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Vol. 12, No. 14, pp. 2188-2199, July 15, 1998
1 Wellcome Trust/Cancer Research Campaign
Institute of Cancer and Developmental Biology and Department of
Zoology, Cambridge University, Cambridge CB2 1QR, UK;
2 Division Biochemistry of the Cell, German Cancer Research
Centre, D-69009 Heidelberg, Germany
DNA-dependent protein kinase (DNA-PK), which is involved in DNA
double-strand break repair and V(D)J recombination, is
comprised of a DNA-targeting component termed Ku and an ~465-kD
catalytic subunit, DNA-PKcs. Although DNA-PK phosphorylates
proteins in the presence of DSBs or other discontinuities in the DNA
double helix in vitro, the possibility exists that it is also activated in other circumstances via its association with additional proteins. Here, through use of the yeast two-hybrid screen, we discover that the
recently identified high affinity DNA binding protein C1D interacts
with the putative leucine zipper region of DNA-PKcs. Furthermore, we show that C1D can interact with DNA-PK in mammalian cells and that C1D is a very effective DNA-PK substrate in vitro. Finally, we establish that C1D directs the activation of DNA-PK in a
manner that does not require DNA termini. Therefore, these studies
provide a function for C1D and suggest novel mechanisms for DNA-PK
activation in vivo.
[Key Words: DNA-PK; DNA repair; recombination; C1D; nuclear matrix]
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