Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases

Biochem Soc Trans. 2011 Apr;39(2):589-94. doi: 10.1042/BST0390589.

Abstract

To cleave DNA, the Type III RM (restriction-modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / pharmacology*
  • Animals
  • Binding Sites / drug effects
  • Binding Sites / genetics
  • DNA / chemistry
  • DNA / metabolism*
  • Deoxyribonucleases, Type III Site-Specific / metabolism*
  • Deoxyribonucleases, Type III Site-Specific / physiology*
  • Humans
  • Models, Biological
  • Movement / physiology*
  • Nucleic Acid Conformation / drug effects
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • Protein Transport
  • Substrate Specificity

Substances

  • Adenosine Triphosphate
  • DNA
  • Deoxyribonucleases, Type III Site-Specific