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Volumn 13, Issue , 2013, Pages

Systematic screening of glycosylation- and trafficking-associated gene knockouts in Saccharomyces cerevisiae identifies mutants with improved heterologous exocellulase activity and host secretion

Author keywords

Cellulase production; Glycosylation; Protein secretion

Indexed keywords

CELLULASE PRODUCTION; CONSOLIDATED BIO-PROCESSING; EXTRACELLULAR ACTIVITY; EXTRACELLULAR CELLULASE; HETEROLOGOUS PROTEINS; PHANEROCHAETE CHRYSOSPORIUM; PROTEIN SECRETION; SITE DIRECTED MUTAGENESIS;

EID: 84883271760     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-13-71     Document Type: Article
Times cited : (31)

References (73)
  • 1
    • 34249935490 scopus 로고    scopus 로고
    • Genetic engineering approaches to improve bioethanol production from maize
    • 10.1016/j.copbio.2007.03.006, 17399975
    • Torney F, Moeller L, Scarpa A, Wang K. Genetic engineering approaches to improve bioethanol production from maize. Current opinion in biotechnology 2007, 18(3):193-199. 10.1016/j.copbio.2007.03.006, 17399975.
    • (2007) Current opinion in biotechnology , vol.18 , Issue.3 , pp. 193-199
    • Torney, F.1    Moeller, L.2    Scarpa, A.3    Wang, K.4
  • 4
    • 34548710320 scopus 로고    scopus 로고
    • Consolidated bioprocessing for bioethanol production using Saccharomyces cerevisiae
    • 10.1007/10_2007_061, 17846725
    • van Zyl WH, Lynd LR, den Haan R, McBride JE. Consolidated bioprocessing for bioethanol production using Saccharomyces cerevisiae. Advances in biochemical engineering/biotechnology 2007, 108:205-235. 10.1007/10_2007_061, 17846725.
    • (2007) Advances in biochemical engineering/biotechnology , vol.108 , pp. 205-235
    • van Zyl, W.H.1    Lynd, L.R.2    den Haan, R.3    McBride, J.E.4
  • 5
    • 0032559366 scopus 로고    scopus 로고
    • Secretion, purification and activity of two recombinant pepper endo-beta-1,4-glucanases expressed in the yeast Pichia pastoris
    • 10.1016/S0014-5793(97)01592-5, 9475162
    • Ferrarese L, Trainotti L, Gattolin S, Casadoro G. Secretion, purification and activity of two recombinant pepper endo-beta-1,4-glucanases expressed in the yeast Pichia pastoris. FEBS Lett 1998, 422(1):23-26. 10.1016/S0014-5793(97)01592-5, 9475162.
    • (1998) FEBS Lett , vol.422 , Issue.1 , pp. 23-26
    • Ferrarese, L.1    Trainotti, L.2    Gattolin, S.3    Casadoro, G.4
  • 6
    • 84862799491 scopus 로고    scopus 로고
    • A comparative study of beta-1, 4-endoglucanase (possessing beta-1, 4-exoglucanase activity) from Bacillus subtilis LH expressed in Pichia pastoris GS115 and Escherichia coli Rosetta (DE3)
    • Zhao XH, Wang W, Wang FQ, Wei DZ. A comparative study of beta-1, 4-endoglucanase (possessing beta-1, 4-exoglucanase activity) from Bacillus subtilis LH expressed in Pichia pastoris GS115 and Escherichia coli Rosetta (DE3). Bioresour Technol 2012, 110:539-545.
    • (2012) Bioresour Technol , vol.110 , pp. 539-545
    • Zhao, X.H.1    Wang, W.2    Wang, F.Q.3    Wei, D.Z.4
  • 8
    • 38549088955 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum (BCC18080) in Pichia pastoris
    • 10.1016/j.pep.2007.10.022, 18083533
    • Wonganu B, Pootanakit K, Boonyapakron K, Champreda V, Tanapongpipat S, Eurwilaichitr L. Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum (BCC18080) in Pichia pastoris. Protein Expr Purif 2008, 58(1):78-86. 10.1016/j.pep.2007.10.022, 18083533.
