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Current Genetics

, Volume 40, Issue 1, pp 40–48 | Cite as

Cloning and disruption of a phenylalanine ammonia-lyase gene from Ustilago maydis

  • Seong Kim
  • Divya Virmani
  • Katherine Wake
  • Kim MacDonald
  • James W. Kronstad
  • Brian E. Ellis
Research Article

Abstract

The enzyme L-phenylalanine ammonia-lyase (PAL) catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and ammonia. This enzyme is universally present in higher plants and it catalyzes the starting reaction for a central pathway that generates hundreds of different phenylpropanoid metabolites. Genes encoding PAL have been identified in fungi, but the role of the enzyme has not been determined. We cloned and characterized a gene that encodes PAL from the phytopathogenic fungus Ustilago maydis and we constructed fungal strains carrying a null mutation in the gene. These mutants behaved like wild-type strains in terms of growth, mating, and pathogenicity. These results indicate that PAL does not play a major role in the life cycle of U. maydis under laboratory conditions.

Ustilago maydis Phenylpropanoid metabolism 

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Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  • Seong Kim
    • 2
  • Divya Virmani
    • 1
  • Katherine Wake
    • 1
  • Kim MacDonald
    • 1
  • James W. Kronstad
    • 1
  • Brian E. Ellis
    • 1
  1. 1.Biotechnology Laboratory, University of British Columbia, 2357 Main Mall, Vancouver V6T 1Z4, British ColumbiaCanada
  2. 2.Chair of Forest Products Biotechnology, Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver V6T 1Z4, British ColumbiaCanada

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