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Volumn 71, Issue 9, 2007, Pages 2256-2265

Molecular cloning of cDNA for trehalase from the european honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris

Author keywords

cDNA; Heterologous expression; Honeybee; Trehalase

Indexed keywords

AMINO ACIDS; DNA; ENZYMES; GENE ENCODING; LIVING SYSTEMS STUDIES; PEPTIDES; YEAST;

EID: 36148935981     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70239     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 0014309246 scopus 로고
    • Partial purification and properties of a trehalase from Streptomyces hygroscopicus
    • Hey, A. E., and Elbein, A. D., Partial purification and properties of a trehalase from Streptomyces hygroscopicus. J. Bacteriol., 96, 105-110 (1968).
    • (1968) J. Bacteriol , vol.96 , pp. 105-110
    • Hey, A.E.1    Elbein, A.D.2
  • 2
    • 0018171916 scopus 로고
    • α,α-Trehalase of Trichoderma reesei
    • Vijayakumar, P., Ross, W., and Reese, E. T., α,α-Trehalase of Trichoderma reesei. Can. J. Microbiol., 24, 1280-1283 (1978).
    • (1978) Can. J. Microbiol , vol.24 , pp. 1280-1283
    • Vijayakumar, P.1    Ross, W.2    Reese, E.T.3
  • 3
    • 0041606366 scopus 로고
    • Studies on carbohydrate-metabolizing enzymes: The hydrolysis of α-glucosides, including nigerose, by extracts of alfalfa and other higher plants
    • Hutson, D. H., and Manners, D. J., Studies on carbohydrate-metabolizing enzymes: the hydrolysis of α-glucosides, including nigerose, by extracts of alfalfa and other higher plants. Biochem. J., 94, 783-789 (1965).
    • (1965) Biochem. J , vol.94 , pp. 783-789
    • Hutson, D.H.1    Manners, D.J.2
  • 4
    • 0042107265 scopus 로고
    • Studies on trehalase in Saccharum spp. leaf and storage tissues
    • Alexander, A. G., Studies on trehalase in Saccharum spp. leaf and storage tissues. Plant Cell Physiol., 14, 157-168 (1973).
    • (1973) Plant Cell Physiol , vol.14 , pp. 157-168
    • Alexander, A.G.1
  • 5
    • 0013456725 scopus 로고
    • Trehalase of silkworm, Bombyx mori: Purification and properties of the enzyme
    • Saito, S., Trehalase of silkworm, Bombyx mori: purification and properties of the enzyme. J. Biochem. (Tokyo), 48, 101-109 (1960).
    • (1960) J. Biochem. (Tokyo) , vol.48 , pp. 101-109
    • Saito, S.1
  • 6
    • 0042107267 scopus 로고
    • Partial purification, stabilization and characterization of adult honey bee midgut trehalase and a new trehalase specific disc gel stain method
    • Talbot, B. G., and Huber, R. E., Partial purification, stabilization and characterization of adult honey bee midgut trehalase and a new trehalase specific disc gel stain method. Insect Biochem., 5, 337-347 (1975).
    • (1975) Insect Biochem , vol.5 , pp. 337-347
    • Talbot, B.G.1    Huber, R.E.2
  • 7
    • 27744582051 scopus 로고    scopus 로고
    • Membrane-penetrating trehalase from silkworm Bombyx mori. Molecular cloning and localization in larval midgut
    • Mitsumasu, K., Azuma, M., Niimi, T., Yamashita, O., and Yaginuma, T., Membrane-penetrating trehalase from silkworm Bombyx mori. Molecular cloning and localization in larval midgut. Insect Mol. Biol., 14, 501-508 (2005).
    • (2005) Insect Mol. Biol , vol.14 , pp. 501-508
    • Mitsumasu, K.1    Azuma, M.2    Niimi, T.3    Yamashita, O.4    Yaginuma, T.5
  • 8
    • 0014305619 scopus 로고
    • Trehalase and the transport of glucose in the mammalian kidney and intestine
    • Sacktor, B., Trehalase and the transport of glucose in the mammalian kidney and intestine. Proc. Natl. Acad. Sci. USA, 60, 1007-1014 (1968).
    • (1968) Proc. Natl. Acad. Sci. USA , vol.60 , pp. 1007-1014
    • Sacktor, B.1
  • 9
    • 0017704035 scopus 로고
    • Purification and properties of trehalase from rat intestinal mucosal cells
    • Nakano, M., Sumi, Y., and Miyakawa, M., Purification and properties of trehalase from rat intestinal mucosal cells. J. Biochem. (Tokyo), 81, 1041-1049 (1977).
    • (1977) J. Biochem. (Tokyo) , vol.81 , pp. 1041-1049
    • Nakano, M.1    Sumi, Y.2    Miyakawa, M.3
  • 10
    • 0021772474 scopus 로고
    • Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit
    • Galand, G., Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit. Biochim. Biophys. Acta, 789, 10-19 (1984).
    • (1984) Biochim. Biophys. Acta , vol.789 , pp. 10-19
    • Galand, G.1
  • 11
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities
    • Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 12
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • eds. Gilbert, H. J, Davies, G, Henrissat, B, and Svensson, B, The Royal Society of Chemistry, Cambridge, pp
