pH-dependent changes in structure and RNA-binding activity of casein kinase 2 from Rana temporaria oocytes.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kandror KV,Kapkov DV,Turapov OA,Stepanov AS

doi

10.1016/0014-5793(91)80593-r

subject

Has Abstract

pub_date

1991-06-03 00:00:00

pages

223-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80593-R

journal_volume

283

pub_type

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