BGL7 beta-glucosidase and nucleic acids encoding the same

Details BGL7 beta-glucosidase and nucleic acids encoding the same BGL7 beta-glucosidase and nucleic acids encoding the same

2002-11-21

2008-08-05

Prouty, Rebecca E. (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

C435S320100, C435S069100, C435S254200, C435S254110, C435S325000, C435S419000, C435S252300, C536S023200, C536S024500

Reexamination Certificate

active

07407788

ABSTRACT:
The present invention provides a novel β-glucosidase nucleic acid sequence, designated bgl7, and the corresponding BGL7 amino acid sequence. The invention also provides expression vectors and host cells comprising a nucleic acid sequence encoding BGL7, recombinant BGL7 proteins and methods for producing the same.

REFERENCES:
patent: 4435307 (1984-03-01), Barbesgaard et al.
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 4822516 (1989-04-01), Suzuki et al.
patent: 5475101 (1995-12-01), Ward et al.
patent: 5648263 (1997-07-01), Schulein et al.
patent: 5691178 (1997-11-01), Schulein et al.
patent: 5776757 (1998-07-01), Schulein et al.
patent: 6162782 (2000-12-01), Clarkson et al.
patent: 6184018 (2001-02-01), Li et al.
patent: 0 562 003 BA (2002-09-01), None
patent: 1368599 (1974-10-01), None
patent: 2 094 826 (1982-09-01), None
patent: 2 095 275 (1982-09-01), None
patent: WO 91/04673 (1991-04-01), None
Janbon et al., Accession No. U16259, 1996 and Gene, vol. 165(1):109-113, 1995.
Altschul, Stephen F. et al., “Basic Local Alignment Search Tool,” J. Mol. Biol. 215:403-410, 1990.
Altschul, Stephen F. et al., “Gapped BLAST and PSI-BLAST: a new generation of protein database search programs,” Nucl. Acids Res. vol. 25, pp. 3389-3402, 1997.
Aro, Nina et al., “ACEII, a Novel Transcriptional Activator Involved in Regulation of Cellulase and Xylanase Genes ofTrichoderma reesei,” J. Biol. Chem., vol. 276, No. 26, pp. 24309-24314, Jun. 29, 2001.
*Aubert, et al., Ed., p. 11 et seq., Academic Press, 1988.
*Ausubel, G. M. et al. Current Protocols in Molecular Biology, John Wiley & Sons, New York, NY, 1993.
Baldwin, Don et al., Curr. Opin. Plant Biol. 2(2):96-103, 1999.
Baulcombe, D., “ Viruses and gene silencing in plants,” 100 Years of Virology, Calisher and Horzinek eds., Springer-Verlag, New York, NY 15:189-201, 1999.
Bhikhabhai, R. et al., “Isolation of Cellulolytic Enzymes fromTrichoderma ressei QM 9414,” J. Appl. Biochem. 6:336-345, 1984.
Brumbauer, Aniko et al., Fractionation of cellulase and β-glucosidase in aTrichoderma reeseiculture liquid by use of two-phase partitioning, Bioseparation 7:287-295, 1999.
Carter, Paul et al., “Improved oligonucleotide site-directed mutagenesis using M13 vectors,”Nucleic Acids Research, vol. 13, No. 12, pp. 4431-4443, 1985.
Cees, Am. M. et al., “Heterologous Gene Expression in Filamentous Fungi,” More Gene Manipulations in Fungi, Bennett and Lasure, ed., pp. 397-428, 1991.
Chen, Huizhong et al., “Purification and characterization of two extracellular β-glucosidases fromTrichoderma ressei” Biochem et Biophysica Acta 1121:54-60 (1992).
*Coligan, J. E. et al., eds., Current Protocols in Immunology, 1991.
Collen, Anna et al., Journal of Chromatography A 910:275-284, 2001.
Coughlan, Michael et al., “Comparative Biochemistry of Fungal and Bacterial Cellulolytic Enzyme Systems” Biochemistry and Genetics of Cellulose Degradation, pp. 11-30 1988.
Cummings, C. et al., “Secretion ofTrichoderma resseiβ-glucosidase bySaccharomyces cerevisiae, ” Curr. Genet. 29:227-233, 1996.
Dayhoff, M.O. et al., “A Model of Evolutionary Change in Proteins,” Atlas of Protein Sequence and Structure, National Biomedical Research Foundation, Washington, D.C., vol. 5, Supplement 3, Chapter 22, pp. 345-352 1978.
Deutscher, Murray P., “Rethinking Your Purification Procedure,” Methods in Enzymology, vol. 182, No. 57, pp. 779, 1990.
*Doolittle, R. R., Of URFs and ORFs, University Science Books, CA, 1986.
Ellouz, S. et al., “Analytical Separation ofTrichoderma reeseiCellulases by Ion-Exchange Fast Protein Liquid Chromatography,” J. Chromatography 396:307-317, 1987.
