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Volumn 395, Issue 4, 2014, Pages 413-424

Characterization of a type D1A EUL-related lectin from rice expressed in Pichia pastoris

Author keywords

carbohydrate specificity; carbohydrate binding protein; glycobiology; recombinant protein expression; rice

Indexed keywords

AMINO ACID; CARBOHYDRATE; EULD1A PROTEIN; LECTIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; PLANT LECTIN;

EID: 84896747700     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0267     Document Type: Article
Times cited : (8)

References (49)
  • 3
    • 84887999305 scopus 로고    scopus 로고
    • Promoter analysis for three types of EUL-related rice lectins in transgenic Arabidopsis
    • Al Atalah, B., Fouquaert, E., and Van Damme, E.J.M. (2013). Promoter analysis for three types of EUL-related rice lectins in transgenic Arabidopsis. Plant Mol. Biol. Rep. 31, 1315-1324.
    • (2013) Plant Mol. Biol. Rep. , vol.31 , pp. 1315-1324
    • Al Atalah, B.1    Fouquaert, E.2    Van Damme, E.J.M.3
  • 4
    • 13444263345 scopus 로고    scopus 로고
    • The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring β-trefoil fold in the progenitor toxin complex
    • DOI 10.1016/j.jmb.2004.12.039
    • Arndt, J.W., Gu, J., Jaroszewski, L., Schwarzenbacher, R., Hanson, M.A., Lebeda, F.J., and Stevens, R.C. (2005). The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring β-trefoil fold in the progenitor toxin complex. J. Mol. Biol. 346, 1083-1093. (Pubitemid 40215532)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 1083-1093
    • Arndt, J.W.1    Gu, J.2    Jaroszewski, L.3    Schwarzenbacher, R.4    Hanson, M.A.5    Lebeda, F.J.6    Stevens, R.C.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 66649116284 scopus 로고    scopus 로고
    • Eukaryotic starch degradation: Integration of plastidial and cytosolic pathways
    • Fettke, J., Hejazi, M., Smirnova, J., Höchel, E., Stage, M., and Steup, M. (2009). Eukaryotic starch degradation: integration of plastidial and cytosolic pathways. J. Exp. Bot. 60, 2907-2922.
    • (2009) J. Exp. Bot. , vol.60 , pp. 2907-2922
    • Fettke, J.1    Hejazi, M.2    Smirnova, J.3    Höchel, E.4    Stage, M.5    Steup, M.6
  • 8
    • 79958769573 scopus 로고    scopus 로고
    • Identification of a novel heteroglycan-interacting protein, HIP 1.3, from Arabidopsis thaliana
    • Fettke, J., Nunes-Nesi, A., Fernie, A.R., and Steup, M. (2011). Identification of a novel heteroglycan-interacting protein, HIP 1.3, from Arabidopsis thaliana. J. Plant Physiol. 168, 1415-1425.
    • (2011) J. Plant Physiol. , vol.168 , pp. 1415-1425
    • Fettke, J.1    Nunes-Nesi, A.2    Fernie, A.R.3    Steup, M.4
  • 9
    • 85016377357 scopus 로고    scopus 로고
    • Promiscuity of the Euonymus carbohydrate-binding domain
    • Fouquaert, E. and Van Damme, E.J.M. (2012). Promiscuity of the Euonymus carbohydrate-binding domain. Biomolecules 2, 415-434.
