title: AAA+ superfamily ATPases: common structure--diverse function.
abstract: 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.
authors.affiliation: Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862-0976, Japan. ogura@gpo.kumamoto-u.ac.jp
authors.forename: T
authors.initials: T
authors.lastname: Ogura
authors.forename: A J
authors.initials: AJ
authors.lastname: Wilkinson
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004261:DNA Replication / Q000502:physiology; D005057:Eukaryotic Cells / Q000166:cytology / Q000201:enzymology*; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D009154:Mutation; D017434:Protein Structure, Tertiary
chemical_list: D018832:Molecular Chaperones; D000251:Adenosine Triphosphatases