Nucleic Acids Research, Vol 24, Issue 5 876-884, Copyright © 1996 by Oxford University Press
T Wada, T Takagi, Y Yamaguchi, H Kawase, M Hiramoto, A Ferdous, M Takayama, KA Lee, HC Hurst and H Handa
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. We found that the kinase interacted with ATF1 in
vitro efficiently. The kinase did not bind directly to DNA. The kinase
mainly phosphorylated ATF1 on serine 36, which was one of target amino
acids for casein kinase (CK) II. Biological features of the kinase were the
same as those of CKII and an anti-CKII serum reacted with the kinase,
indicating that the kinase was CKII. Moreover, it was clearly shown that
one of CKII subunits, the CKII alpha protein bound to glutathione-
S-transferase (GST) fusion ATF1 but not GST in vitro. It has been reported
that a specific CKII inhibitor, 5,6-dichloro-1-beta-D-ribo-
furanosylbenzimidazole (DRB) inhibits transcription by RNA polymerase II
[Zandomeni et al., (1986) J. Biol. Chem. 261, 3414-3419]. Taken together,
these results suggest that ATF/E4TF3 may recruit the CKII activity to a
transcription initiation machinery and stimulate transcription.
ARTICLES
Copurification of casein kinase II with transcription factor ATF/E4TF3
Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan.
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