    • (2008) Protein Expr Purif , vol.58 , Issue.1 , pp. 78-86
    • Wonganu, B.1    Pootanakit, K.2    Boonyapakron, K.3    Champreda, V.4    Tanapongpipat, S.5    Eurwilaichitr, L.6
  • 9
    • 45449118076 scopus 로고    scopus 로고
    • An acidic and thermostable carboxymethyl cellulase from the yeast Cryptococcus sp. S-2: purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris
    • 10.1016/j.pep.2008.03.021, 18479937
    • Thongekkaew J, Ikeda H, Masaki K, Iefuji H. An acidic and thermostable carboxymethyl cellulase from the yeast Cryptococcus sp. S-2: purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris. Protein Expr Purif 2008, 60(2):140-146. 10.1016/j.pep.2008.03.021, 18479937.
    • (2008) Protein Expr Purif , vol.60 , Issue.2 , pp. 140-146
    • Thongekkaew, J.1    Ikeda, H.2    Masaki, K.3    Iefuji, H.4
  • 10
    • 84857628113 scopus 로고    scopus 로고
    • Cloning and bioinformatics analysis of an endoglucanase gene (Aucel12A) from Aspergillus usamii and its functional expression in Pichia pastoris
    • 10.1007/s10295-011-1039-z, 21935697
    • Shi H, Yin X, Wu M, Tang C, Zhang H, Li J. Cloning and bioinformatics analysis of an endoglucanase gene (Aucel12A) from Aspergillus usamii and its functional expression in Pichia pastoris. J Ind Microbiol Biotechnol 2012, 39(2):347-357. 10.1007/s10295-011-1039-z, 21935697.
    • (2012) J Ind Microbiol Biotechnol , vol.39 , Issue.2 , pp. 347-357
    • Shi, H.1    Yin, X.2    Wu, M.3    Tang, C.4    Zhang, H.5    Li, J.6
  • 11
    • 84863330386 scopus 로고    scopus 로고
    • Characterization of Trichoderma reesei endoglucanase II expressed heterologously in Pichia pastoris for better biofinishing and biostoning
    • 10.1007/s12275-012-1207-5, 22752917
    • Samanta S, Basu A, Halder UC, Sen SK. Characterization of Trichoderma reesei endoglucanase II expressed heterologously in Pichia pastoris for better biofinishing and biostoning. J Microbiol 2012, 50(3):518-525. 10.1007/s12275-012-1207-5, 22752917.
    • (2012) J Microbiol , vol.50 , Issue.3 , pp. 518-525
    • Samanta, S.1    Basu, A.2    Halder, U.C.3    Sen, S.K.4
  • 12
    • 0034771917 scopus 로고    scopus 로고
    • Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-beta-glucanase heterologously expressed in Pichia pastoris
    • 10.1104/pp.010269, 125102, 11598241
    • Molhoj M, Ulvskov P, Dal Degan F. Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-beta-glucanase heterologously expressed in Pichia pastoris. Plant Physiol 2001, 127(2):674-684. 10.1104/pp.010269, 125102, 11598241.
    • (2001) Plant Physiol , vol.127 , Issue.2 , pp. 674-684
    • Molhoj, M.1    Ulvskov, P.2    Dal Degan, F.3
  • 13
    • 79952622189 scopus 로고    scopus 로고
    • Production and characterization of Acidothermus cellulolyticus endoglucanase in Pichia pastoris
    • 10.1016/j.pep.2011.01.006, 21262363
    • Lindenmuth BE, McDonald KA. Production and characterization of Acidothermus cellulolyticus endoglucanase in Pichia pastoris. Protein Expr Purif 2011, 77(2):153-158. 10.1016/j.pep.2011.01.006, 21262363.
    • (2011) Protein Expr Purif , vol.77 , Issue.2 , pp. 153-158
    • Lindenmuth, B.E.1    McDonald, K.A.2
  • 14
    • 79954720385 scopus 로고    scopus 로고
    • Cloning and optimized expression of a neutral endoglucanase gene (ncel5A) from Volvariella volvacea WX32 in Pichia pastoris
    • 10.1016/j.jbiosc.2011.01.002, 21367655
    • Li J, Tang C, Shi H, Wu M. Cloning and optimized expression of a neutral endoglucanase gene (ncel5A) from Volvariella volvacea WX32 in Pichia pastoris. J Biosci Bioeng 2011, 111(5):537-540. 10.1016/j.jbiosc.2011.01.002, 21367655.
