Nucleic Acids Research, Vol 26, Issue 16 3854-3861, Copyright © 1998 by Oxford University Press
Y Yamaguchi, T Wada, F Suzuki, T Takagi, J Hasegawa and H Handa
Casein kinase II (CKII) is thought to regulate a broad range of
transcription factors, but its mode of action is not well characterized. We
previously showed that CKII is co-purified with the ATF family of
transcription factors using DNA-affinity latex beads. Here we report a
functional and physical interaction between CKII and transcription factors.
We demonstrate that CKII binds through its catalytic alpha and alpha'
subunits to the basic leucine zipper (bZIP) DNA-binding domains of many
transcription factors, including ATF1. Kinetic analysis using a surface
plasmon resonance sensor suggests that CKII loosely associates with ATF1 in
vivo . Deletion of the bZIP domain of ATF1 markedly reduces its
phosphorylation by CKII, suggesting that the bZIP recruits CKII to the
vicinity of the target site. ATF1-CKII complex is also formed on DNA. Using
CKIIalpha fusedto a heterologous DNA-binding domain, we also demonstrate
that CKII, when bound to DNA, efficiently phosphorylates its substrate,
which is bound to the same DNA molecule. Taken together, CKII may regulate
transcription (and possibly other events) by phosphorylating proteins on
DNA.
ARTICLES
Casein kinase II interacts with the bZIP domains of several transcription factors
Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku,Yokohama 226-8501, Japan.
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