Chyuan-Chuan Wu
National Taiwan University, Taipei, Taipei, Taiwan

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Publications (2)40.63 Total impact

  • Article: New insights into DNA-binding by type IIA topoisomerases.
    Chih-Chiang Chang, Ying-Ren Wang, Shin-Fu Chen, Chyuan-Chuan Wu, Nei-Li Chan
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    ABSTRACT: Type IIA topoisomerases catalyze the passage of two DNA duplexes across each other to resolve the entanglements and coiling of cellular DNA. The ability of these enzymes to interact simultaneously but differentially with two DNA segments is central to their DNA-manipulating functions: one duplex DNA is bound and cleaved to produce a transient double-strand break through which another DNA segment can be transported. Recent structural analyses have revealed in atomic detail how type IIA enzymes contact DNA and how the enzyme-DNA interactions may be exploited by drugs to achieve therapeutic purposes. This review summarizes these new findings, with a special focus on the assembly and structural features of the enzymes' composite DNA-binding surfaces.
    Current Opinion in Structural Biology 12/2012; · 9.42 Impact Factor
  • Article: Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide.
    Chyuan-Chuan Wu, Tsai-Kun Li, Lynn Farh, Li-Ying Lin, Te-Sheng Lin, Yu-Jen Yu, Tien-Jui Yen, Chia-Wang Chiang, Nei-Li Chan
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    ABSTRACT: Type II topoisomerases (TOP2s) resolve the topological problems of DNA by transiently cleaving both strands of a DNA duplex to form a cleavage complex through which another DNA segment can be transported. Several widely prescribed anticancer drugs increase the population of TOP2 cleavage complex, which leads to TOP2-mediated chromosome DNA breakage and death of cancer cells. We present the crystal structure of a large fragment of human TOP2β complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. The analysis of protein-drug interactions provides information applicable for developing an isoform-specific TOP2-targeting strategy.
    Science 07/2011; 333(6041):459-62. · 31.20 Impact Factor

Institutions

  • 2011
    • National Taiwan University
      • Graduate Institute of Biochemistry and Molecular Biology
      Taipei, Taipei, Taiwan
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