    • (2011) J Biosci Bioeng , vol.111 , Issue.5 , pp. 537-540
    • Li, J.1    Tang, C.2    Shi, H.3    Wu, M.4
  • 16
    • 84930478737 scopus 로고    scopus 로고
    • Recombinant expression and characterization of an endoglucanase III (cel12a) from Trichoderma harzianum (Hypocreaceae) in the yeast Pichia pastoris
    • 10.4238/2012.May.21.11, 22653604
    • Generoso WC, Malago-Jr W, Pereira N, Henrique-Silva F. Recombinant expression and characterization of an endoglucanase III (cel12a) from Trichoderma harzianum (Hypocreaceae) in the yeast Pichia pastoris. Genet Mol Res 2012, 11(2):1544-1557. 10.4238/2012.May.21.11, 22653604.
    • (2012) Genet Mol Res , vol.11 , Issue.2 , pp. 1544-1557
    • Generoso, W.C.1    Malago-Jr, W.2    Pereira, N.3    Henrique-Silva, F.4
  • 17
    • 33747199934 scopus 로고    scopus 로고
    • Arabidopsis thaliana beta-Glucosidases BGLU45 and BGLU46 hydrolyse monolignol glucosides
    • 10.1016/j.phytochem.2006.05.022, 16814332
    • Escamilla-Trevino LL, Chen W, Card ML, Shih MC, Cheng CL, Poulton JE. Arabidopsis thaliana beta-Glucosidases BGLU45 and BGLU46 hydrolyse monolignol glucosides. Phytochemistry 2006, 67(15):1651-1660. 10.1016/j.phytochem.2006.05.022, 16814332.
    • (2006) Phytochemistry , vol.67 , Issue.15 , pp. 1651-1660
    • Escamilla-Trevino, L.L.1    Chen, W.2    Card, M.L.3    Shih, M.C.4    Cheng, C.L.5    Poulton, J.E.6
  • 19
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • 10.1111/j.1574-6976.2008.00106.x, 18371173
    • Baldrian P, Valaskova V. Degradation of cellulose by basidiomycetous fungi. FEMS microbiology reviews 2008, 32(3):501-521. 10.1111/j.1574-6976.2008.00106.x, 18371173.
    • (2008) FEMS microbiology reviews , vol.32 , Issue.3 , pp. 501-521
    • Baldrian, P.1    Valaskova, V.2
  • 20
    • 77449097393 scopus 로고    scopus 로고
    • Cellulolytic systems in insects
    • 10.1146/annurev-ento-112408-085319, 19754245
    • Watanabe H, Tokuda G. Cellulolytic systems in insects. Annu Rev Entomol 2010, 55:609-632. 10.1146/annurev-ento-112408-085319, 19754245.
    • (2010) Annu Rev Entomol , vol.55 , pp. 609-632
    • Watanabe, H.1    Tokuda, G.2
  • 21
    • 80051657017 scopus 로고    scopus 로고
    • Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses
    • 10.1186/1754-6834-4-24, 3177772, 21849025
    • Wang TY, Chen HL, Lu MY, Chen YC, Sung HM, Mao CT, Cho HY, Ke HM, Hwa TY, Ruan SK, et al. Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses. Biotechnology for biofuels 2011, 4(1):24. 10.1186/1754-6834-4-24, 3177772, 21849025.
    • (2011) Biotechnology for biofuels , vol.4 , Issue.1 , pp. 24
    • Wang, T.Y.1    Chen, H.L.2    Lu, M.Y.3    Chen, Y.C.4    Sung, H.M.5    Mao, C.T.6    Cho, H.Y.7    Ke, H.M.8    Hwa, T.Y.9    Ruan, S.K.10
  • 22
    • 80055041446 scopus 로고    scopus 로고
    • Cloning, expression, purification, and properties of an endoglucanase gene (glycosyl hydrolase family 12) from Aspergillus niger VTCC-F021 in Pichia pastoris
    • 10.4014/jmb.1104.04030, 22031024
    • Pham TH, Quyen DT, Nghiem NM, Vu TD. Cloning, expression, purification, and properties of an endoglucanase gene (glycosyl hydrolase family 12) from Aspergillus niger VTCC-F021 in Pichia pastoris. J Microbiol Biotechnol 2011, 21(10):1012-1020. 10.4014/jmb.1104.04030, 22031024.
