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 s olubilized in trifluoroacetic acid. Sodium dodecyl sulfate-polyacrylam ide gel electrophoresis of solubilized rodlets revealed a predominant protein of approximately 7 kDa. This protein was absent from preparati ons of N. crassa cultures carrying the eas mutation. The protein was p urified by reverse-phase high-performance liquid chromatography and th e 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. (C) 1995 Academic Pre ss, Inc.