Phosphorylation of S-II, a eukaryotic transcription factor, by casein kinase II.

Phosphorylation of S-II, a eukaryotic transcription factor, by casein kinase II.

Recently, casein kinase II was suggested to play a role in accurate transcription in vitro (R. Zandomeni, M. C. Zandomeni, D. Shungar, and R. Weinmann, J. Biol. Chem., 261, 3414 (1986)). In the present study, we examined whether transcription factor S-II is a target of casein kinase II, because the phosphorylated form of S-II, termed S-II', is known to be present in vivo. We found that S-II was...

Copurification of casein kinase II with transcription factor ATF/E4TF3.

We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. W...

Regulation of topoisomerase II by phosphorylation: a role for casein kinase II.

Inhibition of casein kinase II by heparin.

Casein kinase II, a cyclic nucleotide-independent protein kinase from rabbit reticulocytes, was shown to be inhibited by heparin. Heparin specifically inhibited the enzyme and had no effect on other protein kinases, including casein kinase I, the type I and II cAMP-dependent protein kinases, protease-activated kinase I, and the hemin-controlled repressor. Heparan sulfate was found to be 40-fol...

Phosphorylation of Histone H4 Serine 1 during DNA Damage Requires Casein Kinase II in S. cerevisiae

Distinct patterns of posttranslational histone modifications can regulate DNA-templated events such as mitosis, transcription, replication, apoptosis, and DNA damage, suggesting the presence of a "histone code" in these nuclear processes. Phosphorylation of histone H2A S129 at sites of DNA double-strand breaks (DSBs) has been implicated in damage repair in yeast. Here, we describe another phosp...