Biochemical methods to monitor loading and activation of hexameric helicases

Amy J. Fernandez, James M. Berger

Research output: Chapter in Book/Report/Conference proceedingChapter


Ring-shaped hexameric helicases are an essential class of enzymes that unwind duplex nucleic acids to support a variety of cellular processes. Because of their critical roles in cells, hexameric helicase dysfunction has been linked to DNA damage and genomic instability. Biochemical characterization of hexameric helicase activity and regulation in vitro is necessary for understanding enzyme function and aiding drug discovery efforts. In this chapter, we describe protocols for characterizing mechanisms of helicase loading, activation, and unwinding using the model replicative hexameric DnaB helicase and its cognate DnaC loading factor from E. coli.

Original languageEnglish (US)
Title of host publicationHelicase Enzymes Part A
EditorsMichael A. Trakselis
PublisherAcademic Press Inc.
Number of pages10
ISBN (Print)9780323914765
StatePublished - Jan 2022

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • DNA unwinding
  • Helicase loading
  • Hexameric helicase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Biochemical methods to monitor loading and activation of hexameric helicases'. Together they form a unique fingerprint.

Cite this