    • (2011) J Microbiol Biotechnol , vol.21 , Issue.10 , pp. 1012-1020
    • Pham, T.H.1    Quyen, D.T.2    Nghiem, N.M.3    Vu, T.D.4
  • 23
    • 0029660840 scopus 로고    scopus 로고
    • Trichoderma: a review of biology and systematics of the genus
    • Gary JS. Trichoderma: a review of biology and systematics of the genus. Mycol Res 1996, 100(8):923-935.
    • (1996) Mycol Res , vol.100 , Issue.8 , pp. 923-935
    • Gary, J.S.1
  • 25
    • 0021004837 scopus 로고
    • Trichoderma reesei cellulases
    • Montenecourt BS. Trichoderma reesei cellulases. Trends Biotechnol 1983, 1(5):156-161.
    • (1983) Trends Biotechnol , vol.1 , Issue.5 , pp. 156-161
    • Montenecourt, B.S.1
  • 26
    • 0031776810 scopus 로고    scopus 로고
    • The cellobiohydrolases of Trichoderma reesei: a review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis
    • Sinnott ML. The cellobiohydrolases of Trichoderma reesei: a review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis. Biochem Soc Trans 1998, 26(2):160-164.
    • (1998) Biochem Soc Trans , vol.26 , Issue.2 , pp. 160-164
    • Sinnott, M.L.1
  • 28
    • 0029833985 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mutants selected for increased production of Trichoderma reesei cellulases
    • 10.1007/s002530050780, 8987533
    • Aho S, Arffman A, Korhola M. Saccharomyces cerevisiae mutants selected for increased production of Trichoderma reesei cellulases. Appl Microbiol Biotechnol 1996, 46(1):36-45. 10.1007/s002530050780, 8987533.
    • (1996) Appl Microbiol Biotechnol , vol.46 , Issue.1 , pp. 36-45
    • Aho, S.1    Arffman, A.2    Korhola, M.3
  • 29
    • 38349128431 scopus 로고    scopus 로고
    • Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability
    • 10.1016/j.pep.2007.09.004, 17942322
    • Qin Y, Wei X, Liu X, Wang T, Qu Y. Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability. Protein Expr Purif 2008, 58(1):162-167. 10.1016/j.pep.2007.09.004, 17942322.
    • (2008) Protein Expr Purif , vol.58 , Issue.1 , pp. 162-167
    • Qin, Y.1    Wei, X.2    Liu, X.3    Wang, T.4    Qu, Y.5
  • 30
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • 10.1038/nrmicro1087, 15685223
    • Wildt S, Gerngross TU. The humanization of N-glycosylation pathways in yeast. Nat Rev Microbiol 2005, 3(2):119-128. 10.1038/nrmicro1087, 15685223.
    • (2005) Nat Rev Microbiol , vol.3 , Issue.2 , pp. 119-128
    • Wildt, S.1    Gerngross, T.U.2
  • 31
    • 41549143301 scopus 로고    scopus 로고
    • Yeast glycobiology and its application
    • 10.1271/bbb.70725, 18323647
    • Jigami Y. Yeast glycobiology and its application. Biosci Biotechnol Biochem 2008, 72(3):637-648. 10.1271/bbb.70725, 18323647.
    • (2008) Biosci Biotechnol Biochem , vol.72 , Issue.3 , pp. 637-648
    • Jigami, Y.1
  • 32
    • 47049095366 scopus 로고    scopus 로고
    • Implications of cellobiohydrolase glycosylation for use in biomass conversion
    • 10.1186/1754-6834-1-10, 2427024, 18471276
    • Jeoh T, Michener W, Himmel ME, Decker SR, Adney WS. Implications of cellobiohydrolase glycosylation for use in biomass conversion. Biotechnology for biofuels 2008, 1(1):10. 10.1186/1754-6834-1-10, 2427024, 18471276.
    • (2008) Biotechnology for biofuels , vol.1 , Issue.1 , pp. 10
    • Jeoh, T.1    Michener, W.2    Himmel, M.E.3    Decker, S.R.4    Adney, W.S.5
  • 33
    • 0033020387 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure
    • 91352, 10347017
    • Kruszewska JS, Butterweck AH, Kurzatkowski W, Migdalski A, Kubicek CP, Palamarczyk G. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure. Appl Environ Microbiol 1999, 65(6):2382-2387. 91352, 10347017.
