AAA+ superfamily ATPases: common structure--diverse function

Genes Cells. 2001 Jul;6(7):575-97. doi: 10.1046/j.1365-2443.2001.00447.x.


The AAA+ superfamily of ATPases, which contain a homologous ATPase module, are found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA+ proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA+ ATPases and other ring-shaped ATPases.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / physiology*
  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • DNA Replication / physiology
  • Eukaryotic Cells / cytology
  • Eukaryotic Cells / enzymology*
  • Humans
  • Membrane Fusion / physiology
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism
  • Mutation
  • Protein Structure, Tertiary


  • Molecular Chaperones
  • Adenosine Triphosphatases