Nucleic Acids Research, Vol 27, Issue 2 643-648, Copyright © 1999 by Oxford University Press
C Bachmeyer, CH Mak, CY Yu and LC Wu
The DNA binding protein KRC (forkappaB binding andrecognitioncomponent of
the V(D)J recombination signal sequence) belongs to a family of large zinc
finger proteins that bind to the kappaB motif and contains two widely
separated DNA binding structures. In addition to the kappaB motif, KRC
fusion proteins bind to the signal sequences of V(D)J recombination to form
highly ordered complexes. Here, we report that KRC may be regulated by
post-translational modifications. Specific protein kinases present in the
nucleus of pre-B cells phosphorylated a KRC fusion protein at tyrosine and
serine residues. Such protein modifications increased DNA binding, thereby
providing a mechanism by which KRC responds to signal transduction
pathways. KRC is a substrate of epidermal growth factor receptor kinase and
P34cdc2 kinase in vitro. Our results suggest that activation of the KRC
family of transcription factors may provide a mechanism by which oncogenic
tyrosine kinases regulate genes with kappaB-controlled gene regulatory
elements.
ARTICLES
Regulation by phosphorylation of the zinc finger protein KRC that binds the kappaB motif and V(D)J recombination signal sequences
Department of Internal Medicine and Department of Medical Biochemistry, Ohio State University, Columbus, OH 43210, USA.
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