    • (1999) Appl Environ Microbiol , vol.65 , Issue.6 , pp. 2382-2387
    • Kruszewska, J.S.1    Butterweck, A.H.2    Kurzatkowski, W.3    Migdalski, A.4    Kubicek, C.P.5    Palamarczyk, G.6
  • 34
    • 0036714783 scopus 로고    scopus 로고
    • Microbial cellulose utilization: fundamentals and biotechnology
    • table of contents, 10.1128/MMBR.66.3.506-577.2002, 120791, 12209002
    • Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS. Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol Rev 2002, 66(3):506-577. table of contents, 10.1128/MMBR.66.3.506-577.2002, 120791, 12209002.
    • (2002) Microbiol Mol Biol Rev , vol.66 , Issue.3 , pp. 506-577
    • Lynd, L.R.1    Weimer, P.J.2    van Zyl, W.H.3    Pretorius, I.S.4
  • 35
    • 0032518904 scopus 로고    scopus 로고
    • Engineering yeast for efficient cellulose degradation
    • 10.1002/(SICI)1097-0061(19980115)14:1<67::AID-YEA200>3.0.CO;2-T, 9483796
    • Van Rensburg P, Van Zyl WH, Pretorius IS. Engineering yeast for efficient cellulose degradation. Yeast 1998, 14(1):67-76. 10.1002/(SICI)1097-0061(19980115)14:1<67::AID-YEA200>3.0.CO;2-T, 9483796.
    • (1998) Yeast , vol.14 , Issue.1 , pp. 67-76
    • Van Rensburg, P.1    Van Zyl, W.H.2    Pretorius, I.S.3
  • 36
    • 79953223700 scopus 로고    scopus 로고
    • Cellobiohydrolase hydrolyzes crystalline cellulose on hydrophobic faces
    • 10.1074/jbc.M110.216556, 3064174, 21282110
    • Liu YS, Baker JO, Zeng Y, Himmel ME, Haas T, Ding SY. Cellobiohydrolase hydrolyzes crystalline cellulose on hydrophobic faces. J Biol Chem 2011, 286(13):11195-11201. 10.1074/jbc.M110.216556, 3064174, 21282110.
    • (2011) J Biol Chem , vol.286 , Issue.13 , pp. 11195-11201
    • Liu, Y.S.1    Baker, J.O.2    Zeng, Y.3    Himmel, M.E.4    Haas, T.5    Ding, S.Y.6
  • 38
    • 0029913706 scopus 로고    scopus 로고
    • Lignocellulose degradation by Phanerochaete chrysosporium: gene families and gene expression for a complex process
    • 10.1046/j.1365-2958.1996.474966.x, 8830273
    • Broda P, Birch PR, Brooks PR, Sims PF. Lignocellulose degradation by Phanerochaete chrysosporium: gene families and gene expression for a complex process. Mol Microbiol 1996, 19(5):923-932. 10.1046/j.1365-2958.1996.474966.x, 8830273.
    • (1996) Mol Microbiol , vol.19 , Issue.5 , pp. 923-932
    • Broda, P.1    Birch, P.R.2    Brooks, P.R.3    Sims, P.F.4
  • 39
    • 33646123079 scopus 로고    scopus 로고
    • Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identification of peptides in ligninolytic cultures reveal complex mixtures of secreted proteins
    • 10.1016/j.fgb.2006.01.003, 16524749
    • Vanden Wymelenberg A, Minges P, Sabat G, Martinez D, Aerts A, Salamov A, Grigoriev I, Shapiro H, Putnam N, Belinky P, et al. Computational analysis of the Phanerochaete chrysosporium v2.0 genome database and mass spectrometry identification of peptides in ligninolytic cultures reveal complex mixtures of secreted proteins. Fungal Genet Biol 2006, 43(5):343-356. 10.1016/j.fgb.2006.01.003, 16524749.
    • (2006) Fungal Genet Biol , vol.43 , Issue.5 , pp. 343-356
    • Vanden Wymelenberg, A.1    Minges, P.2    Sabat, G.3    Martinez, D.4    Aerts, A.5    Salamov, A.6    Grigoriev, I.7    Shapiro, H.8    Putnam, N.9    Belinky, P.10
  • 41
    • 67349249841 scopus 로고    scopus 로고
    • The first genome-level transcriptome of the wood-degrading fungus Phanerochaete chrysosporium grown on red oak
    • 10.1007/s00294-009-0243-0, 19396602
    • Sato S, Feltus FA, Iyer P, Tien M. The first genome-level transcriptome of the wood-degrading fungus Phanerochaete chrysosporium grown on red oak. Curr Genet 2009, 55(3):273-286. 10.1007/s00294-009-0243-0, 19396602.