    • Coutinho, P. M., and Henrissat, B., Carbohydrate-active enzymes: an integrated database approach. In "Recent Advances in Carbohydrate Bioengineering," eds. Gilbert, H. J., Davies, G., Henrissat, B., and Svensson, B., The Royal Society of Chemistry, Cambridge, pp. 3-12 (1999).
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 15
    • 0024278388 scopus 로고
    • Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase
    • Weiser, W., Lehmann, J., Chiba, S., Matsui, H., Brewer, C. F., and Hehre, E. J., Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase. Biochemistry, 27, 2294-2300 (1988).
    • (1988) Biochemistry , vol.27 , pp. 2294-2300
    • Weiser, W.1    Lehmann, J.2    Chiba, S.3    Matsui, H.4    Brewer, C.F.5    Hehre, E.J.6
  • 16
    • 33750460281 scopus 로고    scopus 로고
    • Insights into social insects from the genome of the honeybee Apis mellifera
    • The Honeybee Genome Sequencing Consortium
    • The Honeybee Genome Sequencing Consortium, Insights into social insects from the genome of the honeybee Apis mellifera. Nature, 433, 931-949 (2006).
    • (2006) Nature , vol.433 , pp. 931-949
  • 17
    • 0014868542 scopus 로고
    • Solubilization, purification, and some properties of trehalase from honeybee (Apis mellifera)
    • Lefebvre, Y. A., and Huber, R. E., Solubilization, purification, and some properties of trehalase from honeybee (Apis mellifera). Arch. Biochem. Biophys., 140, 514-518 (1970).
    • (1970) Arch. Biochem. Biophys , vol.140 , pp. 514-518
    • Lefebvre, Y.A.1    Huber, R.E.2
  • 18
    • 0013834940 scopus 로고
    • Membrane-bound trehalase from cecropia silkmoth muscle
    • Gussin, A. E. S., and Wyatt, G. R., Membrane-bound trehalase from cecropia silkmoth muscle. Arch. Biochem. Biophys., 112, 626-634 (1965).
    • (1965) Arch. Biochem. Biophys , vol.112 , pp. 626-634
    • Gussin, A.E.S.1    Wyatt, G.R.2
  • 19
    • 0033112556 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs encoding trehalase from post-dormant embryos of the brine shrimp
    • Tanaka, S., Nambu, F., and Nambu, Z., Cloning and characterization of cDNAs encoding trehalase from post-dormant embryos of the brine shrimp, Artemia franciscana. Zool. Sci., 16, 269-277 (1999).
    • (1999) Artemia franciscana. Zool. Sci , vol.16 , pp. 269-277
    • Tanaka, S.1    Nambu, F.2    Nambu, Z.3
  • 20
    • 0024675975 scopus 로고
    • Membrane anchors of alkaline phosphatase and trehalase associated with the plasma membrane of larval midgut epithelial cells of the silkworm
    • Takesue, Y., Yokota, K., Miyajima, S., Taguchi, R., and Ikezawa, H., Membrane anchors of alkaline phosphatase and trehalase associated with the plasma membrane of larval midgut epithelial cells of the silkworm, Bombyx mori. J. Biochem. (Tokyo), 105, 998-1001 (1989).
    • (1989) Bombyx mori. J. Biochem. (Tokyo) , vol.105 , pp. 998-1001
    • Takesue, Y.1    Yokota, K.2    Miyajima, S.3    Taguchi, R.4    Ikezawa, H.5
  • 21
    • 0022544619 scopus 로고
    • Solubilization of trehalase from rabbit renal and intestinal brush-border membranes by a phosphatidylinositol-specific phospholipase C
    • Takesue, Y., Yokota, K., Nishi, Y., Taguchi, R., and Ikezawa, H., Solubilization of trehalase from rabbit renal and intestinal brush-border membranes by a phosphatidylinositol-specific phospholipase C. FEBS Lett., 201, 5-8 (1986).
    • (1986) FEBS Lett , vol.201 , pp. 5-8
    • Takesue, Y.1    Yokota, K.2    Nishi, Y.3    Taguchi, R.4    Ikezawa, H.5
  • 22
    • 0025024244 scopus 로고
    • Rabbit small intestinal trehalase. Purification, cDNA cloning, expression, and verification of glycosylphosphatidylinositol anchoring
    • Ruf, J., Wacker, H., James, P., Maffia, M., Seiler, P., Galand, G., von Kieckebusch, A., Semenza, G., and Matei, N., Rabbit small intestinal trehalase. Purification, cDNA cloning, expression, and verification of glycosylphosphatidylinositol anchoring. J. Biol. Chem., 265, 15034-15039 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 15034-15039
    • Ruf, J.1    Wacker, H.2    James, P.3    Maffia, M.4    Seiler, P.5    Galand, G.6    von Kieckebusch, A.7    Semenza, G.8    Matei, N.9
  • 24
    • 27644512261 scopus 로고    scopus 로고
    • Glucoamylase originating from Schwanniomyces occidentalis is a typical α-glucosidase
    • Sato, F., Okuyama, M., Nakai, H., Mori, H., Kimura, A., and Chiba, S., Glucoamylase originating from Schwanniomyces occidentalis is a typical α-glucosidase. Biosci. Biotechnol. Biochem., 69, 1905-1913 (2005).
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1905-1913
    • Sato, F.1    Okuyama, M.2    Nakai, H.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 26
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction
