pH-dependent changes in structure and RNA-binding activity of casein kinase 2 from Rana temporaria oocytes.
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.
Kandror
K V
KV
A.N. Bakh Institute of Biochemistry, USSR Academy of Sciences, Moscow.
Kapkov
D V
DV
Turapov
O A
OA
Stepanov
A S
AS
D000818:Animals; D047388:Casein Kinases; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009865:Oocytes / Q000201:enzymology*; D011485:Protein Binding; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D012335:RNA, Ribosomal / Q000378:metabolism*; D011896:Rana temporaria
D046911:Macromolecular Substances; D012335:RNA, Ribosomal; D011494:Protein Kinases; D047388:Casein Kinases