    • (2009) Curr Genet , vol.55 , Issue.3 , pp. 273-286
    • Sato, S.1    Feltus, F.A.2    Iyer, P.3    Tien, M.4
  • 42
    • 0031805826 scopus 로고    scopus 로고
    • Phanerochaete chrysosporium cellobiohydrolase and cellobiose dehydrogenase transcripts in wood
    • 106252, 9572973
    • Vallim MA, Janse BJ, Gaskell J, Pizzirani-Kleiner AA, Cullen D. Phanerochaete chrysosporium cellobiohydrolase and cellobiose dehydrogenase transcripts in wood. Appl Environ Microbiol 1998, 64(5):1924-1928. 106252, 9572973.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.5 , pp. 1924-1928
    • Vallim, M.A.1    Janse, B.J.2    Gaskell, J.3    Pizzirani-Kleiner, A.A.4    Cullen, D.5
  • 44
    • 79957616856 scopus 로고    scopus 로고
    • Heterologous expression of endo-1,4-beta-xylanaseC from Phanerochaete chrysosporium in Pichia pastoris
    • 10.1016/j.jbiosc.2011.02.010, 21393056
    • Huy ND, Kim SW, Park SM. Heterologous expression of endo-1,4-beta-xylanaseC from Phanerochaete chrysosporium in Pichia pastoris. J Biosci Bioeng 2011, 111(6):654-657. 10.1016/j.jbiosc.2011.02.010, 21393056.
    • (2011) J Biosci Bioeng , vol.111 , Issue.6 , pp. 654-657
    • Huy, N.D.1    Kim, S.W.2    Park, S.M.3
  • 45
    • 0035861979 scopus 로고    scopus 로고
    • Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes
    • 10.1006/jmbi.2000.5180, 11743726
    • Munoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, Stahlberg J. Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes. Journal of molecular biology 2001, 314(5):1097-1111. 10.1006/jmbi.2000.5180, 11743726.
    • (2001) Journal of molecular biology , vol.314 , Issue.5 , pp. 1097-1111
    • Munoz, I.G.1    Ubhayasekera, W.2    Henriksson, H.3    Szabo, I.4    Pettersson, G.5    Johansson, G.6    Mowbray, S.L.7    Stahlberg, J.8
  • 46
    • 0036841854 scopus 로고    scopus 로고
    • Transcript analysis of genes encoding a family 61 endoglucanase and a putative membrane-anchored family 9 glycosyl hydrolase from Phanerochaete chrysosporium
    • 10.1128/AEM.68.11.5765-5768.2002, 129927, 12406778
    • Wymelenberg AV, Denman S, Dietrich D, Bassett J, Yu X, Atalla R, Predki P, Rudsander U, Teeri TT, Cullen D. Transcript analysis of genes encoding a family 61 endoglucanase and a putative membrane-anchored family 9 glycosyl hydrolase from Phanerochaete chrysosporium. Appl Environ Microbiol 2002, 68(11):5765-5768. 10.1128/AEM.68.11.5765-5768.2002, 129927, 12406778.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.11 , pp. 5765-5768
    • Wymelenberg, A.V.1    Denman, S.2    Dietrich, D.3    Bassett, J.4    Yu, X.5    Atalla, R.6    Predki, P.7    Rudsander, U.8    Teeri, T.T.9    Cullen, D.10
  • 48
    • 84855232037 scopus 로고    scopus 로고
    • Deglycosylation of cellulosomal enzyme enhances cellulosome assembly in Saccharomyces cerevisiae
    • 10.1016/j.jbiotec.2011.11.015, 22154562
    • Suzuki H, Imaeda T, Kitagawa T, Kohda K. Deglycosylation of cellulosomal enzyme enhances cellulosome assembly in Saccharomyces cerevisiae. J Biotechnol 2012, 157(1):64-70. 10.1016/j.jbiotec.2011.11.015, 22154562.
    • (2012) J Biotechnol , vol.157 , Issue.1 , pp. 64-70
    • Suzuki, H.1    Imaeda, T.2    Kitagawa, T.3    Kohda, K.4
  • 49
    • 84863629890 scopus 로고    scopus 로고
    • Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae
    • 10.1111/j.1567-1364.2012.00810.x, 22533807
    • Hou J, Tyo KEJ, Liu ZH, Petranovic D, Nielsen J. Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae. FEMS Yeast Res 2012, 12(5):491-510. 10.1111/j.1567-1364.2012.00810.x, 22533807.
