메뉴 건너뛰기




Volumn 49, Issue 1-3, 1996, Pages 211-218

Cloning and characterization of the gene for the thermostable xylanase XynA from Thermomyces lanuginosus

Author keywords

Fusion protein; Thermomyces lanuginosus; Xylanase

Indexed keywords

AMINO ACIDS; COLIFORM BACTERIA; DNA SEQUENCES; ELECTROPHORESIS; ENZYMES; FUNGI; GENES; POLYPEPTIDES; PURIFICATION;

EID: 0030595046     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/0168-1656(96)01516-7     Document Type: Article
Times cited : (73)

References (40)
  • 1
    • 0023544693 scopus 로고
    • Isolation of RNA using guanidinium salts
    • Abelson, J.N. and Simon, M.I. (1987) Isolation of RNA using guanidinium salts. Methods Enzymol. 152, 219-227.
    • (1987) Methods Enzymol. , vol.152 , pp. 219-227
    • Abelson, J.N.1    Simon, M.I.2
  • 2
    • 0025091982 scopus 로고
    • Purification and properties of a xylanase from the thermophilic fungus, Humicola lanuginosa (Griffon and Maublanc) Bunce
    • Anand, L., Krishnamurthgy, S. and Vithayathil, P.J. (1990) Purification and properties of a xylanase from the thermophilic fungus, Humicola lanuginosa (Griffon and Maublanc) Bunce. Arch. Biochem. Biophys. 276, 546-553.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 546-553
    • Anand, L.1    Krishnamurthgy, S.2    Vithayathil, P.J.3
  • 3
    • 0027631061 scopus 로고
    • Cloning and targeted gene disruption of xyl1, a beta-1,4-xylanase gene from the maize pathogen Cochliobolus carbonum
    • Apel, P.C., Panaccione, D.G., Holden, F.R. and Walton, J.D. (1993) Cloning and targeted gene disruption of xyl1, a beta-1,4-xylanase gene from the maize pathogen Cochliobolus carbonum. Mol. Plant-Microbe Interact. 6, 467-473.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 467-473
    • Apel, P.C.1    Panaccione, D.G.2    Holden, F.R.3    Walton, J.D.4
  • 6
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey, M.J., Biely, P. and Poutanen, K. (1992) Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 23, 257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 7
    • 0022946198 scopus 로고
    • Sequences important for gene expression in filamentous fungi
    • Ballance, D.J. (1986) Sequences important for gene expression in filamentous fungi. Yeast 2, 229-236.
    • (1986) Yeast , vol.2 , pp. 229-236
    • Ballance, D.J.1
  • 9
    • 0028070908 scopus 로고
    • Crystal-structure, at 2.6-Angstrom resolution, of the Streptomyces lividans xylanase-A, a member of the F-family of beta-1,4-D-glycanases
    • Derewenda, U., Swenson, L., Green, R., Wei, Y.Y., Morosoli, R., Shareck, F., Kluepfel, D. and Derewenda, Z.S. (1994) Crystal-structure, at 2.6-Angstrom resolution, of the Streptomyces lividans xylanase-A, a member of the F-family of beta-1,4-D-glycanases. J. Biol. Chem. 269, 20811-20814.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20811-20814
    • Derewenda, U.1    Swenson, L.2    Green, R.3    Wei, Y.Y.4    Morosoli, R.5    Shareck, F.6    Kluepfel, D.7    Derewenda, Z.S.8
  • 10
    • 0027169343 scopus 로고
    • A modular esterase from Pseudomonas fluorescens subsp. Cellulosa contains a noncatalytic cellulose-binding domain
    • Ferreira, L.M.A., Wood, T.M., Williamson, G., Faulds, C., Hazlewood, G.P., Black, G.W. and Gilbert, H.J. (1993) A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a noncatalytic cellulose-binding domain. Biochem. J. 294, 349-355.
    • (1993) Biochem. J. , vol.294 , pp. 349-355
    • Ferreira, L.M.A.1    Wood, T.M.2    Williamson, G.3    Faulds, C.4    Hazlewood, G.P.5    Black, G.W.6    Gilbert, H.J.7
  • 11
    • 0027326658 scopus 로고
    • Production of high-level of cellulase-free and thermostable xylanase by a wild strain of Thermomyces lanuginosus using beechwood xylan
