Type IA DNA Topoisomerases: A Universal Core and Multiple Activities

Methods Mol Biol. 2018:1703:1-20. doi: 10.1007/978-1-4939-7459-7_1.

Abstract

All the type IA topoisomerases display universal characteristics relying on a core region basically responsible for the transesterification and the strand passage reaction. First limited to the bacterial domain for a long time, these enzymes were further retrieved in Archaea and Eukarya as well. This is representative of an extremely ancient origin, probably due to an inheritance from the RNA world. As remaining evidence, some current topoisomerases IA have retained a RNA topoisomerase activity. Despite the presence of this core region in all of these TopoIAs, some differences exist and are originated from variable regions, located essentially within both extremities, conferring on them their specificities. During the last 2 decades the evidence of multiple activities and dedicated roles highlighted the importance of the topoisomerases IA. It is now obvious that topoisomerases IA are key enzymes involved in the maintenance of the genome stability. The discovery of these new activities was done thanks to the use of more accurate assays, based on new sophisticated DNA substrates.

Keywords: Reverse gyrase; Topoisomerase I; Topoisomerase III; Topoisomerases; Type 1A; topA; topB; toprim.

MeSH terms

  • Catalytic Domain
  • DNA Topoisomerases, Type I / chemistry*
  • DNA Topoisomerases, Type I / metabolism*
  • Esterification
  • Models, Molecular
  • Protein Conformation
  • Protein Domains

Substances

  • DNA Topoisomerases, Type I