    • (2012) Biomolecules , vol.2 , pp. 415-434
    • Fouquaert, E.1    Van Damme, E.J.M.2
  • 10
    • 51549094455 scopus 로고    scopus 로고
    • The "old" Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins
    • DOI 10.1104/pp.108.116764
    • Fouquaert, E., Peumans, W.J., Smith, D.F., Proost, P., Savvides, S.N., and Van Damme, E.J.M. (2008). The old Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins. Plant Physiol. 147, 1316-1324. (Pubitemid 352844265)
    • (2008) Plant Physiology , vol.147 , Issue.3 , pp. 1316-1324
    • Fouquaert, E.1    Peumans, W.J.2    Smith, D.F.3    Proost, P.4    Savvides, S.N.5    Van Damme, E.J.M.6
  • 13
    • 0036300580 scopus 로고    scopus 로고
    • Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: Sugar binding structure of the family 13 carbohydrate binding module
    • DOI 10.1006/jmbi.2001.5338
    • Fujimoto, Z., Kuno, A., Kaneko, S., Kobayashi, H., Kusakabe, I., and Mizuno, H. (2002). Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module. J. Mol. Biol. 316, 65-78. (Pubitemid 34729266)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.1 , pp. 65-78
    • Fujimoto, Z.1    Kuno, A.2    Kaneko, S.3    Kobayashi, H.4    Kusakabe, I.5    Mizuno, H.6
  • 14
    • 26944477789 scopus 로고    scopus 로고
    • Biopharmaceutical production in plants: Problems, solutions and opportunities
    • DOI 10.1016/j.tibtech.2005.09.003, PII S0167779905002453
    • Gomord, V., Chamberlain, P., Jefferis, R., and Faye, L. (2005). Biopharmaceutical production in plants: problems, solutions and opportunities. Trends Biotechnol. 23, 559-565. (Pubitemid 41483773)
    • (2005) Trends in Biotechnology , vol.23 , Issue.11 , pp. 559-565
    • Gomord, V.1    Chamberlain, P.2    Jefferis, R.3    Faye, L.4
  • 15
    • 33846886702 scopus 로고    scopus 로고
    • Regulation of methanol utilisation pathway genes in yeasts
    • Hartner, F.S. and Glieder, A. (2006). Regulation of methanol utilisation pathway genes in yeasts. Microb. Cell. Fact. 5, 39.
    • (2006) Microb. Cell. Fact. , vol.5 , pp. 39
    • Hartner, F.S.1    Glieder, A.2
  • 16
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • DOI 10.1016/S0168-1656(03)00003-8
    • Jahic, M., Gustavsson, M., Jansen, A.K., Martinelle, M., and Enfors, S.O. (2003). Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J. Biotechnol. 102, 45-53. (Pubitemid 36369202)
    • (2003) Journal of Biotechnology , vol.102 , Issue.1 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.-K.3    Martinelle, M.4    Enfors, S.-O.5
  • 17
    • 77950261904 scopus 로고    scopus 로고
    • Evolutionary history and stress regulation of the lectin superfamily in higher plants
    • Jiang, S.Y., Ma, Z., and Ramachandran, S. (2010). Evolutionary history and stress regulation of the lectin superfamily in higher plants. BMC Evol. Biol. 10, 79.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 79
    • Jiang, S.Y.1    Ma, Z.2    Ramachandran, S.3
  • 18
    • 15244359424 scopus 로고    scopus 로고
    • Occurrence of Lewis a epitope in N-glycans of a glycoallergen, Jun a 1, from mountain cedar (Juniperus ashei) pollen
    • DOI 10.1271/bbb.69.137
    • Kimura, Y., Kamamoto, M., Maeda, M., Okano, M., Yokoyama, M., and Kino, K. (2005). Occurrence of Lewis a epitope in N-glycans of a glycoallergen, Jun a 1, from mountain cedar (Juniperus ashei) pollen. Biosci. Biotechnol. Biochem. 69, 137-144. (Pubitemid 40383493)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.1 , pp. 137-144
    • Kimura, Y.1    Kamamoto, M.2    Maeda, M.3    Okano, M.4    Yokoyama, M.5    Kino, K.6
  • 19
    • 0025672675 scopus 로고
    • Isolation and characterization of BanLec-I, a mannoside binding lectin from Musa paradisiac (banana)
    • Koshte, V.L., Van Dijk, W., Van Der Stelt, M.E., and Aalberse, R.A. (1990). Isolation and characterization of BanLec-I, a mannoside binding lectin from Musa paradisiac (banana). Biochem. J. 272, 721-726.
