title: The Ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor.
abstract: BACKGROUND
  The Ferritins are part of the extensive 'Ferritin-like superfamily' which have diverse functions but are linked by the presence of a common four-helical bundle domain. The role performed by Ferritins as the cellular repository of excess iron is unique. In many ways Ferritins act as tiny organelles in their ability to secrete iron away from the delicate machinery of the cell, and then to release it again in a controlled fashion avoiding toxicity. The Ferritins are ancient proteins, being common in all three domains of life. This ubiquity reflects the key contribution that Ferritins provide in achieving iron homeostasis.
  
  
  OBJECTIVE
  This review compares the features of the different Ferritins and considers how they, and other members of the Ferritin-like superfamily, have evolved. It also considers relevant features of the eleven other known families within the Ferritin-like superfamily, particularly the highly diverse rubrerythrins.
  
  
  CONCLUSIONS
  The Ferritins have travelled a considerable evolutionary journey, being derived from far more simplistic rubrerythrin-like molecules which play roles in defence against toxic oxygen species. The forces of evolution have moulded such molecules into three distinct types of iron storing (or detoxifying) protein: the classical and universal 24-meric ferritins; the haem-containing 24-meric bacterioferritins of prokaryotes; and the prokaryotic 12-meric Dps proteins. These three Ferritin types are similar, but also possess unique properties that distinguish them and enable then to achieve their specific physiological purposes.
  
  
  CONCLUSIONS
  A wide range of biological functions have evolved from a relatively simple structural unit.
authors.affiliation: The School of Biological Sciences, The University of Reading, Whiteknights, Reading, RG6 6AJ, UK.
authors.forename: Simon C
authors.initials: SC
authors.lastname: Andrews
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D005293:Ferritins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism* / Q000502:physiology; D006422:Hemerythrin / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000502:physiology; D010802:Phylogeny; D011487:Protein Conformation; D012416:Rubredoxins / Q000737:chemistry / Q000235:genetics*; D017385:Sequence Homology
chemical_list: D006422:Hemerythrin; D012416:Rubredoxins; C055857:rubrerythrins; D005293:Ferritins; D007501:Iron