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Related Experiment Videos

A universal type IA topoisomerase fold.

Michel Duguet1, Marie-Claude Serre, Claire Bouthier de La Tour

  • 1Laboratoire d'Enzymologie des Acides Nucléiques, Institut de Génétique et Microbiologie, Université Paris-Sud, Unité Mixte de Recherche 8621, Centre National de la Recherche Scientifique, 91405 Orsay, France.

Journal of Molecular Biology
|May 2, 2006
PubMed
Summary

DNA topoisomerases control DNA topology. This study reveals a conserved structural unit, the "topofold," common to all type IA topoisomerases, suggesting an evolutionary origin from gene duplication.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • DNA topoisomerases regulate DNA topology, crucial for genome stability.
  • Type IA topoisomerases are ubiquitous enzymes found across all life forms.
  • These enzymes share a common toroidal structure.

Purpose of the Study:

  • To investigate the conserved structural and sequence features of type IA topoisomerases.
  • To identify the fundamental building block of the type IA topoisomerase toroidal structure.
  • To explore the evolutionary origins of the type IA topoisomerase family.

Main Methods:

  • Limited proteolysis of Thermotoga maritima topoisomerase I.
  • Structural data analysis of known topoisomerase I structures.

Related Experiment Videos

  • Sequence data analysis across the topoisomerase IA family.
  • Secondary and tertiary structure conservation analysis.

    • Main Results:

    • The toroidal structure of type IA topoisomerases can be dissociated into repeating units.
    • A conserved elementary fold, termed the "topofold" (approx. 150 amino acids), is identified in the entire family.
    • Two conserved sequence motifs (MI and MII) are present at the base of the ring structure.
    • While sequences diverge, secondary and tertiary structures of topofolds are highly conserved.

    Conclusions:

    • The topofold represents a fundamental, conserved unit within type IA topoisomerases.
    • The conserved MI and MII motifs likely play critical roles in enzyme function.
    • The observed twofold repeat suggests an evolutionary history involving gene duplication and fusion of an ancestral topofold.