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Volumn 71, Issue 11, 2007, Pages 2688-2696

Identification and characterization of an intracellular lectin, calnexin, from Aspergillus oryzae using N-glycan-conjugated beads

Author keywords

Aspergillus oryzae; Calnexin; Lectin; N glycan; Quality control

Indexed keywords

ASPERGILLUS ORYZAE; CALNEXIN; ENDOPLASMIC RETICULUM; LECTIN; SEPHAROSE BEADS;

EID: 36448934888     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70289     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 0036366095 scopus 로고    scopus 로고
    • Molecular biology of the Koji molds
    • Kitamoto, K., Molecular biology of the Koji molds. Adv. Appl. Microbiol., 51, 129-153 (2002).
    • (2002) Adv. Appl. Microbiol , vol.51 , pp. 129-153
    • Kitamoto, K.1
  • 2
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: Progress, limitations and prospects
    • Gouka, R. J., Punt, P. J., and van den Hondel, C. A., Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl. Microbiol. Biotechnol., 47, 1-11 (1997).
    • (1997) Appl. Microbiol. Biotechnol , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    van den Hondel, C.A.3
  • 3
    • 0033777226 scopus 로고    scopus 로고
    • Filamentous fungi as microbial cell factories for food use
    • Archer, D. B., Filamentous fungi as microbial cell factories for food use. Curr. Opin. Biotechnol., 11, 478-483 (2000).
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 478-483
    • Archer, D.B.1
  • 5
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A., and Aebi, M., Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem., 73, 1019-1049 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 6
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams, D. B., Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci., 119, 615-623 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 7
    • 15944408403 scopus 로고    scopus 로고
    • In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control
    • Paquet, M. E., Leach, M. R., and Williams, D. B., In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control. Methods, 35, 338-347 (2005).
    • (2005) Methods , vol.35 , pp. 338-347
    • Paquet, M.E.1    Leach, M.R.2    Williams, D.B.3
  • 8
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach, M. R., Cohen-Doyle, M. F., Thomas, D. Y., and Williams, D. B., Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem., 277, 29686-29697 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 9
    • 15944401370 scopus 로고    scopus 로고
    • Glycoprotein reglucosylation
    • Trombetta, E. S., and Parodi, A. J., Glycoprotein reglucosylation. Methods, 35, 328-337 (2005).
    • (2005) Methods , vol.35 , pp. 328-337
    • Trombetta, E.S.1    Parodi, A.J.2
  • 10
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda, Y., Hosokawa, N., Wada, I., and Nagata, K., EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science, 299, 1394-1397 (2003).
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 11
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari, M., Calance, V., Galli, C., Lucca, P., and Paganetti, P., Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science, 299, 1397-1400 (2003).
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calance, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 12
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary, R., Bielmann, R., Nita-Lazar, M., Burda, P., and Jakob, C. A., Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol. Cell, 19, 765-775 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 13
    • 1542504611 scopus 로고    scopus 로고
    • Synthesis of an octamannosyled glycan chain, the key oligosaccharide structure in ER-associated degradation
    • Matsuo, I., and Ito, Y., Synthesis of an octamannosyled glycan chain, the key oligosaccharide structure in ER-associated degradation. Carbohydr. Res., 338, 2163-2168 (2003).
    • (2003) Carbohydr. Res , vol.338 , pp. 2163-2168
    • Matsuo, I.1    Ito, Y.2
  • 14
    • 0037467411 scopus 로고    scopus 로고
    • Synthesis of monoglucosylated high-mannose-type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticulin
    • Matsuo, I., Wada, M., Manabe, S., Yamaguchi, Y., Otake, K., Kato, K., and Ito, Y., Synthesis of monoglucosylated high-mannose-type dodecasaccharide, a putative ligand for molecular chaperone, calnexin, and calreticulin. J. Am. Chem. Soc., 125, 3402-3403 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 3402-3403
    • Matsuo, I.1    Wada, M.2    Manabe, S.3    Yamaguchi, Y.4    Otake, K.5    Kato, K.6    Ito, Y.7
  • 16
    • 33745940580 scopus 로고    scopus 로고
    • Comprehensive synthesis of ER related high-mannose-type sugar chains by convergent strategy
    • Matsuo, I., Totani, K., Tatami, A., and Ito, Y., Comprehensive synthesis of ER related high-mannose-type sugar chains by convergent strategy. Tetrahedron, 62, 8262-8277 (2006).
    • (2006) Tetrahedron , vol.62 , pp. 8262-8277
    • Matsuo, I.1    Totani, K.2    Tatami, A.3    Ito, Y.4
  • 17
    • 25844518421 scopus 로고    scopus 로고
