Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Mitoxantrone Binds to Nopp140, an Intrinsically Unstructured Protein, and Modulate its Interaction with Protein Kinase CK2

  • Lee, Won-Kyu (Department of Chemistry, Kookmin University) ;
  • Lee, Sang-Yeop (Department of Chemistry, Kookmin University) ;
  • Na, Jung-Hyun (Department of Chemistry, Kookmin University) ;
  • Jang, Sung-Woo (Department of Chemistry, Kookmin University) ;
  • Park, Chan-Ryang (Department of Chemistry, Kookmin University) ;
  • Kim, Soo-Youl (Cancer Cell & Molecular Biology Branch, Division of Cancer Biology, Research Institute, National Cancer Center) ;
  • Lee, Si-Hyeong (Division of Biosystems Research, Korea Research Institute of Bioscience and Biotechnology) ;
  • Han, Kyou-Hoon (Division of Biosystems Research, Korea Research Institute of Bioscience and Biotechnology) ;
  • Yu, Yeon-Gyu (Department of Chemistry, Kookmin University)
  • Received : 2012.02.20
  • Accepted : 2012.03.22
  • Published : 2012.06.20
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Abstract

Nopp140 is a highly phosphorylated protein that resides in the nucleolus of mammalian cell and is involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome. It also can bind to a ubiquitous protein kinase CK2 that mediates cell growth and prevents apoptosis. We found that Nopp140 is an intrinsically unfolded protein (IUP) lacking stable secondary structures over its entire sequence of 709 residues. We discovered that mitoxantrone, an anticancer agent, was able to enhance the interaction between Nopp140 and CK2 and maintain suppressed activity of CK2. Surface plasma resonance studies on different domains of Nopp140 show that the C-terminal region of Nopp140 is responsible for binding with mitoxantrone. Our results present an interesting example where a small chemical compound binds to an intrinsically unfolded protein (IUP) and enhances protein-protein interactions.

Keywords

References

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