A novel stimulator of protein phosphorylation in Neurospora crassa

ULLOA RM; GLIKIN GC; TÉLLEZ-IÑÓN MT; TORRES HN; JUDEWICZ ND

MOLECULAR AND CELLULAR BIOCHEMISTRY

Kluwer

Año: 1987 vol. 77 p. 11 - 17

0300-8177

An endogenous thermostable activator of Protein kinase III (PKIII) was purified from 100000 x g supernarants ofNeurospora crassa mycelial extracts. This 38 000 dalton polypeptide, clearly separable from calmodulin on P-60 gel filtration, specifically stimulated N. crassa PKIII activity on casein or phosvitin "in vitro" phosphorylation. The factor was only present in the initial growth phase of the fungus. The mechanism of PKIII activation and its possible regulatory role are discussed.mycelial extracts. This 38 000 dalton polypeptide, clearly separable from calmodulin on P-60 gel filtration, specifically stimulated N. crassa PKIII activity on casein or phosvitin "in vitro" phosphorylation. The factor was only present in the initial growth phase of the fungus. The mechanism of PKIII activation and its possible regulatory role are discussed.crassa PKIII activity on casein or phosvitin "in vitro" phosphorylation. The factor was only present in the initial growth phase of the fungus. The mechanism of PKIII activation and its possible regulatory role are discussed.