The global regulator FfSge1 is required for expression of secondary metabolite gene clusters but not for pathogenicity in Fusarium fujikuroi.

The plant pathogenic fungus Fusarium fujikuroi is the causal agent of bakanae disease on rice due to its ability to produce gibberellins. Besides these phytohormones, F. fujikuroi is able to produce several other secondary metabolites (SMs).

Characterization of the fusaric acid gene cluster in Fusarium fujikuroi.

The "bakanae" fungus Fusarium fujikuroi is a common pathogen of rice and produces a variety of mycotoxins, pigments, and phytohormones. Fusaric acid is one of the oldest known secondary metabolites produced by F. fujikuroi and some other Fusarium species.

Deciphering the cryptic genome: genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites.

The fungus Fusarium fujikuroi causes "bakanae" disease of rice due to its ability to produce gibberellins (GAs), but it is also known for producing harmful mycotoxins. However, the genetic capacity for the whole arsenal of natural compounds and their role in the fungus' interaction with rice remained unknown. Here, we present a high-quality genome sequence of F.

The mitogen-activated protein kinase BcSak1 of Botrytis cinerea is required for pathogenic development and has broad regulatory functions beyond stress response.

The mitogen-activated protein kinase (MAPK) BcSak1 of Botrytis cinerea is activated upon exposure to H(2)O(2) and, hence, might be involved in coping with oxidative stress during infection. However, beside osmotic and oxidative stress sensitivity, Δbcsak1 mutants have a pleiotropic phenotype, as they do not produce conidia and are unable to penetrate unwounded host tissue. In this study, the role of BcSak1 was investigated in the stress response and during infection of French beans by Botrytis cinerea.

The Botrytis cinerea early secretome.

The extracellular proteome, or secretome, of phytopathogenic fungi is presumed to be a key element of their infection strategy. Especially interesting constituents of this set are those proteins secreted at the beginning of the infection, during the germination of conidia on the plant surfaces or wounds, since they may play essential roles in the establishment of a successful infection. We have germinated Botrytis cinerea conidia in conditions that resemble the plant environment, a synthetic medium enriched with low molecular weight plant compounds, and we have collected the proteins secreted during the first 16 h by a double precipitation protocol.

The Botrytis cinerea aspartic proteinase family.

The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice.

Drill-assisted genomic DNA extraction from Botrytis cinerea.

Current DNA extraction protocols for genomic DNA from Botrytis cinerea almost always start with mycelium that has been reduced to powder with liquid N(2) in a mortar, and this makes their application to a large number of samples slow and cumbersome. Here we present an adaptation of an existing method [Möller et al. (1992) Nucleic Acids Res 20: 6115-6116] for which the initial steps have been modified, including the homogenization of the fungus with sand and the aid of a common household drill.

Methodological improvements in the expression of foreign genes and in gene replacement in the phytopathogenic fungus Botrytis cinerea.

SUMMARY Genetic transformation is generally carried out in Botrytis cinerea by random integration of the foreign DNA into the genome, resulting in transformants that show differences among them in, for example, the expression of a reporter gene. Here we report a system for site-directed integration in which a novel recipient strain containing a 5'-truncated copy of the hygromycin resistance gene, hph, is transformed with a vector containing another truncated copy, now in the opposite end, of the same selection marker. Homologous recombination in the region shared by these two truncated copies of hph is the only way by which antibiotic-resistant transformants can be generated.

The endo-beta-1,4-xylanase xyn11A is required for virulence in Botrytis cinerea.

Phytopathogenic fungi can degrade xylan, an abundant hemicellulose in plant cell walls, by the coordinate action of a group of extracellular enzymes. Among these, endo-beta-1,4-xylanases carry out the initial breakdown by cleaving internal bonds in the polymer backbone. We have isolated and characterized a gene, xyn11A, coding for an endo-beta-1,4-xylanase belonging to family 11 of glycosyl hydrolases.