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      Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds.

      Williamson, Adele; Leiros, Hanna-Kirsti S.
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      2020 williamson Nucleic Acids Research.pdf
      Published version, 7.794Mb
      DOI
       10.1093/nar/gkaa307
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      Williamson, A., & Leiros, H.-K. S. (2020). Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds. Nucleic Acids Res, 48(15), 8225–8242. https://doi.org/10.1093/nar/gkaa307
      Permanent Research Commons link: https://hdl.handle.net/10289/13873
      Abstract
      DNA ligases are diverse enzymes with essential functions in replication and repair of DNA; here we review recent advances in their structure and distribution and discuss how this contributes to understanding their biological roles and technological potential. Recent high-resolution crystal structures of DNA ligases from different organisms, including DNA-bound states and reaction intermediates, have provided considerable insight into their enzymatic mechanism and substrate interactions. All cellular organisms possess at least one DNA ligase, but many species encode multiple forms some of which are modular multifunctional enzymes. New experimental evidence for participation of DNA ligases in pathways with additional DNA modifying enzymes is defining their participation in non-redundant repair processes enabling elucidation of their biological functions. Coupled with identification of a wealth of DNA ligase sequences through genomic data, our increased appreciation of the structural diversity and phylogenetic distribution of DNA ligases has the potential to uncover new biotechnological tools and provide new treatment options for bacterial pathogens.
      Date
      2020
      Type
      Journal Article
      Rights
      © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

      This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
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