    • (1990) Biochem. J. , vol.272 , pp. 721-726
    • Koshte, V.L.1    Van Dijk, W.2    Van Der Stelt, M.E.3    Aalberse, R.A.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 33947354555 scopus 로고    scopus 로고
    • Expression of the nucleocytoplasmic tobacco lectin in the yeast Pichia pastoris
    • DOI 10.1016/j.pep.2007.01.007, PII S1046592807000216
    • Lannoo, N., Vervecken, W., Proost, P., Rougé, P., and Van Damme, E.J.M. (2007). Expression of the nucleocyto-plasmic tobacco lectin in the yeast Pichia pastoris. Protein Expr. Purif. 53, 275-282. (Pubitemid 46454450)
    • (2007) Protein Expression and Purification , vol.53 , Issue.2 , pp. 275-282
    • Lannoo, N.1    Vervecken, W.2    Proost, P.3    Rouge, P.4    Van Damme, E.J.M.5
  • 23
    • 34247616380 scopus 로고    scopus 로고
    • Glycome mapping on DNA sequencing equipment
    • Laroy, W., Contreras, R., and Callewaert, N. (2006). Glycome mapping on DNA sequencing equipment. Nat. Protoc. 1, 397-407.
    • (2006) Nat. Protoc. , vol.1 , pp. 397-407
    • Laroy, W.1    Contreras, R.2    Callewaert, N.3
  • 25
    • 33750287032 scopus 로고    scopus 로고
    • Expression profiling of rice genes in early defense responses to blast and bacterial blight pathogens using cDNA microarray
    • DOI 10.1016/j.pmpp.2006.06.002, PII S0885576506000440
    • Li, Q., Chen, F., Sun, L., Zhang, Z., Yang, Y., and He, Z. (2006). Expression profiling of rice genes in early defense responses to blast and bacterial blight pathogens using cDNA microarray. Physiol. Mol. Plant Pathol. 68, 51-60. (Pubitemid 44633581)
    • (2006) Physiological and Molecular Plant Pathology , vol.68 , Issue.1-3 , pp. 51-60
    • Li, Q.1    Chen, F.2    Sun, L.3    Zhang, Z.4    Yang, Y.5    He, Z.6
  • 27
    • 78649955872 scopus 로고    scopus 로고
    • Intracellular and extracellular free N-glycans produced by plant cells: Occurrence of unusual plant complex-type free N-glycans in extracellular spaces
    • Maeda, M., Kimura, M., and Kimura, Y. (2010). Intracellular and extracellular free N-glycans produced by plant cells: occurrence of unusual plant complex-type free N-glycans in extracellular spaces. J. Biochem. 148, 681-692.
    • (2010) J. Biochem. , vol.148 , pp. 681-692
    • Maeda, M.1    Kimura, M.2    Kimura, Y.3
  • 29
    • 0030739509 scopus 로고    scopus 로고
    • An abscisic-acid- and salt-stress-responsive rice cDNA from a novel plant gene family
    • DOI 10.1007/s004250050148
    • Moons, A., Gielen, J., Vandekerckhove, J., Van Der Straeten, D., Gheysen, G., and Van Montagu, M. (1997). An abscisic-acid and salt-stress-responsive rice cDNA from a novel plant gene family. Planta 202, 443-454. (Pubitemid 27324637)
    • (1997) Planta , vol.202 , Issue.4 , pp. 443-454
    • Moons, A.1    Gielen, J.2    Vandekerckhove, J.3    Van Der Straeten, D.4    Gheysen, G.5    Van Montagu, M.6
  • 30
    • 0037298461 scopus 로고    scopus 로고
    • Production of native recombinant human midkine in the yeast, Pichia pastoris
    • DOI 10.1016/S1046-5928(02)00587-9, PII S1046592802005879
    • Murasugi, A. and Tohma-Aiba, Y. (2003). Production of native recombinant human midkine in the yeast, Pichia pastoris. Protein Expr. Purif. 27, 244-252. (Pubitemid 36339295)
