Structure and Properties of Casein Kinase IIs from Allomyces arbuscula Phosphorylating Serine Residues

Article Article scientifique Article Structure and Properties of Casein Kinase IIs from Allomyces arbuscula Phosphorylating Serine Residues eng 1994-12 author Ojha Mukti 25001 author Cattaneo Arlette 26052 author Norberg Wiveca 41254 349-362 10.1016/S0147-5975(06)80008-3 0147-5975 https://linkinghub.elsevier.com/retrieve/pii/S0147597506800083 Structure and properties of casein kinase Its from Allomyces arbuscula phosphorylating serine residues. Experimental Mycology 18, 349–362. Two casein kinase (CK) activities have been purified from the aquatic fungus Allomyces arbuscula and have been referred to as CK IIA and CK IIB. Both enzymes have the properties characteristic of animal and yeast casein kinase II, i.e., tetrameric holoenzyme, ability to use ATP as well as GTP as donor of phosphate group in phosphotransferase reactions, inhibition of kinase activity by heparin, and inability to use basic protein like histone H1 as substrate. The two enzymes differ from each other by their affinity to DE-52-cellulose, CK IIA does not bind to DE-52 while CK IIB does. The kinetic parameters of the two enzymes also differ. The Km of CK IIA has been found to be 7.7 μM, 20.83 μM, and 0.96 mM and that of CK IIB 22.2 νM, 41.7 ~LM, and 1.86 mM, for casein, ATP, and Mgt2+ , respectively. Both α and β subunits of CK IIA and CK IIB undergo autophosphorylation. Polylysine is inhibitory to autophosphorylation of a subunit whereas spermine, protamine, and histone H1 are stimulatory. Phosphoamino acid analysis showed that serine was the phospho-accepting amino acid. The phosphopeptide analysis showed that the trypsin recognition sites of the α and β subunits in CK IIA and CK IIB are different. Casein kinase IIA and IIB Phosphorylating serine residues Allomyces arbuscula CK, casein kinase Mops, 4-morpholine propane sulfonic acid EGTA, ethylene glycol bis BSA, bovine serum albumin PMSF, phenylmethylsulfonyl fluoride SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis Dewey 580 45 Département des sciences végétales 163 false Experimental mycology 18 4 a398a363-5fa3-4076-9c2e-17206614cd47 Article (Published version) Restricted Ojha_EM_199418349.pdf 2102105 application/pdf f576123a8fe40ca1f478dac308ba4fb2748ad4f9395222308003fb4cca976cbe restrictedAccess Faculté des sciences / Section de biologie / Département des sciences végétales

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Structure and Properties of Casein Kinase IIs from Allomyces arbuscula Phosphorylating Serine Residues	Experimental mycology			1994	18	0

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