    • (2012) FEMS Yeast Res , vol.12 , Issue.5 , pp. 491-510
    • Hou, J.1    Tyo, K.E.J.2    Liu, Z.H.3    Petranovic, D.4    Nielsen, J.5
  • 50
    • 77249147339 scopus 로고    scopus 로고
    • Engineering of protein secretion in yeast: strategies and impact on protein production
    • 10.1007/s00253-010-2447-0, 20140428
    • Idiris A, Tohda H, Kumagai H, Takegawa K. Engineering of protein secretion in yeast: strategies and impact on protein production. Appl Microbiol Biotechnol 2010, 86(2):403-417. 10.1007/s00253-010-2447-0, 20140428.
    • (2010) Appl Microbiol Biotechnol , vol.86 , Issue.2 , pp. 403-417
    • Idiris, A.1    Tohda, H.2    Kumagai, H.3    Takegawa, K.4
  • 52
    • 78651491150 scopus 로고    scopus 로고
    • Identification of genes that enhance cellulase protein production in yeast
    • 10.1016/j.jbiotec.2010.12.002, 21167225
    • Kitagawa T, Kohda K, Tokuhiro K, Hoshida H, Akada R, Takahashi H, Lmaeda T. Identification of genes that enhance cellulase protein production in yeast. J Biotechnol 2011, 151(2):194-203. 10.1016/j.jbiotec.2010.12.002, 21167225.
    • (2011) J Biotechnol , vol.151 , Issue.2 , pp. 194-203
    • Kitagawa, T.1    Kohda, K.2    Tokuhiro, K.3    Hoshida, H.4    Akada, R.5    Takahashi, H.6    Lmaeda, T.7
  • 53
    • 4344717009 scopus 로고    scopus 로고
    • Disruption of the MNN10 gene enhances protein secretion in Kluyveromyces lactis and Saccharomyces cerevisiae
    • 10.1016/j.femsyr.2004.03.001, 15450190
    • Bartkeviciute D, Sasnauskas K. Disruption of the MNN10 gene enhances protein secretion in Kluyveromyces lactis and Saccharomyces cerevisiae. FEMS Yeast Res 2004, 4(8):833-840. 10.1016/j.femsyr.2004.03.001, 15450190.
    • (2004) FEMS Yeast Res , vol.4 , Issue.8 , pp. 833-840
    • Bartkeviciute, D.1    Sasnauskas, K.2
  • 56
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • 10.1146/annurev.biochem.73.011303.073752, 15189166
    • Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 2004, 73:1019-1049. 10.1146/annurev.biochem.73.011303.073752, 15189166.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 57
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases
    • 10.1002/anie.200601645, 17024709
    • Lehle L, Strahl S, Tanner W. Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew Chem Int Ed Engl 2006, 45(41):6802-6818. 10.1002/anie.200601645, 17024709.
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.41 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 59
    • 0020049833 scopus 로고
    • Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation
    • Huffaker TC, Robbins PW. Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J Biol Chem 1982, 257(6):3203-3210.
    • (1982) J Biol Chem , vol.257 , Issue.6 , pp. 3203-3210
    • Huffaker, T.C.1    Robbins, P.W.2
  • 60
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics A, Orlean P. Glycoprotein biosynthesis in yeast. FASEB J 1993, 7(6):540-550.
    • (1993) FASEB J , vol.7 , Issue.6 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 61
    • 70149116132 scopus 로고    scopus 로고
    • Genome-wide identification of Saccharomyces cerevisiae genes required for maximal tolerance to ethanol
    • 10.1128/AEM.00845-09, 2747848, 19633105
    • Teixeira MC, Raposo LR, Mira NP, Lourenco AB, Sa-Correia I. Genome-wide identification of Saccharomyces cerevisiae genes required for maximal tolerance to ethanol. Appl Environ Microbiol 2009, 75(18):5761-5772. 10.1128/AEM.00845-09, 2747848, 19633105.
