If you need an accessible version of this item please contact JSTOR User Support

MPG1 Encodes a Fungal Hydrophobin Involved in Surface Interactions during Infection-Related Development of Magnaporthe grisea

Nicholas J. Talbot, Michael J. Kershaw, Gavin E. Wakley, Onno M. H. de Vries, Joseph G. H. Wessels and John E. Hamer
The Plant Cell
Vol. 8, No. 6 (Jun., 1996), pp. 985-999
DOI: 10.2307/3870210
Stable URL: http://www.jstor.org/stable/3870210
Page Count: 15
  • Download PDF
  • Cite this Item

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If you need an accessible version of this item please contact JSTOR User Support
MPG1 Encodes a Fungal Hydrophobin Involved in Surface Interactions during Infection-Related Development of Magnaporthe grisea
Preview not available

Abstract

The rice blast fungus expresses a pathogenicity gene, MPG1, during appressorium formation, disease symptom development, and conidiation. The MPG1 gene sequence predicts a small protein belonging to a family of fungal proteins designated hydrophobins. Using random ascospore analysis and genetic complementation, we showed that MPG1 is necessary for infection-related development of Magnaporthe grisea on rice leaves and for full pathogenicity toward susceptible rice cultivars. The protein product of MPG1 appears to interact with hydrophobic surfaces, where it may act as a developmental sensor for appressorium formation. Ultrastructural studies revealed that MPG1 directs formation of a rodlet layer on conidia composed of interwoven ∼5-nm rodlets, which contributes to their surface hydrophobicity. Using combined genetic and biochemical approaches, we identified a 15-kD secreted protein with characteristics that establish it as a class I hydrophobin. The protein is able to form detergent-insoluble high molecular mass complexes, is soluble in trifluoroacetic acid, and exhibits mobility shifts after treatment with performic acid. The production of this protein is directed by MPG1.

Page Thumbnails

  • Thumbnail: Page 
[985]
    [985]
  • Thumbnail: Page 
986
    986
  • Thumbnail: Page 
987
    987
  • Thumbnail: Page 
[988]
    [988]
  • Thumbnail: Page 
989
    989
  • Thumbnail: Page 
990
    990
  • Thumbnail: Page 
991
    991
  • Thumbnail: Page 
[992]
    [992]
  • Thumbnail: Page 
993
    993
  • Thumbnail: Page 
994
    994
  • Thumbnail: Page 
995
    995
  • Thumbnail: Page 
996
    996
  • Thumbnail: Page 
997
    997
  • Thumbnail: Page 
998
    998
  • Thumbnail: Page 
999
    999