SOLUBILIZATION OF NEUROSPORA-CRASSA RODLET PROTEINS AND IDENTIFICATION OF THE PREDOMINANT PROTEIN AS THE PROTEOLYTICALLY PROCESSED EAS (CCG-2) GENE-PRODUCT
Md. Templeton et al., SOLUBILIZATION OF NEUROSPORA-CRASSA RODLET PROTEINS AND IDENTIFICATION OF THE PREDOMINANT PROTEIN AS THE PROTEOLYTICALLY PROCESSED EAS (CCG-2) GENE-PRODUCT, Experimental mycology, 19(2), 1995, pp. 166-169
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.