    • Gomes, J., Gomes, I., Kreiner, W., Esterbauer, H., Sinner, M. and Steiner, W. (1993a) Production of high-level of cellulase-free and thermostable xylanase by a wild strain of Thermomyces lanuginosus using beechwood xylan. J. Biotechnol. 30, 283-297.
    • (1993) J. Biotechnol. , vol.30 , pp. 283-297
    • Gomes, J.1    Gomes, I.2    Kreiner, W.3    Esterbauer, H.4    Sinner, M.5    Steiner, W.6
  • 12
    • 0027201148 scopus 로고
    • Production of a high-level of cellulase-free xylanase by the thermophilic fungus Thermomyces lanuginosus in laboratory and pilot scales using lignocellulosic materials
    • Gomes, J., Purkarthofer, H., Hayn, M., Kapplmüller, J., Sinner, M. and Steiner, W. (1993b) Production of a high-level of cellulase-free xylanase by the thermophilic fungus Thermomyces lanuginosus in laboratory and pilot scales using lignocellulosic materials. Appl. Microbiol. Biotechnol. 39, 700-707.
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 700-707
    • Gomes, J.1    Purkarthofer, H.2    Hayn, M.3    Kapplmüller, J.4    Sinner, M.5    Steiner, W.6
  • 13
    • 0027229324 scopus 로고
    • Cloning and structural organization of a xylanase-encoding gene from Penicillium chrysogenum
    • Haas, H., Friedlin, E., Stoffler, G. and Redl, B. (1993) Cloning and structural organization of a xylanase-encoding gene from Penicillium chrysogenum. Gene 126, 237-242.
    • (1993) Gene , vol.126 , pp. 237-242
    • Haas, H.1    Friedlin, E.2    Stoffler, G.3    Redl, B.4
  • 14
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (Eds.) (1988) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 16
    • 0003106858 scopus 로고
    • ExAssist helper phage and SOLR cells for lambda ZapII excissions
    • Hay, B. and Short, J.M. (1992) ExAssist helper phage and SOLR cells for lambda ZapII excissions. Stratagies 5, 16-18.
    • (1992) Stratagies , vol.5 , pp. 16-18
    • Hay, B.1    Short, J.M.2
  • 17
    • 0027477020 scopus 로고
    • Gene sequence and properties of celi, a family-E endoglucanase from Clostridium thermocellum
    • Hazlewood, G.P., Davidson, K., Laurie, J.I., Huskisson, N.S. and Gilbert, H.J. (1993) Gene sequence and properties of celi, a family-E endoglucanase from Clostridium thermocellum. J. Gen. Microbiol. 139, 307-316.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 307-316
    • Hazlewood, G.P.1    Davidson, K.2    Laurie, J.I.3    Huskisson, N.S.4    Gilbert, H.J.5
  • 18
    • 0011803575 scopus 로고
    • Analysis of hemicellulases sequences. Relationship to other glycanases
    • Visser, J., Kusters-van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Elsevier, Amsterdam
    • Henrissat, B. (1992) Analysis of hemicellulases sequences. Relationship to other glycanases. In: Visser, J., Kusters-van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Xylans and Xylanases, Elsevier, Amsterdam, pp. 97-110.
    • (1992) Xylans and Xylanases , pp. 97-110
    • Henrissat, B.1
  • 19
    • 0027459055 scopus 로고
    • Cloning of a Microbispora bispora cellobiohydrolase gene in Streptomyces lividans
    • Hu, P., Chase, T. and Eveleigh, D.E. (1993) Cloning of a Microbispora bispora cellobiohydrolase gene in Streptomyces lividans. Appl. Microbiol. Biotechnol. 38, 631-637.
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 631-637
    • Hu, P.1    Chase, T.2    Eveleigh, D.E.3
  • 20
    • 0026496315 scopus 로고
    • Site-Directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus
    • Ko, E.P., Akatsuka, H., Moriyama, H., Shinmyo, A., Hata, Y., Katsube, Y., Urabe, I. and Okada, H. (1992) Site-Directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus. Biochem. J. 288, 117-121.
    • (1992) Biochem. J. , vol.288 , pp. 117-121
    • Ko, E.P.1    Akatsuka, H.2    Moriyama, H.3    Shinmyo, A.4    Hata, Y.5    Katsube, Y.6    Urabe, I.7    Okada, H.8
  • 21
    • 0023930331 scopus 로고
