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Original Articles

Cloning and Expression of 1,2-α-Mannosidase Gene (fmanIB) from Filamentous Fungus Aspergillus oryzae: in Vivo Visualization of the FmanIBp-GFP Fusion Protein

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Pages 471-479 | Received 26 Aug 2005, Accepted 04 Nov 2005, Published online: 22 May 2014

  • 1) Herscovics, A., Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim. Biophys. Acta, 1473, 96–107 (1999).
  • 2) Moremen, K., Trimble, R., and Herscovics, A., Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology, 4, 113–125 (1994).
  • 3) Yoshida, T., Inoue, T., and Ichishima, E., 1,2-α-Mannosidase from Penicillium citrinum: molecular and enzymic properties of two isoenzymes. Biochem. J., 290, 349–354 (1993).
  • 4) Yoshida, T., and Ichishima, E., Molecular cloning and nucleotide sequence of the genomic DNA for 1,2-α-mannosidase gene, msdC from Penicillium citrinum. Biochim. Biophys. Acta, 1263, 159–162 (1995).
  • 5) Inoue, T., Yoshida, T., and Ichishima, E., Molecular cloning and nucleotide sequence of the 1,2-α-mannosidase gene, msdS, from Aspergillus saitoi and expression of the gene in yeast cells. Biochim. Biophis. Acta, 1253, 141–145 (1995).
  • 6) Eades, C. J., and Hintz, W. E., Characterization of the class I α-mannosidase gene family in the filamentous fungus Aspergillus nidulans. Gene, 255, 25–34 (2000).
  • 7) Maras, M., Callewaert, N., Piens, K., Claeyssens, M., Martinet, W., Dewaele, S., Contreras, H., Dewerte, I., Penttila, M., and Contreras, R., Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-α-D-mannosidase. J. Biotechnol., 77, 255–263 (2000).
  • 8) Ichishima, E., Taya, N., Ikeguchi, M., Chiba, Y., Nakamura, M., Kawabata, C., Inoue, T., Takahashi, K., Minetoki, T., Ozeki, K., Kumagai, C., Gomi, K., Yoshida, T., and Nakajima, T., Molecular and enzymic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells. Biochem. J., 339, 589–597 (1999).
  • 9) Yamamoto, K., Hitomi, J., Kobatake, K., and Yamaguchi, H., Purification and characterization of 1,2-α-mannosidase of Aspergillus oryzae. J. Biochem., 91, 1971–1979 (1982).
  • 10) Yoshida, T., Nakajima, T., and Ichishima, E., Overproduction of 1,2-α-mannosidase, a glycoprotein processing enzyme, by Aspergillus oryzae. Biosci. Biotechnol. Biochem., 62, 309–315 (1998).
  • 11) Lovsanov, Y. D., Vallee, F., Imberty, A., Yoshida, T., Yip, P., Herscovics, A., and Howell, P. L., Structure of Penicillium citrinum α1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes. J. Biol. Chem., 277, 5620–5630 (2002).
  • 12) Tsuchiya, K., Nagashima, T., Yamamoto, Y., Gomi, K., Kitamoto, K., Kumagai, C., and Tamura, G., High level secretion of calf chymosin using a glucoamylase-prochymosin fusion gene in Aspergillus oryzae. Biosci. Biotechnol. Biochem., 58, 895–899 (1994).
  • 13) Hata, Y., Ishida, H., Kojima, Y., Ichikawa, E., Kawato, A., Suhinami, K., and Imayasu, S., Comparison of two glucoamylases produced by Aspergillus oryzae in solid-state culture (koji) and submerged culture. J. Ferment. Bioeng., 84, 532–537 (1997).
  • 14) Akao, T., Gomi, K., Goto, K., Okazaki, N., and Akita, O., Subtractive cloning of cDNA from Aspergillus oryzae differentially regulated between solid-state culture and liquid (submerged) culture. Curr. Genet., 41, 275–281 (2002).
  • 15) Yamada, O., Na, Nah S., Akao, T., Tominaga, M., Watanabe, H., Satoh, T., Enei, H., and Akita, O., dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis. J. Biosci. Bioeng., 95, 82–88 (2003).
  • 16) Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265–275 (1951).
