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Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
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Published on: November 1, 2019

Staphylococcus aureus DinG, a helicase that has evolved into a nuclease.

Anne-Marie McRobbie1, Bjoern Meyer, Christophe Rouillon

  • 1Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK.

The Biochemical Journal
|December 15, 2011
PubMed
Summary

The Staphylococcus aureus DinG protein, unlike other bacterial DinG enzymes, functions as a 3′→5′ exonuclease, not a DNA helicase. This bacterial exonuclease activity may fulfill a similar role to canonical DNA helicases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • DinG (damage inducible gene G) is a bacterial superfamily 2 helicase.
  • DinG proteins share an essential FeS (iron–sulfur)-binding domain with the XPD helicase family.
  • In some bacteria, DinG is fused with an exonuclease domain.

Purpose of the Study:

  • To characterize the function of the DinG protein from Staphylococcus aureus.
  • To investigate the enzymatic activities of S. aureus DinG in the absence of an FeS domain.

Main Methods:

  • Biochemical assays to assess DNA helicase and exonuclease activities.
  • Enzyme kinetics studies involving ATP hydrolysis.
  • Site-directed mutagenesis of the putative ATP-binding cleft.

Main Results:

  • S. aureus DinG lacks an FeS domain and does not exhibit DNA helicase activity.
  • The protein possesses DNA-dependent ATP hydrolysis activity.
  • It functions as an active 3′→5′ exonuclease on single-stranded DNA and RNA.
  • Nuclease activity is modulated by mutations in the helicase domain and inhibited by ATP/ADP.

Conclusions:

  • S. aureus DinG is a functional 3′→5′ exonuclease, distinct from canonical DinG helicases.
  • The inactive helicase domain likely plays a regulatory role in controlling nuclease activity.
  • Degradation of nucleic acids by S. aureus DinG may serve a similar biological purpose to DNA displacement by canonical helicases.