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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Doxorubicin Binds to Un-phosphorylated Form of hNopp140 and Reduces Protein Kinase CK2-Dependent Phosphorylation of hNopp140

  • Kim, Yun-Kyoung (Biomedical Research Center, Korea Institute of Science and Technology) ;
  • Lee, Won-Kyu (Biomedical Research Center, Korea Institute of Science and Technology) ;
  • Jin, Young-nam (Biomedical Research Center, Korea Institute of Science and Technology) ;
  • Lee, Kong-Joo (Division of Molecular Life Sciences, Ewha Womans University) ;
  • Jeon, Hye-sung (Biomedical Research Center, Korea Institute of Science and Technology) ;
  • Yu, Yeon-Gyu (Department of Chemistry, Kookmin University)
  • Received : 2006.05.12
  • Accepted : 2006.08.11
  • Published : 2006.11.30
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Abstract

Human nucleolar phosphoprotein p140 (hNopp140) is a nucleolar phosphoprotein that can bind to doxorubicin, an anti-cancer agent. We have examined the interaction between hNopp140 and doxorubicin as well as the folding property of hNopp140. Also, the effects of ATP and phosphorylation on the affinity of hNopp140 to doxorubicin are investigated by affinity dependent co-precipitation and surface plasmon resonance methods. Doxorubicin preferentially binds to un-phosphorylated form of hNopp140 with a $K_D$ value of $3.3\;{\times}\;10^{-7}$ M. Furthermore, doxorubicin reduces the protein kinase CK2-dependent phosphorylation of hNopp140, indicating that doxorubicin may perturb the cellular function of hNopp140 by reducing the protein kinase CK2-dependent phosphorylation of hNopp140. Low contents of the secondary structures of hNopp140 and the fast rate of proteolysis imply that hNopp140 has a high percentage of flexible regions or extended loop structures.

Keywords

References

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