  • 17) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680–685 (1970).
  • 18) Park, J. T., and Johnson, M. J., A submicro determination of glucose. J. Biol. Chem., 181, 149–151 (1949).
  • 19) Yamada, O., Lee, B. R., Gomi, K., and Iimura, Y., Cloning and functional analysis of the Aspergillus oryzae conidiation regulator gene brlA by its disruption and misscheduled expression. J. Biosci. Bioeng., 87, 424–429 (1999).
  • 20) Wedlich-Soldner, R., Schulz, I., Straube, A., and Steinberg, G., Dynein supports motility of endoplasmic reticulum in the fungus Ustilago maydis. Mol. Biol. Cell, 13, 965–977 (2002).
  • 21) Herscovics, A., Processing glycosidases of Saccharomyces cerevisiae. Biochim. Biophys. Acta, 1426, 275–285 (1999).
  • 22) Lipari, F., and Herscovics, A., Production, purification and characterization of recombinant yeast processing α1,2-mannosidase. Glycobiology, 4, 679–702 (1994).
  • 23) Lal, A., Pang, P., Kalelker, S., Romero, P. A., Herscivics, A., and Moremen, K. W., Substrate specificities of recombinant murine Golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing α1,2-mannosidases. Glycobiology, 8, 981–995 (1998).
  • 24) Fernandez-Abalos, J. M., Fox, H., Pitt, C., Wells, B., and Doonan, J. H., Plant-adapted green fluorescent protein is a versatile vital reporter for gene expression, protein localization and mitosis in the filamentous fungus, Aspergillus nidulans. Mol. Microbiol., 27, 121–130 (1998).
  • 25) Maruyama, J., Nakajima, H., and Kitamoto, K., Observation of EGFP-visualized nuclei and distribution of vacuoles in Aspergillus oryzae arpA null mutant. FEMS Microbiol. Lett., 206, 57–61 (2002).
  • 26) Gordon, C. L., Khalaj, V., Ram, A. F., Archer, D. B., Brookman, J. L., Trinci, A. P., Jeenes, D. J., Doonan, J. H., Wells, B., Punt, P. J., van den Hondel, C. A., and Robson, G. D., Glucoamylase::green fluorescent protein fusions to monitor protein secretion in Aspergillus niger. Microbiology, 146, 415–426 (2000).
  • 27) Masai, K., Maruyama, J., Nakajima, H., and Kitamoto, K., In vivo visualization of the distribution of a secretory protein in Aspergillus oryzae hyphae using the RntA-EGFP fusion protein. Biosci. Biotechnol. Biochem., 67, 455–459 (2003).
  • 28) Masai, K., Maruyama, J., Nakajima, H., and Kitamoto, K., Effects of protein transport inhibitors on the distribution and secretion of the fusion protein RntA-EGFP in Aspergillus oryzae. Biosci. Biotechnol. Biochem., 68, 1569–1573 (2004).
  • 29) Peberdy, J. F., Protein secretion in filamentous fungi:trying to understand a highly productive black box. Trends Biotechnol., 12, 50–57 (1994).
  • 30) Eneyskaya, E. V., Kulminskaya, A. A., Savel’ev, A. N., Shabalin, K. A., Golubev, A. M., and Neustroev, K. N., α-Mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins. Biochem. Biophys. Res. Commun., 245, 43–49 (1998).
  • 31) Herscovics, A., Structure and function of Class I α1,2-mannosidases involved in glycoprotein synthesis and endoplasmic reticulum quality control. Biochimie, 83, 757–762 (1998).
  • 32) Yoshida, T., Kato, Y., Asada, Y., and Nakajima, T., Filamentous fungus Aspergillus oryzae has two types of α-1,2-mannosidases, one of which is a microsomal enzyme that removes a single mannose residue from Man9GlcNAc2. Glycoconj. J., 17, 745–748 (2000).
  • 33) Tatara, Y., Lee, B. R., Yoshida, T., Takahashi, K., and Ichishima, E., Identification of catalytic residues of Ca2+-independent 1,2-α-D-mannosidase from Aspergillus saitoi by site-directed mutagenesis. J. Biol. Chem., 278, 25289–25294 (2003).

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