    • Synthetic substrates for an endoplasmic reticulum protein-folding sensor, UDP-glucose: Glycoprotein glucosyltransferase
    • Totani, K., Ihara, Y., Matsuo, I., Koshino, H., and Ito, Y., Synthetic substrates for an endoplasmic reticulum protein-folding sensor, UDP-glucose: glycoprotein glucosyltransferase. Angew. Chem. Int. Ed. Engl., 44, 7950-7954 (2005).
    • (2005) Angew. Chem. Int. Ed. Engl , vol.44 , pp. 7950-7954
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Koshino, H.4    Ito, Y.5
  • 18
    • 33845969527 scopus 로고    scopus 로고
    • Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans
    • Totani, K., Ihara, Y., Matsuo, I., and Ito, Y., Substrate specificity analysis of endoplasmic reticulum glucosidase II using synthetic high mannose-type glycans. J. Biol. Chem., 281, 31502-31508 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 31502-31508
    • Totani, K.1    Ihara, Y.2    Matsuo, I.3    Ito, Y.4
  • 19
    • 0036154223 scopus 로고    scopus 로고
    • Calnexin overexpression increases manganese peroxidase production in Aspergillus niger
    • Conesa, A., Jeenes, D., Archer, D. B., van den Hondel, C. A., and Punt, P. J., Calnexin overexpression increases manganese peroxidase production in Aspergillus niger. Appl. Environ. Microbiol., 68, 846-851 (2002).
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 846-851
    • Conesa, A.1    Jeenes, D.2    Archer, D.B.3    van den Hondel, C.A.4    Punt, P.J.5
  • 20
    • 20444391995 scopus 로고    scopus 로고
    • Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: A frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30
    • Geysens, S., Pakula, T., Uusitalo, J., Dewerte, I., Penttila, M., and Contreras, R., Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: a frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30. Appl. Environ. Microbiol., 71, 2910-2924 (2005).
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 2910-2924
    • Geysens, S.1    Pakula, T.2    Uusitalo, J.3    Dewerte, I.4    Penttila, M.5    Contreras, R.6
  • 21
    • 33745142954 scopus 로고    scopus 로고
    • High-mannose-type glycan modifications of dihydrofolate reductase using glycan-methotrexate conjugates
    • Totani, K., Matsuo, I., Ihara, Y., and Ito, Y., High-mannose-type glycan modifications of dihydrofolate reductase using glycan-methotrexate conjugates. Bioorg. Med. Chem., 14, 5220-5229 (2006).
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 5220-5229
    • Totani, K.1    Matsuo, I.2    Ihara, Y.3    Ito, Y.4
  • 22
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L., Tissue sulfhydryl groups. Arch. Biochem. Biophys., 82, 70-77 (1959).
    • (1959) Arch. Biochem. Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 23
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem., 68, 850-858 (1996).
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis, 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 33747835577 scopus 로고    scopus 로고
    • Development of a versatile expression plasmid construction system for Aspergillus oryzae and its application to visualization of mitochondria
    • Mabashi, Y., Kikuma, T., Maruyama, J., Arioka, M., and Kitamoto, K., Development of a versatile expression plasmid construction system for Aspergillus oryzae and its application to visualization of mitochondria. Biosci. Biotechnol. Biochem., 70, 1882-1889 (2006).
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 1882-1889
    • Mabashi, Y.1    Kikuma, T.2    Maruyama, J.3    Arioka, M.4    Kitamoto, K.5
  • 26
    • 85009547782 scopus 로고    scopus 로고
    • Transformation system for Aspergillus oryzae with double auxotrophic mutations, niaD and sC
    • Yamada, O., Lee, B. R., and Gomi, K., Transformation system for Aspergillus oryzae with double auxotrophic mutations, niaD and sC. Biosci. Biotechnol. Biochem., 61, 1367-1369 (1997).
    • (1997) Biosci. Biotechnol. Biochem , vol.61 , pp. 1367-1369
    • Yamada, O.1    Lee, B.R.2    Gomi, K.3
  • 28
    • 33746845238 scopus 로고    scopus 로고
    • Differential distribution of the endoplasmic reticulum network as visualized by the BipA-EGFP fusion protein in hyphal compartments across the septum of the filamentous fungus
    • Maruyama, J., Kikuchi, S., and Kitamoto, K., Differential distribution of the endoplasmic reticulum network as visualized by the BipA-EGFP fusion protein in hyphal compartments across the septum of the filamentous fungus, Aspergillus oryzae. Fungal Genet. Biol., 43, 642-654 (2006).
    • (2006) Aspergillus oryzae. Fungal Genet. Biol , vol.43 , pp. 642-654
    • Maruyama, J.1    Kikuchi, S.2    Kitamoto, K.3
  • 29
    • 33745966302 scopus 로고    scopus 로고
    • Design and synthesis of oligosaccharides that interfere with glycoprotein quality-control systems
    • Arai, M. A., Matsuo, I., Hagihara, S., Totani, K., Maruyama, J., Kitamoto, K., and Ito, Y., Design and synthesis of oligosaccharides that interfere with glycoprotein quality-control systems. Chembiochem, 6, 2281-2289 (2005).
    • (2005) Chembiochem , vol.6 , pp. 2281-2289
    • Arai, M.A.1    Matsuo, I.2    Hagihara, S.3    Totani, K.4    Maruyama, J.5    Kitamoto, K.6    Ito, Y.7
  • 30
    • 0028921010 scopus 로고