Fields, Stanley et al., “A novel genetic system to detect protein-protein interactions,” Nature, 340:245-246, 1989.
Filho, Edivaldo, “Purification and characterization of a β-glucosidase from solid-state cultures ofHumicola griseavar.thermoidea,” Can. J. Microbiol. 42:1-5, 1996.
Fliess, A. et al., “Characterization of Cellulases by HPLC Separation,” Eur. J. Appl. Microbiol. Biotechnol. 17:314-318, 1983.
Freer, Shelby, “Kinetic Characterization of a β-Glucosidase from a Yeast,Candida wickerhamii,” J. Biol. Chem. vol. 268, No. 13, pp. 9337-9342, 1993.
*Freshney, R. I., ed., Animal Cell Culture, 1987.
Goyal, Anil et al. “Characteristics oif Funal Cellulases,” Bioresource Technol. 36:37-50, 1991.
Halldorsdottir, S et al., “Cloning, sequencing and overexpression of aRhodothermus marinusgene coding a thermostable cellulase of glycosyl hydrolase family 12,” Appl Microbiol Biotechnol. 49(3):277-84, 1998.
Hemmpel, W.H., “The surface modificationof woven and knitted cellulose fibre fabrics by enzymatic degradation,” ITB Dyeing/Printing/Finishing 3:5-14, 1991.
Henrissant, Bernard et al., “New families in the classification of glycosyl hydrolases based on amino acid sequence similarities,” Biochem. L. 293:781-788, 1993.
Herr, D. et al., “Purification and Properties of an Extracellular β-Glucosidase fromLenzites trabea,” European Appl. Microbiol. Biotechnol. 5:29-36, 1978.
Hu, Qianjin et al., “Antibodies Specific for the Human Retinoblastoma Protein Identify a Family of Related Polypeptides,” Mol Cell Biol. vol. 11, No. 11, pp. 5792-5799, 1991.
Ilmen, Marja et al., “Regulation of Cellulase Gene Expression in the Filamentous FungusTrichoderma reesei,” Appl. and Envir. Micro., vol. 63, No. 4, pp. 1298-1306, 1997.
Jakobovits, Aya, et al., Production of Antigen-Specific Human Antibodies from Mice Engineered with Human Heavy and Light Chain YACsaAnnals New York Academy of Sciences, 764:525-535, 1995.
Jakobovits, Aya, “Production of fully human antibodies by transgenic mice,” Curr Opin Biotechnol 6(5):561-6, 1995.
Jones, Peter et al., “Replacing the complementarity—determining region sin a human antibody with thos from a mouse,” Nature 321:522-525, 1986.
Kawaguchi, Takashi et al., “Cloning and sequencing of the cDNA encoding β-glucosidase 1 fromAspergillus aculeatus,” Gene 173(2):287-8, 1996.
Knowles, Jonathan et al., TIBTECH 5, 255-261, 1987.
Kohler, G. et al., “Continuous cultures of fused cells secreting antibody of predefined specificity,”Nature, vol. 256, pp. 495-499, Aug. 7, 1975.
Krishna, S. Hari et al., “Simultaneous saccharification and fermentation of lignocellulosic wastes to ethanol using a thermotolerant yeast,” Bioresource Tech. 77:193-196, 2001.
Kumar, Akhil., “Optimizing the Use of Cellulase Enzymes in Finishing Cellulosic Fabrics,” Textile Chemist and Colorist, 29:37-42, 1997.
Lehtio, Janne. et al., FEMS Microbiology Letters 195:197-204, 2001.
Li, Xin-Liang et al. “Expression ofAureobasidium pullulans xynAin, and Secretion of the Xylanase from,Saccharomyces cerevisiae,” Appl. Environ. Microbiol. 62, No. 1, pp. 209-213, 1996.
Linder, Marcus et al., “The roles and function of cellulose-binding domains,” Journal of Biotechnol. 57:15-28, 1997.
Liukkonen, Pere J., et al., “Use of Purified Enzymes in Mechanical Pulping,” 1996 Tappi Pulping Conference, pp. 693-696, Nashville, TN.
Loftus, Joseph C. et al. “A β3Integrin Mutation Abolishes Ligand Binding and Alters Divalent Cation-Dependent Conformation,” Science, vol. 245, pp. 915-921, Aug. 24, 1990.
Medve, Jozsef et al., “Ion-exchange chromatoraphic purification and quantitative analysis ofTrichoderma reeseicellulases cellobiohydrolase I, II and endoglucanase II by fast protein liquid chromatography,” J. Chromatography A 808:153-165, 1998.
Nielsen, Henrik et al. “Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites,” Protein Engineering, vol. 10, No. 1, pp. 1-6, 1997.
Ohmiya, Kun

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