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pH-dependent changes in structure and RNA-binding activity of casein kinase 2 from Rana temporaria oocytes
K V Kandror1, D V Kapkov, O A Turapov
1A.N. Bakh Institute of Biochemistry, USSR Academy of Sciences, Moscow.
FEBS Letters
|June 3, 1991
Abstract:
It is demonstrated by filter-binding assay that casein kinase 2 from Rana temporaria oocytes binds rRNA in vitro with high affinity. Ligand-blotting shows that rRNA-binding activity is inherent to alpha and alpha' subunits of the enzyme. Increase of pH from 6.5 to 7.5 has little effect on casein kinase but completely suppresses rRNA-binding activity of the enzyme. Sedimentation coefficient of casein kinase 2 also depends on pH: at pH 7.5 it is mainly 10 S, and at pH 6.5-18 S. At pH 6.95 the amounts of both forms are equal. The heavy form of casein kinase 2 practically lacks rRNA-binding activity.