Current Genetics

, Volume 20, Issue 4, pp 301–307

Identification and characterization of a second polygalacturonase gene of Aspergillus niger

  • H. J. D. Bussink
  • K. B. Brouwer
  • L. H. de Graaff
  • H. C. M. Kester
  • J. Visser
Original Articles

DOI: 10.1007/BF00318519

Cite this article as:
Bussink, H.J.D., Brouwer, K.B., de Graaff, L.H. et al. Curr Genet (1991) 20: 301. doi:10.1007/BF00318519

Summary

The filamentous fungus Aspergillus niger produces several endopolygalacturonases that are involved in the degradation of pectin. PGI, the enzyme representing the second most abundant activity in a commmercial enzyme preparation, was further characterized and the corresponding gene was isolated. The nucleotide sequence of the pgaI gene was determined and the protein coding region was found to be interrupted by two short introns, one of which has a unusual donor splice site. The deduced 368 amino acids long protein with a putative prepropeptide of 31 amino acids shows 60% sequence identity to PGII in the mature protein. PGI overproducting A. niger strains were obtained by contransformation with the cloned gene.

Key words

Pectin degradationFilamentous fungusIntronsOverexpression

Copyright information

© Springer-Verlag 1991

Authors and Affiliations

  • H. J. D. Bussink
    • 1
  • K. B. Brouwer
    • 1
  • L. H. de Graaff
    • 1
  • H. C. M. Kester
    • 1
  • J. Visser
    • 1
  1. 1.Section of Molecular Genetics, Department of GeneticsAgricultural UniversityWageningenThe Netherlands