    • Transformation of Penicillium chrysogenum using dominant selection markers and expression of an Escherichia coli lacZ fusion gene
    • Kolar, M., Punt, P.J., van den Hondel, C.A.M.J.J. and Schwab, H. (1988) Transformation of Penicillium chrysogenum using dominant selection markers and expression of an Escherichia coli lacZ fusion gene. Gene 62, 127-134.
    • (1988) Gene , vol.62 , pp. 127-134
    • Kolar, M.1    Punt, P.J.2    Van Den Hondel, C.A.M.J.J.3    Schwab, H.4
  • 22
    • 0028063768 scopus 로고
    • Cloning, sequencing, and regulation of a xylanase gene from the fungus Aureobasidium pullulans-Y-2311-1
    • Correction: Appl. Environ. Microbiol. 60, 4647
    • Li, X.L. and Ljungdahl, L.G. (1994) Cloning, sequencing, and regulation of a xylanase gene from the fungus Aureobasidium pullulans-Y-2311-1. Appl. Environ. Microbiol. 60, 4647-4647. Correction: Appl. Environ. Microbiol. 60, 4647.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4647-4647
    • Li, X.L.1    Ljungdahl, L.G.2
  • 24
    • 0028244925 scopus 로고
    • Identification of glutamic-acid-78 as the active-site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass-spectrometry
    • Miao, S.C., Ziser, L., Aebersold, R. and Withers, S.G. (1994) Identification of glutamic-acid-78 as the active-site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass-spectrometry. Biochemistry 33, 7027-7032
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.C.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 25
    • 0028214219 scopus 로고
    • Evidence for a general role for high-affinity noncatalytic cellulose-binding domains in microbial plant-cell wall hydrolases
    • Millwardsadler, S.J., Poole, D.M., Henrissat, B., Hazlewood, G.P., Clarke, J.H. and Gilbert, H.J. (1994) Evidence for a general role for high-affinity noncatalytic cellulose-binding domains in microbial plant-cell wall hydrolases. Mol. Microbiol. 11, 375-382
    • (1994) Mol. Microbiol. , vol.11 , pp. 375-382
    • Millwardsadler, S.J.1    Poole, D.M.2    Henrissat, B.3    Hazlewood, G.P.4    Clarke, J.H.5    Gilbert, H.J.6
  • 27
    • 0027642084 scopus 로고
    • Cellulase-free xylanase from Thermomyces lanuginosus - Optimization of production in submerged and solid-state culture
    • Purkarthofer, H., Sinner, M. and Steiner, W. (1993a) Cellulase-free xylanase from Thermomyces lanuginosus - optimization of production in submerged and solid-state culture. Enzyme Microbe Technol. 115, 677-682
    • (1993) Enzyme Microbe Technol. , vol.115 , pp. 677-682
    • Purkarthofer, H.1    Sinner, M.2    Steiner, W.3
  • 28
    • 0027175083 scopus 로고
    • Effect of shear rate and culture pH on the production of xylanase by Thermomyces lanuginosus
    • Purkarthofer, H., Sinner, M. and Steiner, W. (1993b) Effect of shear rate and culture pH on the production of xylanase by Thermomyces lanuginosus. Biotechnol. Lett. 15, 405-410
    • (1993) Biotechnol. Lett. , vol.15 , pp. 405-410
    • Purkarthofer, H.1    Sinner, M.2    Steiner, W.3
  • 29
    • 0027548085 scopus 로고
    • Nucleotide-sequence of the Clostridium stercorarium xyna gene encoding xylanase-A: Identification of catalytic and cellulose binding domains
    • Sakka, K., Kojima, Y., Kondo, T., Karita, S., Ohmiya, K. and Shimada, K. (1993) Nucleotide-sequence of the Clostridium stercorarium xyna gene encoding xylanase-A: identification of catalytic and cellulose binding domains. Biosci. Biotechnol. Biochem. 57, 273-277.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 273-277
    • Sakka, K.1    Kojima, Y.2    Kondo, T.3    Karita, S.4    Ohmiya, K.5    Shimada, K.6
  • 30
    • 0025606604 scopus 로고
    • Role of a disulfide cross-link in the conformational stability of a thermostable xylanase
