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Control of glucosylceramide production and morphogenesis by the Bar1 ceramide synthase in Fusarium graminearum.


ABSTRACT: The contribution of plasma membrane proteins to the virulence of plant pathogenic fungi is poorly understood. Accordingly, the objective of this study was to characterize the acyl-CoA dependent ceramide synthase Bar1 (previously implicated in plasma membrane organization) in the wheat pathogen Fusarium graminearum. The role of Bar1 in mediating cell membrane organization was confirmed as ?BAR1 mutants failed to display a distinct sterol-rich domain at the hyphal tip. The ?BAR1 mutants were non-pathogenic when inoculated onto wheat heads, and their in vitro growth also was severely perturbed. ?BAR1 mutants were incapable of producing perithecia (sexual fruiting structures) and only produced macroconidia (asexual spores) in the presence of NaCl. Sphingolipid analyses indicated that Bar1 is specifically necessary for the production of glucosylceramides in both F. graminearum and Aspergillus nidulans. Interestingly, glucosylceramides appear to mediate sensitivity to heat stable antifungal factor (HSAF), as, in addition to ?BAR1 mutants, a glucosylceramide synthase deficient mutant of Yarrowia lipolytica is also resistant to HSAF.

SUBMITTER: Rittenour WR 

PROVIDER: S-EPMC3084840 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Control of glucosylceramide production and morphogenesis by the Bar1 ceramide synthase in Fusarium graminearum.

Rittenour William R WR   Chen Ming M   Cahoon Edgar B EB   Harris Steven D SD  

PloS one 20110429 4


The contribution of plasma membrane proteins to the virulence of plant pathogenic fungi is poorly understood. Accordingly, the objective of this study was to characterize the acyl-CoA dependent ceramide synthase Bar1 (previously implicated in plasma membrane organization) in the wheat pathogen Fusarium graminearum. The role of Bar1 in mediating cell membrane organization was confirmed as ΔBAR1 mutants failed to display a distinct sterol-rich domain at the hyphal tip. The ΔBAR1 mutants were non-p  ...[more]

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