Identification and isolation of actin from Neurospora crassa.
Crude cell extracts of Neurospora crassa contained an abundant protein that was identified as actin by a number of criteria. The protein, either in cell extracts or in pure form, co-migrated with rabbit skeletal muscle actin in polyacrylamide gels. The N. crassa actin was purified by DEAE-cellulose and DNAase I-Sepharose chromatography and had the expected property of inhibiting DNAase I activity. Although N. crassa actin could polymerize and depolymerize, purification based entirely on this characteristic was ineffective. The actin was susceptible to proteolytic degradation, and under certain conditions, a breakdown product of defined size was observed.
D000199:Actins / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D002848:Chromatography, DEAE-Cellulose; D003850:Deoxyribonuclease I; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors; D004720:Endonucleases / Q000037:antagonists & inhibitors; D009491:Neurospora / Q000032:analysis*; D009492:Neurospora crassa / Q000032:analysis*; D011108:Polymers
D000199:Actins; D011108:Polymers; D003851:Deoxyribonucleases; D004720:Endonucleases; D003850:Deoxyribonuclease I