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.
Templeton
M D
MD
Molecular Genetics Group, Horticulture and Food Research Institute of New Zealand.
Greenwood
D R
DR
Beever
R E
RE
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D015870:Gene Expression; D008969:Molecular Sequence Data; D009492:Neurospora crassa / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013172:Spores, Fungal / Q000737:chemistry
D005656:Fungal Proteins; D010450:Endopeptidases