Access

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 Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Sfp-Type 4'-Phosphopantetheinyl Transferase Is Indispensable for Fungal Pathogenicity

Ralf Horbach, Alexander Graf, Fabian Weihmann, Luis Antelo, Sebastian Mathea, Johannes C. Liermann, Till Opatz, Eckhard Thines, Jesús Aguirre and Holger B. Deising
The Plant Cell
Vol. 21, No. 10 (Oct., 2009), pp. 3379-3396
Stable URL: http://www.jstor.org/stable/40537513
Page Count: 18
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Sfp-Type 4'-Phosphopantetheinyl Transferase Is Indispensable for Fungal Pathogenicity
Preview not available

Abstract

In filamentous fungi, Sfp-type 4'-phosphopantetheinyl transferases (PPTases) activate enzymes involved in primary (α-aminoadipate reductase [AAR]) and secondary (polyketide synthases and nonribosomal peptide synthetases) metabolism. We cloned the PPTase gene PPT1 of the maize anthracnose fungus Colletotrich urn graminicola and generated PPTasedeficient mutants [Δppt1). Δppti strains were auxotrophic for Lys, unable to synthesize siderophores, hypersensitive to reactive oxygen species, and unable to synthesize polyketides (PKs). A differential analysis of secondary metabolites produced by wild-type and Δppt1 strains led to the identification of six novel PKs. Infection-related morphogenesis was affected in Δppt1 strains. Rarely formed appressoria of Δppt1 strains were nonmelanized and ruptured on intact plant. The hyphae of Δppt1 strains colonized wounded maize (Zea mays) leaves but failed to generate necrotic anthracnose disease symptoms and were defective in asexual sporulation. To analyze the pleiotropic pathogenicity phenotype, we generated AAR-deficient mutants (Δaar1) and employed a melanin-deficient mutant (M1.502). Results indicated that PPT1 activates enzymes required at defined stages of infection. Melanization is required for cell wall rigidity and appressorium function, and Lys supplied by the AAR1 pathway is essential for necrotrophic development. As PPTase-deficient mutants of Magnaporthe oryzea were also nonpathogenic, we conclude that PPTases represent a novel fungal pathogenicity factor.

Page Thumbnails

  • Thumbnail: Page 
[3379]
    [3379]
  • Thumbnail: Page 
3380
    3380
  • Thumbnail: Page 
3381
    3381
  • Thumbnail: Page 
3382
    3382
  • Thumbnail: Page 
3383
    3383
  • Thumbnail: Page 
3384
    3384
  • Thumbnail: Page 
3385
    3385
  • Thumbnail: Page 
3386
    3386
  • Thumbnail: Page 
3387
    3387
  • Thumbnail: Page 
3388
    3388
  • Thumbnail: Page 
3389
    3389
  • Thumbnail: Page 
3390
    3390
  • Thumbnail: Page 
3391
    3391
  • Thumbnail: Page 
3392
    3392
  • Thumbnail: Page 
3393
    3393
  • Thumbnail: Page 
3394
    3394
  • Thumbnail: Page 
3395
    3395
  • Thumbnail: Page 
3396
    3396