    • (2003) Protein Expression and Purification , vol.27 , Issue.2 , pp. 244-252
    • Murasugi, A.1    Tohma-Aiba, Y.2
  • 31
    • 0034768744 scopus 로고    scopus 로고
    • Production of recombinant human bile salt-stimulated lipase in Pichia pastoris
    • DOI 10.1006/prep.2001.1509
    • Murasugi, A., Asami, Y., and Mera-Kikuchi, Y. (2001). Production of recombinant human bile salt stimulated lipase in Pichia pastoris. Protein Expr. Purif. 23, 282-288. (Pubitemid 33037796)
    • (2001) Protein Expression and Purification , vol.23 , Issue.2 , pp. 282-288
    • Murasugi, A.1    Asami, Y.2    Mera-Kikuchi, Y.3
  • 32
    • 56749156122 scopus 로고    scopus 로고
    • Changes in structural features of free N-glycan and endoglycosidase activity during tomato fruit ripening
    • Nakamura, K., Inoue, M., Yoshiie, T., Hosoi, K., and Kimura, Y. (2008). Changes in structural features of free N-glycan and endoglycosidase activity during tomato fruit ripening. Biosci. Biotechnol. Biochem. 72, 2936-2945.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 2936-2945
    • Nakamura, K.1    Inoue, M.2    Yoshiie, T.3    Hosoi, K.4    Kimura, Y.5
  • 33
    • 45449112140 scopus 로고    scopus 로고
    • Expression of frutalin, an α-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris
    • Oliveira, C., Felix, W., Moreira, R.A., Teixeira, J.A., and Domingues, L. (2008). Expression of frutalin, an α-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris. Protein Expr. Purif. 60, 188-193.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 188-193
    • Oliveira, C.1    Felix, W.2    Moreira, R.A.3    Teixeira, J.A.4    Domingues, L.5
  • 34
    • 0029379651 scopus 로고
    • Lectins as plant defense proteins
    • Peumans, W.J. and Van Damme, E.J.M. (1995). Lectins as plant defense proteins. Plant Physiol. 109, 347-352.
    • (1995) Plant Physiol. , vol.109 , pp. 347-352
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 37
    • 0027605811 scopus 로고
    • Structure of ten free N-glycans in ripening tomato fruit
    • Priem, B., Gitti, R., Bush, C.A., and Gross, K.C. (1993). Structure of ten free N-glycans in ripening tomato fruit. Plant Physiol. 102, 445-458.
    • (1993) Plant Physiol. , vol.102 , pp. 445-458
    • Priem, B.1    Gitti, R.2    Bush, C.A.3    Gross, K.C.4
  • 38
    • 9744256938 scopus 로고    scopus 로고
    • A database analysis of jacalin-like lectins: Sequence-structure-function relationships
    • DOI 10.1093/glycob/cwh140
    • Raval, S., Gowda, S.B., Singh, D.D., and Chandra, N.R. (2004). A database analysis of jacalin-like lectins: sequence-structure-function relationships. Glycobiol. 14, 1247-1263. (Pubitemid 39585358)
    • (2004) Glycobiology , vol.14 , Issue.12 , pp. 1247-1263
    • Raval, S.1    Gowda, S.B.2    Singh, D.D.3    Chandra, N.R.4
  • 40
    • 84863472557 scopus 로고    scopus 로고
    • Arabidopsis F-box protein containing a Nictaba-related lectin domain interacts with N-acetyllactosamine structures
    • Stefanowicz, K., Lannoo, N., Proost, P., and Van Damme, E.J.M. (2012). Arabidopsis F-box protein containing a Nictaba-related lectin domain interacts with N-acetyllactosamine structures. FEBS Open Bio. 2, 151-158.
