Nucleic acids can regulate the activity of casein kinase II

Casein kinase II purified from nuclei of Xenopus laevis oocytes is inhibited by several specific nucleic acids. This kinase, the main phosphorylating activity of the oocyte nucleus, is markedly inhibited by poly U at 10 μg/ml, and this polymer is a competitive inhibitor of the phosporylation of the...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1989-09, Vol.255 (2), p.414-418
Main Authors: Gatica, Marta, Allende, Catherine C., Allende, Jorge E.
Format: Article
Language:English
Subjects:
Animals
Casein Kinases
Deoxyribonucleases
DNA, single-stranded
DNA, Single-Stranded - pharmacology
DNA, Viral - pharmacology
Female
Kinetics
nucleic acids
Nucleus
oocytes
Oocytes - enzymology
Poly U
Poly U - pharmacology
Protein kinase
Protein Kinases - isolation & purification
Protein Kinases - metabolism
Ribonucleases
tRNA
Xenopus laevis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Casein kinase II purified from nuclei of Xenopus laevis oocytes is inhibited by several specific nucleic acids. This kinase, the main phosphorylating activity of the oocyte nucleus, is markedly inhibited by poly U at 10 μg/ml, and this polymer is a competitive inhibitor of the phosporylation of the substrate casein (Kiapp 80 nM). M 13 phage ssDNA and unfractionated yeast tRNA also inhibit between 50 and 200 μg/ml. Poly C, poly A, poly AG, dsDNA and Escherichia coli rRNA do not alter activity significantly at similar concentrations. Inhibitions are reversed by RNase (poly U, tRNA) or S 1 nuclease (ssDNA). Oocyte casein kinase I or rabbit cAMP-dependent protein kinase are not inhibited by poly U at 200 μg/ml. The sensitivity of the casein kinase II to these inhibitors suggests a regulatory role for nucleic acids in nuclear phosphorylation reactions.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81135-4