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Genetics, Vol. 157, 591-600, February 2001, Copyright © 2001

Genetic Involvement of a cAMP-Dependent Protein Kinase in a G Protein Signaling Pathway Regulating Morphological and Chemical Transitions in Aspergillus nidulans

Kiminori Shimizua and Nancy P. Kellera
a Department of Plant Pathology and Microbiology, Texas A&M University, College Station, Texas 77843-2132

Corresponding author: Nancy P. Keller, 882 Russell Labs, Department of Plant Pathology, 1630 Linden Dr., University of Wisconsin, Madison, WI 53706., npk{at}plantpath.wisc.edu (E-mail)

Communicating editor: M. E. ZOLAN

In the filamentous fungus Aspergillus nidulans, a heterotrimeric G protein {alpha}-subunit and an RGS domain protein, encoded by fadA and flbA, respectively, regulate production of the carcinogenic metabolite sterigmatocystin (ST) and asexual spores (i.e., conidia). We investigated the genetic involvement of the cAMP-dependent protein kinase catalytic subunit (PkaA), a potential downstream target of FadA activity, in ST production and conidiation. Relative to wild type, sporulation was decreased in the pkaA overexpression strain but was not totally absent, as occurs in {Delta}flbA or fadAG42R (fadA-dominant active) strains. Deletion of pkaA resulted in a hyper-conidiating strain with limited radial growth. This phenotype was epistatic to mutation in flbA or fadA; the double mutants {Delta}pkaA; {Delta}flbA and {Delta}pkaA; fadAG42R recovered sporulation and their radial growth was severely restricted. PkaA overexpression also negatively regulated AflR, the ST biosynthesis-specific transcription factor, both transcriptionally and post-transcriptionally. Deletion of pkaA restored ST production in the {Delta}flbA background but not in the fadAG42R background. These data provide genetic evidence that the FlbA/FadA signaling pathway regulating ST production and morphological development is partially mediated through PkaA.




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