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Proteomic dissection of DNA polymerization
Faculty of Science - Papers (Archive)
  • Jennifer L Beck, University of Wollongong
  • Thitima Urathamakul, University of Wollongong
  • Stephen James Watt, University of Wollongong
  • Margaret Sheil, University of Wollongong
  • Patrick M Schaeffer, Australian National University
  • Nicholas E Dixon, Australian National University
RIS ID
15824
Publication Date
1-1-2006
Publication Details

Beck, J. L., Urathamakul, T., Watt, S., Sheil, M., Schaeffer, P. M. & Dixon, N. E. (2006). Proteomic dissection of DNA polymerization. Expert Review of Proteomics, 3 (2), 197-211.

Abstract

DNA polymerases replicate the genome by associating with a range of other proteins that enable rapid, high-fidelity copying of DNA. This complex of proteins and nucleic acids is called the replisome. Proteins of the replisome must interact with other networks of proteins, such as those involved in DNA repair. Many of the proteins involved in DNA polymerisation and the accessory proteins are known, but the array of proteins they interact with, and the spatial and temporal arrangement of these interactions is a current research topic. Mass spectrometry is a technique that can be used to identify the sites of these interactions and to determine the precise stoichiometries of binding partners in a functional complex. A complete understanding of the macromolecular interactions involved in DNA replication and repair may lead to discovery of new targets for antibiotics against bacteria and biomarkers for diagnosis of diseases such as cancer in humans.

Citation Information
Jennifer L Beck, Thitima Urathamakul, Stephen James Watt, Margaret Sheil, et al.. "Proteomic dissection of DNA polymerization" (2006) p. 197 - 211
Available at: http://works.bepress.com/nick_dixon/53/