CARBON REGULATION OF THE CUTICLE-DEGRADING ENZYME PR1 FROM METARHIZIUM-ANISOPLIAE MAY INVOLVE A TRANS-ACTING DNA-BINDING PROTEIN CRR1, A FUNCTIONAL EQUIVALENT OF THE ASPERGILLUS-NIDULANS CREA PROTEIN

The pr1 gene of the entomopathogenic fungus Metarhizium anisopliae enc odes a serine protease that is highly active towards the insect cuticl e and whose synthesis is subject to both carbon and nitrogen repressio n. The prl promoter region was sequenced revealing the presence of put ative CREA- and AREA-binding sites. In vitro bandshift experiments dem onstrated that an Aspergillus nidulans GST-CREA fusion protein was cap able of binding to two of the three putative CREA sites. Using a PCR-b ased strategy the M. anisopliae crr1 gene was identified; it encodes a putative C2H2-type DNA-binding protein with significant sequence simi larity to A. nidulans CREA. Complementation experiments with an A. nid ulans strain carrying creA204 demonstrated that CRR1 can partially sub stitute for CREA function.