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Article
Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I
Biomolecular Sciences Institute: Faculty Publications
  • Kemin Tan, Argonne National Laboratory
  • Qingxuan Zhou, Department of Chemistry and Biochemistry, Florida International University
  • Bokun Cheng, New York Medical College
  • Zhongtao Zhang, New York Medical College
  • Andrzej Joachimiak, Argonne National Laboratory
  • Yuk-Ching Tse-Dinh, Biomolecular Sciences Institute and Department of Chemistry and Biochemistry, Florida International University, Miami, Florida
Date of this Version
10-20-2015
Document Type
Article
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Abstract
Escherichia coli topoisomerase I has an essential function in preventing hypernegative supercoiling of DNA. A full length structure of E. coli topoisomerase I reported here shows how the C-terminal domains bind single-stranded DNA (ssDNA) to recognize the accumulation of negative supercoils in duplex DNA. These C-terminal domains of E. coli topoisomerase I are known to interact with RNA polymerase, and two flexible linkers within the C-terminal domains may assist in the movement of the ssDNA for the rapid removal of transcription driven negative supercoils. The structure has also unveiled for the first time how the 4-Cys zinc ribbon domain and zinc ribbon-like domain bind ssDNA with primarily π-stacking interactions. This novel structure, in combination with new biochemical data, provides important insights into the mechanism of genome regulation by type IA topoisomerases that is essential for life, as well as the structures of homologous type IA TOP3α and TOP3β from higher eukaryotes that also have multiple 4-Cys zinc ribbon domains required for their physiological functions.
DOI
10.1093/nar/gkv1073
Identifier
FIDC001624
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Originally published in Nucleic Acids Research.

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Creative Commons Attribution 4.0
Citation Information
Kemin Tan, Qingxuan Zhou, Bokun Cheng, Zhongtao Zhang, Andrzej Joachimiak, Yuk-Ching Tse-Dinh; Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I. Nucleic Acids Res 2015; 43 (22): 11031-11046. doi: 10.1093/nar/gkv1073