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Characterization of the Role of the FluG Protein in Asexual Development of Aspergillus nidulans
Cletus A. D'Souzaa, Bee Na Leea, and Thomas H. Adamsaa Department of Biology, Texas A&M University, College Station, Texas 77843
Corresponding author: Cletus A. D'Souza, Rm. 320, CARL Bldg., Box 3546, Department of Genetics, Duke University Medical Center, Durham, NC 27710., dsouz003{at}mc.duke.edu (E-mail)
Communicating editor: J. J. LOROS
fluG mutation results in a block in Aspergillus nidulans asexual sporulation and that overexpression of fluG activates sporulation in liquid-submerged culture, a condition that does not normally support sporulation of wild-type strains. Here we demonstrate that the entire N-terminal region of FluG (
400 amino acids) can be deleted without affecting sporulation, indicating that FluG activity resides in the C-terminal half of the protein, which bears significant similarity with GSI-type glutamine synthetases. While FluG has no apparent role in glutamine biosynthesis, we propose that it has an enzymatic role in sporulation factor production. We also describe the isolation of dominant suppressors of fluG(dsg) that should identify components acting downstream of FluG and thereby define the function of FluG in sporulation. The dsgA1 mutation also suppresses the developmental defects resulting from flbA and dominant activating fadA mutations, which both cause constitutive induction of the mycelial proliferation pathway. However, dsgA1 does not suppress the negative influence of these mutations on production of the aflatoxin precursor, sterigmatocystin, indicating that dsgA1 is specific for asexual development. Taken together, our studies define dsgA as a novel component of the asexual sporulation pathway.
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