Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor.

@article{Labourier1998InteractionBT,
  title={Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor.},
  author={Emmanuel Labourier and Ferdinand Rossi and Imed-edine Gallouzi and Eric Allemand and Gilles Divita and Jamal Tazi},
  journal={Nucleic acids research},
  year={1998},
  volume={26 12},
  pages={2955-62}
}
Human DNA topoisomerase I, known for its DNA-relaxing activity, is possibly one of the kinases phosphorylating members of the SR protein family of splicing factors, in vivo. Little is known about the mechanism of action of this novel kinase. Using the prototypical SR protein SF2/ASF (SRp30a) as model substrate, we demonstrate that serine residues phosphorylated by topo I/kinase exclusively located within the most extended arginine-serine repeats of the SF2/ASF RS domain. Unlike other kinases… CONTINUE READING