A novel stimulator of protein phosphorylation in Neurospora crassa

An endogenous thermostable activator of Protein kinase III (PKIII) was purified from 100000 × g supernatants of Neurospora 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...

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Detalles Bibliográficos
Autores principales: Ulloa, R.M., Glikin, G.C., Téllez-Ĩnón, M.T., Torres, H.N., Judewicz, N.D.
Formato: JOUR
Materias:
Neurospora crassa
protein kinase regulation
fungal protein
protein kinase
article
enzyme activation
enzymology
gel chromatography
growth, development and aging
kinetics
metabolism
molecular weight
Neurospora
phosphorylation
Chromatography, Gel
Enzyme Activation
Fungal Proteins
Kinetics
Molecular Weight
Phosphorylation
Protein Kinases
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03008177_v77_n1_p11_Ulloa
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:An endogenous thermostable activator of Protein kinase III (PKIII) was purified from 100000 × g supernatants of Neurospora 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. © 1987 Martinus Nijhoff Publishers.

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