    • (2012) FEBS Open Bio. , vol.2 , pp. 151-158
    • Stefanowicz, K.1    Lannoo, N.2    Proost, P.3    Van Damme, E.J.M.4
  • 41
    • 84870946443 scopus 로고    scopus 로고
    • A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes
    • Tiels, P., Baranova, B., Piens, K., Visscher, C.D., Pynaert, G., Nerinckx, W., Stout, J., Fudalej, F., Hulpiau, P., Tännler, S., et al. (2012). A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes. Nat. Biotechnol. 30, 1225-1231.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1225-1231
    • Tiels, P.1    Baranova, B.2    Piens, K.3    Visscher, C.D.4    Pynaert, G.5    Nerinckx, W.6    Stout, J.7    Fudalej, F.8    Hulpiau, P.9    Tännler, S.10
  • 43
    • 4644226850 scopus 로고    scopus 로고
    • Cytoplasmic/nuclear plant lectins: A new story
    • DOI 10.1016/j.tplants.2004.08.003, PII S1360138504001980
    • Van Damme, E.J.M., Barre, A., Rougé, P., and Peumans, W.J. (2004a). Cytoplasmic/nuclear plant lectins: a new story. Trends Plant Sci. 9, 484-489. (Pubitemid 39301186)
    • (2004) Trends in Plant Science , vol.9 , Issue.10 , pp. 484-489
    • Van Damme, E.J.M.1    Barre, A.2    Rouge, P.3    Peumans, W.J.4
  • 44
    • 16644383558 scopus 로고    scopus 로고
    • The identification of inducible cytoplasmic/nuclear carbohydrate-binding proteins urges to develop novel concepts about the role of plant lectins
    • DOI 10.1023/B:GLYC.0000038291.67527.a5
    • Van Damme, E.J.M., Lannoo, N., Fouquaert, E., and Peumans, W.J. (2004b). The identification of inducible cytoplasmic/nuclear carbohydrate binding proteins urges to develop novel concepts about the role of plant lectins. Glycoconj. J. 20, 449-460. (Pubitemid 43014139)
    • (2004) Glycoconjugate Journal , vol.20 , Issue.7-8 , pp. 449-460
    • Van Damme, E.J.M.1    Lannoo, N.2    Fouquaert, E.3    Peumans, W.J.4
  • 46
    • 85016367050 scopus 로고    scopus 로고
    • Carbohydrate protein interactions: Plant lectins
    • J.P. Kamerling, G.J. Boons, Y.C. Lee, A. Suzuki, N. Taniguchi, A.G.J. Voragen, eds. (New York: Elsevier)
    • Van Damme, E.J.M., Rougé, P., and Peumans, W.J. (2007b). Carbohydrate protein interactions: plant lectins. In: Comprehensive glycoscience-from chemistry to systems biology, J.P. Kamerling, G.J. Boons, Y.C. Lee, A. Suzuki, N. Taniguchi, A.G.J. Voragen, eds. (New York: Elsevier), pp. 563-599.
    • (2007) Comprehensive Glycoscience-from Chemistry to Systems Biology , pp. 563-599
    • Van Damme, E.J.M.1    Rougé, P.2    Peumans, W.J.3
  • 49
    • 77956261162 scopus 로고    scopus 로고
    • High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: Toward clinical implementation of GlycoHepatoTest
    • Vanderschaeghe, D., Szekrényes, Á., Wenz, C., Gassmann, M., Naik, N., Bynum, M., Yin, H., Delanghe, J., Guttman, A., and Callewaert, N. (2010). High-throughput profiling of the serum N-glycome on capillary electrophoresis microfluidics systems: toward clinical implementation of GlycoHepatoTest. Anal. Chem. 82, 7408-7415.
    • (2010) Anal. Chem. , vol.82 , pp. 7408-7415
    • Vanderschaeghe, D.1    Szekrényes, Á.2    Wenz, C.3    Gassmann, M.4    Naik, N.5    Bynum, M.6    Yin, H.7    Delanghe, J.8    Guttman, A.9    Callewaert, N.10


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