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Ras is a small GTPase that regulates numerous processes in the cellular development and morphogenesis of many organisms. In this study, we identified and functionally characterized the  Clg2p  gene of  Curvularia lunata , which is homologous with the Ras protein. The  Clg2p  deletion mutant (Δ Clg2p ) had altered appressorium formation and conidial morphology and produced fewer, smaller lesions compared with the wild-type strain. When a dominant  Clg2p  allele was introduced into the mutant, all of these defective phenotypes were completely restored. To further understand the regulation of  Clg2p  in appressorium formation and conidial morphology, and its role in pathogenicity, seven Clg2p-interacting proteins were screened using a yeast two-hybrid assay. Two of these proteins, Clf, a homologue of Mst11, which corresponds to MAP kinase kinase kinase in  Magnaporthe oryzae , and urate oxidase (designated ClUrase) were functionally characterized. Clg2p specifically interacted with Clf through its RA domain to regulate appressorium formation and pathogenicity, whereas the Clg2p-ClUrase interaction regulated conidial morphology without affecting fungal pathogenicity. This report is the first to elucidate the regulatory mechanism of the key Ras protein Clg2p in  C. lunata.

Clg2p interacts with Clf and ClUrase to regulate appressorium formation, pathogenicity and conidial morphology in Curvularia lunata