-sequence cleavage and putative proteolytic processing results in the mature HFBI protein of 75 amino acids. Antibodies raised against the HFBI protein expressed in Escherichia coli detected the T. reesei HFBI protein in the fungal cell wall and in the culture medium of submerged glucose-containing cultures. The identity of HFBI was verified by N-terminal and peptide sequencing of proteins purified both from the cell wall and culture medium. In the cell wall most of the HFBI formed SDS-insoluble complexes that could be extracted with trifluoroacetic acid. Bubbling or freezing of the culture medium caused HFBI to form aggregates that coprecipitated with a yellow pigment produced by the fungus.
Masahiro Samejima - One of the best experts on this subject based on the ideXlab platform.
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visualization of cellobiohydrolase i from Trichoderma reesei moving on crystalline cellulose using high speed atomic force microscopy
Methods in Enzymology, 2012Co-Authors: Kiyohiko Igarashi, Takayuki Uchihashi, Anu Koivula, Masahisa Wada, Satoshi Kimura, Toshio Ando, Merja Penttila, Masahiro SamejimaAbstract:Cellulases hydrolyze β-1,4-glucosidic linkages of insoluble cellulose at the solid/liquid interface, generating soluble cellooligosaccharides. We describe here our method for real-time observation of the behavior of cellulase molecules on the substrate, using high-speed atomic force microscopy (HS-AFM). When glycoside hydrolase family 7 cellobiohydrolase from Trichoderma reesei (TrCel7A) was incubated with crystalline cellulose, many enzyme molecules were observed to move unidirectionally on the surface of the substrate by HS-AFM. The velocity of the moving molecules of TrCel7A on cellulose I crystals was estimated by means of image analysis.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:The crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:Abstract The crystal structure of endo-β-(1→4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical β-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1–II′.
Kiyohiko Igarashi - One of the best experts on this subject based on the ideXlab platform.
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visualization of cellobiohydrolase i from Trichoderma reesei moving on crystalline cellulose using high speed atomic force microscopy
Methods in Enzymology, 2012Co-Authors: Kiyohiko Igarashi, Takayuki Uchihashi, Anu Koivula, Masahisa Wada, Satoshi Kimura, Toshio Ando, Merja Penttila, Masahiro SamejimaAbstract:Cellulases hydrolyze β-1,4-glucosidic linkages of insoluble cellulose at the solid/liquid interface, generating soluble cellooligosaccharides. We describe here our method for real-time observation of the behavior of cellulase molecules on the substrate, using high-speed atomic force microscopy (HS-AFM). When glycoside hydrolase family 7 cellobiohydrolase from Trichoderma reesei (TrCel7A) was incubated with crystalline cellulose, many enzyme molecules were observed to move unidirectionally on the surface of the substrate by HS-AFM. The velocity of the moving molecules of TrCel7A on cellulose I crystals was estimated by means of image analysis.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:The crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:Abstract The crystal structure of endo-β-(1→4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical β-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1–II′.
Naotake Konno - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:The crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'.
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crystal structure of polysaccharide lyase family 20 endo β 1 4 glucuronan lyase from the filamentous fungus Trichoderma reesei
FEBS Letters, 2009Co-Authors: Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira IsogaiAbstract:Abstract The crystal structure of endo-β-(1→4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical β-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1–II′.