    • Tatu, U., Murthy, S.K. and Vithayathil, P.J. (1990) Role of a disulfide cross-link in the conformational stability of a thermostable xylanase. J. Protein Chem. 9, 641-646.
    • (1990) J. Protein Chem. , vol.9 , pp. 641-646
    • Tatu, U.1    Murthy, S.K.2    Vithayathil, P.J.3
  • 31
    • 0026522151 scopus 로고
    • Purification and characterization of an endoglucanase from Streptomyces lividans-66 and DNA-sequence of the gene
    • Theberge, M., Lacaze, P., Shareck, F., Morosoli, R. and Kluepfel, D. (1992) Purification and characterization of an endoglucanase from Streptomyces lividans-66 and DNA-sequence of the gene. Appl. Environ, Microbiol. 58, 815-820.
    • (1992) Appl. Environ, Microbiol. , vol.58 , pp. 815-820
    • Theberge, M.1    Lacaze, P.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5
  • 33
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Törrönen, A., Harkki, A. and Rouvinen, J. (1994) Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J. 13, 2493-2501.
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 34
    • 0028911057 scopus 로고
    • Structural comparison of 2 major endo-1,4-xylanases from Trichoderma reesei
    • Törrönen, A. and Rouvinen, J. (1995) Structural comparison of 2 major endo-1,4-xylanases from Trichoderma reesei. Biochemistry 34, 847-856.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törrönen, A.1    Rouvinen, J.2
  • 35
    • 0002858205 scopus 로고
    • Gene Organization in Industrial Filamentous Fungi
    • Kinghorn, J.R. and Turner, G. (Eds.), Chapman and Hall, London
    • Unkles, S.E. (1992) Gene Organization in Industrial Filamentous Fungi. In: Kinghorn, J.R. and Turner, G. (Eds.), Applied Molecular Genetics of Filamentous Fungi, Chapman and Hall, London, pp. 28-53.
    • (1992) Applied Molecular Genetics of Filamentous Fungi , pp. 28-53
    • Unkles, S.E.1
  • 36
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 37
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active-site residues of the Bacillus circulans xylanase
    • Wakarchuk, W.W., Campbell, R.L., Sung W.L., Davoodi, J. and Yaguchi, M. (1994a) Mutational and crystallographic analyses of the active-site residues of the Bacillus circulans xylanase. Protein Sci. 3, 467-475.
    • (1994) Protein Sci. , vol.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 38
    • 0028080502 scopus 로고
    • Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds
    • Wakarchuk, W.W., Sung, W.L., Campbell, R.L., Cunningham, A., Watson, D.C. and Yaguchi, M. (1994b) Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. Protein Eng. 7, 1379-1386.
    • (1994) Protein Eng. , vol.7 , pp. 1379-1386
    • Wakarchuk, W.W.1    Sung, W.L.2    Campbell, R.L.3    Cunningham, A.4    Watson, D.C.5    Yaguchi, M.6
  • 39
    • 0002746984 scopus 로고
    • Aminoacid sequence of the low molecular weight xylanase from Trichoderma viride. Relationship to other glycanases
    • Visser, J., Kusters-van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Elsevier, Amsterdam
    • Yaguchi, M., Roy, C., Ujiie, M., Watson, D.C. and Wakarchuk, W. (1992) Aminoacid sequence of the low molecular weight xylanase from Trichoderma viride. Relationship to other glycanases. In: Visser, J., Kusters-van Someren, M.A., Beldman, G. and Voragen, A.G.J. (Eds.), Xylans and Xylanases, Elsevier, Amsterdam, pp. 149-154.
    • (1992) Xylans and Xylanases , pp. 149-154
    • Yaguchi, M.1    Roy, C.2    Ujiie, M.3    Watson, D.C.4    Wakarchuk, W.5
  • 40
    • 0001617063 scopus 로고
    • Efficient isolation of genes by using antibody probes
    • Young, R.A. and Davis, R.W. (1983) Efficient isolation of genes by using antibody probes. Proc. Natl. Acad. Sci. USA 80, 1194-1198.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1194-1198
    • Young, R.A.1    Davis, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.