Solubilization of neurospora crassa rodlet proteins and identification of the predominant protein as the proteolytically processed eas (ccg-2) gene product.

Proteins from conidial rodlet preparations of Neurospora crassa were solubilized in trifluoroacetic acid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized rodlets revealed a predominant protein of approximately 7 kDa. This protein was absent from preparations of N. crassa cultures carrying the eas mutation. The protein was purified by reverse-phase high-performance liquid chromatography and the N-terminal amino acid sequence of the purified protein was found to be identical to an internal portion of the deduced amino acid sequence of eas. Comparison of the sequences indicates a 29-amino-acid leader which is cleaved to generate the mature protein.