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Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
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UPF1-like helicase grip on nucleic acids dictates processivity.

Joanne Kanaan1, Saurabh Raj1,2,3, Laurence Decourty4

  • 1Institut de biologie de l'Ecole normale supérieure (IBENS), Ecole normale supérieure, CNRS, INSERM, PSL Research University, 46 rue d'Ulm, 75005, Paris, France.

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Helicases like UPF1 use their grip on nucleic acids (NA) to unwind DNA. Tighter binding increases helicase processivity and nonsense-mediated mRNA decay (NMD) efficiency.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Helicases are crucial molecular motors for nucleic acid (NA) metabolism.
  • Understanding helicase processivity is essential for genome stability and gene expression.
  • The factors governing helicase binding and translocation remain largely unknown.

Purpose of the Study:

  • To investigate the relationship between helicase binding lifetime and processivity.
  • To determine the role of nucleic acid binding dynamics in UPF1 helicase function.
  • To explore the impact of altered UPF1 binding on nonsense-mediated mRNA decay (NMD) in vivo.

Main Methods:

  • Development of single-molecule assays to measure helicase binding duration on DNA.
  • Characterization of UPF1 and IGHMBP2 helicase residence times.
  • Construction and functional analysis of UPF1 mutants with altered DNA binding affinity.
  • In vivo assessment of NMD efficiency.

Main Results:

  • UPF1 exhibits prolonged nucleic acid binding, correlating with high processivity.
  • IGHMBP2, despite structural similarity, shows a significantly shorter residence time.
  • Helicase grip tightness directly influences residence time and processivity.
  • Reduced UPF1 binding affinity impairs NMD efficiency in vivo.

Conclusions:

  • Helicase processivity is modulated by the tightness of nucleic acid binding.
  • A three-state model (bound, sliding, unbound) can predict helicase processivity.
  • UPF1's strong nucleic acid interaction is critical for its role in NMD.