    • Chomczynski, P., and Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction. Anal. Biochem., 162, 156-159 (1987).
    • (1987) Anal. Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 27
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman, M. A., Dush, M. K., and Martin, G. R., Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA, 85, 8998-9002 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 29
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and Sommer, S. S., The "megaprimer" method of site-directed mutagenesis. BioTechniques, 8, 404-407 (1990).
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 30
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F., Colorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350-356 (1956).
    • (1956) Anal. Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng., 10, 1-6 (1997).
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 32
    • 0019363396 scopus 로고
    • Organization and expression of eucaryotic split genes coding for proteins
    • Breathnach, R., and Chambon, P., Organization and expression of eucaryotic split genes coding for proteins. Ann. Rev. Biochem., 50, 349-383 (1981).
    • (1981) Ann. Rev. Biochem , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 33
    • 0027989645 scopus 로고
    • Molecular characterization of ovary trehalase of the silkworm, Bombyx mori and its transcriptional activation by diapause hormone
    • Su, Z.-H., Ikeda, M., Sato, Y., Saito, H., Imai, K., and Isobe, M., Molecular characterization of ovary trehalase of the silkworm, Bombyx mori and its transcriptional activation by diapause hormone. Biochim. Biophys. Acta, 1218, 366-374 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 366-374
    • Su, Z.-H.1    Ikeda, M.2    Sato, Y.3    Saito, H.4    Imai, K.5    Isobe, M.6
  • 34
  • 35
    • 0026451149 scopus 로고
    • Trehalase from male accessory gland of an insect, Tenebrio molitor: CDNA sequencing and developmental profile of the gene expression
    • Takiguchi, M., Niimi, T., Su, Z.-H., and Yaginuma, T., Trehalase from male accessory gland of an insect, Tenebrio molitor: cDNA sequencing and developmental profile of the gene expression. Biochem. J., 288, 19-22 (1992).
    • (1992) Biochem. J , vol.288 , pp. 19-22
    • Takiguchi, M.1    Niimi, T.2    Su, Z.-H.3    Yaginuma, T.4
  • 36
    • 0024677030 scopus 로고
    • Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12
    • Gutierrez, C., Ardourel, M., Bremer, E., and Middendorf, A., Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12. Mol. Gen. Genet., 217, 347-354 (1989).
    • (1989) Mol. Gen. Genet , vol.217 , pp. 347-354
    • Gutierrez, C.1    Ardourel, M.2    Bremer, E.3    Middendorf, A.4
  • 37
    • 0023440994 scopus 로고
    • Rat intestinal trehalase: Studies of the active site
    • Chen, C. C., Guo, W. J., and Isselbacher, K. J., Rat intestinal trehalase: studies of the active site. Biochem. J., 247, 715-724 (1987).
    • (1987) Biochem. J , vol.247 , pp. 715-724
    • Chen, C.C.1    Guo, W.J.2    Isselbacher, K.J.3
  • 38
    • 0042107266 scopus 로고
    • The purification and properties of trehalase from lady beetle
    • Ogawa, M., and Ariyoshi, U., The purification and properties of trehalase from lady beetle, Harmonia axyridis. Insect Biochem., 11, 397-400 (1981).
    • (1981) Harmonia axyridis. Insect Biochem , vol.11 , pp. 397-400
    • Ogawa, M.1    Ariyoshi, U.2
  • 39
    • 4744350436 scopus 로고    scopus 로고
    • The role of carboxyl, guanidine and imidazole groups in catalysis by a midgut trehalase purified from an insect larvae
    • Silva, M. C. P., Terra, W. R., and Ferreira, C., The role of carboxyl, guanidine and imidazole groups in catalysis by a midgut trehalase purified from an insect larvae. Insect Biochem. Mol. Biol., 34, 1089-1099 (2004).
    • (2004) Insect Biochem. Mol. Biol , vol.34 , pp. 1089-1099
    • Silva, M.C.P.1    Terra, W.R.2    Ferreira, C.3
  • 40
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T., The PSIPRED protein structure prediction server. Bioinformatics, 16, 404-405 (2000).
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 41
    • 28444469149 scopus 로고    scopus 로고
    • Evolutionary and mechanistic relationships between glycosidases acting on α- and β-bonds
    • Stam, M. R., Blanc, E., Coutinho, P. M., and Henrissat, B., Evolutionary and mechanistic relationships between glycosidases acting on α- and β-bonds. Carbohydr. Res., 340, 2728-2734 (2005).
    • (2005) Carbohydr. Res , vol.340 , pp. 2728-2734
    • Stam, M.R.1    Blanc, E.2    Coutinho, P.M.3    Henrissat, B.4


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