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Eukaryotic Cell, June 2009, p. 867-876, Vol. 8, No. 6
1535-9778/09/$08.00+0 doi:10.1128/EC.00048-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907,1 Biotech Center and College of Plant Protection, Northwest A&F University, Yangling, Shaanxi 712100, China,2 Department of Biology, University of Saskatchewan, 112 Science Place, Saskatoon, SK S7N 5E2, Canada,3 USDA Agricultural Research Service, Cereal Disease Laboratory, Department of Plant Pathology, University of Minnesota, St. Paul, Minnesota 551084
Received 11 February 2009/ Accepted 1 April 2009
Fusarium head blight caused by Fusarium graminearum is an important disease of wheat and barley. In a previous study, we identified several mutants with reduced virulence by insertional mutagenesis. A transducin beta-like gene named FTL1 was disrupted in one of these nonpathogenic mutants. FTL1 is homologous to Saccharomyces cerevisiae SIF2, which is a component of the Set3 complex involved in late stages of ascospore formation. The
ftl1 mutant was significantly reduced in conidiation and failed to cause typical disease symptoms. It failed to colonize the vascular tissues of rachis or cause necrosis on the rachis of inoculated wheat heads. The
ftl1 mutant also was defective in spreading from infected anthers to ovaries and more sensitive than the wild type to plant defensins MsDef1 and osmotin. However, the activation of two mitogen-activated protein kinases, Mgv1 and Gpmk1, production of deoxynivalenol, and expression of genes known to be important for plant infection in F. graminearum were not affected, indicating that the defect of the
ftl1 mutant in plant infection is unrelated to known virulence factors in this pathogen and may involve novel mechanisms. The
ftl1 deletion mutant was significantly reduced in histone deacetylation, and many members of the yeast Set3 complex are conserved in F. graminearum. FTL1 appears to be a component of this well-conserved protein complex that plays a critical role in the penetration and colonization of wheat tissues.
Published ahead of print on 17 April 2009.
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