Current Genetics

, Volume 42, Issue 1, pp 43–50 | Cite as

Isomaltose formed by α-glucosidases triggers amylase induction in Aspergillus nidulans

  • Naoki Kato
  • Yuriko Murakoshi
  • Masashi Kato
  • Tetsuo KobayashiEmail author
  • Norihiro Tsukagoshi
Research Article


Among various α-glucobioses examined, isomaltose was the most effective inducer for amylase synthesis in Aspergillus nidulans. Amylase induction by maltose was completely inhibited by addition of cast-anospermine or cycloheximide, while induction by isomaltose was not affected by the inhibitors, suggesting that amylase induction by maltose requires inducible α-glucosidases. Disruption of the α-glucosidase A gene (agdA), the α-glucosidase B gene (agdB), or both genes did not abolish maltose-dependent induction, although amylase production induced by maltose decreased about 2-fold in the agdA/agdB double disruptant, compared with that in the agdB disruptant at all concentrations tested. Upon induction by isomaltose, amylase synthesis was enhanced considerably in the agdB and agdA/agdB disruptants. Even at 3 nM, isomaltose induced amylase production in the double disruptant, supporting the suggestion that isomaltose is a physiological inducer for amylase. Therefore, maltose must be converted to isomaltose by α-glucosidases prior to triggering amylase synthesis, but no specific α-glucosidase is required for amylase induction by maltose. Probably any α-glucosidases having isomaltqse-forming activity, including AgdA and AgdB, may participate in amylase induction by maltose.


Aspergillus nidulans α-Glucosidase Isomaltose Amylase induction 


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  1. Ballance DJ, Turner G (1985) Development of a high-frequency transforming vector for Aspergillus nidulans. Gene 36:321–331PubMedCrossRefGoogle Scholar
  2. Blank TE, Woods MP, Lebo CM, Xin P, Hopper JE (1997) Novel Gal3 proteins showing altered Gal80p binding cause constitutive transcription of Gal4p-activated genes in Saccharomyces cerevisiae. Mol Cell Biol 17:2566–2575PubMedGoogle Scholar
  3. Chambers JP, Elbein AD (1986) Effects of castanospermine on purified lysosomal alpha-1,4-glucosidase. Enzyme 35:53–56PubMedGoogle Scholar
  4. Chiba S (1988) α-Glucosidases. In: Amylase Research Society of Japan (ed) Handbook of amylases and related enzymes. Pergamon, Oxford, pp 104–105Google Scholar
  5. Duan KJ, Sheu DC, Lin CT (1995) Transglucosylation of a fungal α-glucosidase. The enzyme properties and correlation of isomaltooligosaccharide production. Ann NY Acad Sci 750:325–328PubMedCrossRefGoogle Scholar
  6. Ellmers BR, Rhinehart BL, Robinson KM (1987) Castanospermine: an apparent tight-binding inhibitor of hepatic lysosomal alpha-glucosidase. Biochem Pharmacol 36:2381–2385PubMedCrossRefGoogle Scholar
  7. Flipphi M, Mathieu M, Cirpus I, Panozzo C, Felenbok B (2001) Regulation of the aldehyde dehydrogenase gene (aldA) and its role in the control of the coinducer level necessary for induction of the ethanol utilization pathway in Aspergillus nidulans. J Biol Chem 276:6950–6958PubMedCrossRefGoogle Scholar
  8. Gomi K et al (2000) Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae. Biosci Biotechnol Biochem 64:816–827PubMedCrossRefGoogle Scholar
  9. Hasper AA, Visser J, Graaff LH de (2000) The Aspergillus niger transcriptional activator XlnR, which is involved in the degradation of the polysaccharides xylan and cellulose, also regulates d-xylose reductase gene expression. Mol Microbiol 36:193–200PubMedCrossRefGoogle Scholar
  10. Kato M, Aoyama A, Naruse F, Kobayashi T, Tsukagoshi N (1997) An Aspergillus nidulans nuclear protein, AnCP, involved in enhancement of Taka-amylase A gene expression, binds to the CCAAT-containing taaG2, amdS, and gatA promoters. Mol Gen Genet 254:119–126PubMedCrossRefGoogle Scholar
  11. Kato N, Suyama S, Shirokane M, Kato M, Kobayashi T, Tsukagoshi N (2002) Novel α-glucosidase from Aspergillus nidulans with strong transglycosylation activity. Appl Environ Microbiol 68:1250–1256PubMedCrossRefGoogle Scholar
  12. Kita A, Matsui H, Somoto A, Kimura A, Takata M, Chiba S (1991) Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger. Agric Biol Chem 55:2327–2335Google Scholar
  13. Mala S, Dvorakova H, Hrabal R, Kralova B (1999) Towards regioselective synthesis of oligosaccharides by use of α-glucosidases with different substrate specificity. Carbohydr Res 322:209–218.PubMedCrossRefGoogle Scholar
  14. McCleary BV, Gibson TS (1989) Purification, properties, and industrial significance of transglucosidase from Aspergillus niger. Carbohydr Res 185:147–162CrossRefGoogle Scholar
  15. Nelson N (1944) A photometric adaptation of the Somogyi method for the determination of glucose. J Biol Chem 153:375–380Google Scholar
  16. Osmani AH, May GS, Osmani SA (1999) The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers. J Biol Chem 274:23565–23569PubMedCrossRefGoogle Scholar
  17. Pazur JH, Cepure A, Okada S, Forsberg LS (1977) Comparison of the action of glucoamylase and glucosyltransferase on d-glucose, maltose, and malto-oligosaccharides. Carbohydr Res 58:193–202PubMedCrossRefGoogle Scholar
  18. Peng G, Hopper JE (2000) Evidence for Gal3p’s cytoplasmic location and Gal80p’s dual cytoplasmic-nuclear location implicates new mechanisms for controlling Gal4p activity in Saccharomyces cerevisiae. Mol Cell Biol 20:5140–5148PubMedCrossRefGoogle Scholar
  19. Petersen KL, Lehmbeck J, Christensen T (1999) A new transcriptional activator for amylase genes in Aspergillus. Mol Gen Genet 262:668–676PubMedCrossRefGoogle Scholar
  20. Rowlands RT, Turner G (1973) Nuclear and extranuclear inheritance of oligomycin resistance in Aspergillus nidulans. Mol Gen Genet 126:201–216PubMedCrossRefGoogle Scholar
  21. Tani S et al (2001) Characterization of the amyR gene encoding a transcriptional activator for the amylase genes in Aspergillus nidulans. Curr Genet 39:10–15PubMedCrossRefGoogle Scholar
  22. Tonomura K, Suzuki H, Nakamura N, Kuraya K, Tanabe O (1961) On the inducers of α-amylase formation in Aspergillus oryzae. Agric Biol Chem 25:1–6Google Scholar
  23. Tsukagoshi N, Furukawa M, Nagaba H, Kirita N, Tsuboi A, Udaka S (1989) Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence for multiple related genes. Gene 84:319–327PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2002

Authors and Affiliations

  • Naoki Kato
    • 1
  • Yuriko Murakoshi
    • 1
  • Masashi Kato
    • 1
  • Tetsuo Kobayashi
    • 1
    Email author
  • Norihiro Tsukagoshi
    • 1
  1. 1.Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural SciencesNagoya UniversityNagoyaJapan

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