    • The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability
    • Jannatipour, M., and Rokeach, L. A., The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability. J. Biol. Chem., 270, 4845-4853 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 4845-4853
    • Jannatipour, M.1    Rokeach, L.A.2
  • 31
    • 0029006125 scopus 로고
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain. EMBO J., 14, 3064-3072 (1995).
    • (1995) EMBO J , vol.14 , pp. 3064-3072
    • Parlati, F.1    Dignard, D.2    Bergeron, J.J.3    Thomas, D.Y.4
  • 33
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro, R. G., Zhu, Q., Bhoyroo, V., and Soling, H. D., Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem., 271, 11588-11594 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 34
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos, A., Michalak, M., Lehrman, M. A., and Williams, D. B., Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry, 37, 3480-3490 (1998).
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 35
    • 0034799402 scopus 로고    scopus 로고
    • The Structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J. D., Bergeron, J. J., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., and Cygler, M., The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell, 8, 633-644 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 36
    • 0034235397 scopus 로고    scopus 로고
    • Calcium, a signaling molecule in the endoplasmic reticulum?
    • Corbett, E. F., and Michalak, M., Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem. Sci., 25, 307-311 (2000).
    • (2000) Trends Biochem. Sci , vol.25 , pp. 307-311
    • Corbett, E.F.1    Michalak, M.2
  • 37
    • 0002949582 scopus 로고
    • The structure and organisation of nuclear genes in filamentous fungi
    • ed. Kinghorn, J. R, IRL Press, Oxford, pp
    • Gurr, S. J., Unkles, S. E., and Kinghorn, J. R., The structure and organisation of nuclear genes in filamentous fungi. In "Gene Structure in Eukaryotic Microbes," ed. Kinghorn, J. R., IRL Press, Oxford, pp. 93-139 (1987).
    • (1987) Gene Structure in Eukaryotic Microbes , pp. 93-139
    • Gurr, S.J.1    Unkles, S.E.2    Kinghorn, J.R.3
  • 38
    • 33745699785 scopus 로고    scopus 로고
    • HACA, the transcriptional activator of the unfolded protein response (UPR) in Aspergillus niger, binds to partly palindromic UPR elements of the consensus sequence 5′-CAN(G/A)NTGT/GCCT-3′
    • Mulder, H. J., Nikolaev, I., and Madrid, S. M., HACA, the transcriptional activator of the unfolded protein response (UPR) in Aspergillus niger, binds to partly palindromic UPR elements of the consensus sequence 5′-CAN(G/A)NTGT/GCCT-3′. Fungal Genet. Biol., 43, 560-572 (2006).
    • (2006) Fungal Genet. Biol , vol.43 , pp. 560-572
    • Mulder, H.J.1    Nikolaev, I.2    Madrid, S.M.3
  • 39
    • 25844454688 scopus 로고    scopus 로고
    • Structural approaches to the study of oligosaccharides in glycoprotein quality control
    • Ito, Y., Hagihara, S., Matsuo, I., and Totani, K., Structural approaches to the study of oligosaccharides in glycoprotein quality control. Curr. Opin. Struct. Biol., 15, 481-489 (2005).
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 481-489
    • Ito, Y.1    Hagihara, S.2    Matsuo, I.3    Totani, K.4
  • 40
    • 18244371937 scopus 로고    scopus 로고
    • Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1
    • Hagihara, S., Totani, K., Matsuo, I., and Ito, Y., Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1. J. Med. Chem., 48, 3126-3129 (2005).
    • (2005) J. Med. Chem , vol.48 , pp. 3126-3129
    • Hagihara, S.1    Totani, K.2    Matsuo, I.3    Ito, Y.4
  • 41
    • 3142610777 scopus 로고    scopus 로고
    • P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue
    • Xu, X., Azakami, H., and Kato, A., P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett., 570, 155-160 (2004).
    • (2004) FEBS Lett , vol.570 , pp. 155-160
    • Xu, X.1    Azakami, H.2    Kato, A.3
  • 42
    • 0037070208 scopus 로고    scopus 로고
    • Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes
    • Song, Y., Azakami, H., Shamima, B., He, J., and Kato, A., Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes. FEBS Lett., 512, 213-217 (2002).
    • (2002) FEBS Lett , vol.512 , pp. 213-217
    • Song, Y.1    Azakami, H.2    Shamima, B.3    He, J.4    Kato, A.5
  • 43
    • 0035660414 scopus 로고    scopus 로고
    • Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes
    • Song, Y., Sata, J., Saito, A., Usui, M., Azakami, H., and Kato, A., Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J. Biochem., 130, 757-764 (2001).
    • (2001) J. Biochem , vol.130 , pp. 757-764
    • Song, Y.1    Sata, J.2    Saito, A.3    Usui, M.4    Azakami, H.5    Kato, A.6
  • 44
    • 0032945481 scopus 로고    scopus 로고
    • Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells
    • Parodi, A. J., Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells. Biochim. Biophys. Acta, 1426, 287-295 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 287-295
    • Parodi, A.J.1


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