Helicase unwinding at the replication fork

Divya Nandakumar, Smita S. Patel

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

Abstract

Ring-shaped hexameric helicases play an essential role of double-stranded DNA unwinding during genome replication. The NTPase-powered unwinding activity of the hexameric helicases is required both for replication initiation and fork progression. We describe ensemble biophysical methods to measure the unwinding activity of ring-shaped helicases during fork progression using the T7 bacteriophage replicative helicase gp4A' as a model enzyme. These assays provide insights into the stepping mechanism of translocation, active or passive mechanism of unwinding, and regulation by associated proteins such as single strand DNA binding protein, DNA polymerase, and primase enzymes.

Original languageEnglish (US)
Title of host publicationMolecular Biophysics for the Life Sciences
PublisherSpringer New York
Pages291-312
Number of pages22
ISBN (Electronic)9781461485483
ISBN (Print)9781461485476
DOIs
StatePublished - Jan 1 2013

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Social Sciences(all)

Keywords

  • DNA polymerase
  • DNA unwinding
  • Gfit
  • Global regression analysis
  • Hexameric helicase
  • Primase
  • Replication
  • SSB
  • T7 bacteriophage
  • Unwinding assays
  • Unwinding mechanism

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