    • (2009) Appl Environ Microbiol , vol.75 , Issue.18 , pp. 5761-5772
    • Teixeira, M.C.1    Raposo, L.R.2    Mira, N.P.3    Lourenco, A.B.4    Sa-Correia, I.5
  • 62
    • 1642505521 scopus 로고    scopus 로고
    • O-glycosylation as a sorting determinant for cell surface delivery in yeast
    • 10.1091/mbc.E03-07-0511, 379253, 14742720
    • Proszynski TJ, Simons K, Bagnat M. O-glycosylation as a sorting determinant for cell surface delivery in yeast. Mol Biol Cell 2004, 15(4):1533-1543. 10.1091/mbc.E03-07-0511, 379253, 14742720.
    • (2004) Mol Biol Cell , vol.15 , Issue.4 , pp. 1533-1543
    • Proszynski, T.J.1    Simons, K.2    Bagnat, M.3
  • 63
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital
    • 452322, 8918452
    • Gentzsch M, Tanner W. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J 1996, 15(21):5752-5759. 452322, 8918452.
    • (1996) EMBO J , vol.15 , Issue.21 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 65
    • 0343981695 scopus 로고
    • Preparation and characterization of mRNA from ligninolytic fungi
    • Haylock R, Broda P. Preparation and characterization of mRNA from ligninolytic fungi. Methods Enzymol 1988, 161:221-228.
    • (1988) Methods Enzymol , vol.161 , pp. 221-228
    • Haylock, R.1    Broda, P.2
  • 66
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Kohrer K, Domdey H. Preparation of high molecular weight RNA. Methods Enzymol 1991, 194:398-405.
    • (1991) Methods Enzymol , vol.194 , pp. 398-405
    • Kohrer, K.1    Domdey, H.2
  • 67
    • 0036087525 scopus 로고    scopus 로고
    • High-throughput screening of soluble recombinant proteins
    • 2373646, 12070324
    • Shih YP, Kung WM, Chen JC, Yeh CH, Wang AH, Wang TF. High-throughput screening of soluble recombinant proteins. Protein Sci 2002, 11(7):1714-1719. 2373646, 12070324.
    • (2002) Protein Sci , vol.11 , Issue.7 , pp. 1714-1719
    • Shih, Y.P.1    Kung, W.M.2    Chen, J.C.3    Yeh, C.H.4    Wang, A.H.5    Wang, T.F.6
  • 68
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • 10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2, 9483801
    • Brachmann CB, Davies A, Cost GJ, Caputo E, Li J, Hieter P, Boeke JD. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 1998, 14(2):115-132. 10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2, 9483801.
    • (1998) Yeast , vol.14 , Issue.2 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 69
    • 0025963054 scopus 로고
    • Putting the HO gene to work: practical uses for mating-type switching
    • Herskowitz I, Jensen RE. Putting the HO gene to work: practical uses for mating-type switching. Methods Enzymol 1991, 194:132-146.
    • (1991) Methods Enzymol , vol.194 , pp. 132-146
    • Herskowitz, I.1    Jensen, R.E.2
  • 70
    • 33644792045 scopus 로고    scopus 로고
    • Yeast transformation by the LiAc/SS Carrier DNA/PEG method
    • Gietz RD, Woods RA. Yeast transformation by the LiAc/SS Carrier DNA/PEG method. Methods Mol Biol 2006, 313:107-120.
    • (2006) Methods Mol Biol , vol.313 , pp. 107-120
    • Gietz, R.D.1    Woods, R.A.2
  • 71
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: the proteomics server for in-depth protein knowledge and analysis
    • 10.1093/nar/gkg563, 168970, 12824418
    • Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 2003, 31(13):3784-3788. 10.1093/nar/gkg563, 168970, 12824418.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 72
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • 10.1093/bioinformatics/bti770, 16301204
    • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22(2):195-201. 10.1093/bioinformatics/bti770, 16301204.
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 73
    • 17444404534 scopus 로고    scopus 로고
    • Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors
    • 10.1111/j.1742-4658.2005.04625.x, 15819888
    • Ubhayasekera W, Munoz IG, Vasella A, Stahlberg J, Mowbray SL. Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors. FEBS J 2005, 272(8):1952-1964. 10.1111/j.1742-4658.2005.04625.x, 15819888.
    • (2005) FEBS J , vol.272 , Issue.8 , pp. 1952-1964
    • Ubhayasekera, W.1    Munoz, I.G.2    Vasella, A.3    Stahlberg, J.4    Mowbray, S.L.5


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