Macromolecular complexes that unwind nucleic acids

Bioessays. 2003 Dec;25(12):1168-77. doi: 10.1002/bies.10369.

Abstract

In this essay, we consider helicases, defined as enzymes that use the free energies of binding and hydrolysis of ATP to drive the unwinding of double-stranded nucleic acids, and ask how they function within, and are "coupled" to, the macromolecular machines of gene expression. To illustrate the principles of the integration of helicases into such machines, we consider the macromolecular complexes that direct and control DNA replication and DNA-dependent RNA transcription, and use these systems to illustrate how machines centered around coupled polymerase-helicase systems can be regulated by small changes in the interactions of their functional components.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • DNA / metabolism
  • DNA Helicases / physiology*
  • DNA-Directed DNA Polymerase / metabolism
  • Escherichia coli / physiology
  • Hydrolysis
  • Kinetics
  • Models, Chemical
  • Models, Genetic
  • Nucleic Acid Conformation*
  • Protein Binding
  • RNA / metabolism
  • Thermodynamics
  • Transcription, Genetic

Substances

  • RNA
  • Adenosine Triphosphate
  • DNA
  • DNA-Directed DNA Polymerase
  • DNA Helicases