The cryptochromes

Genome Biol. 2005;6(5):220. doi: 10.1186/gb-2005-6-5-220. Epub 2005 Apr 29.

Abstract

Cryptochromes are photoreceptors that regulate entrainment by light of the circadian clock in plants and animals. They also act as integral parts of the central circadian oscillator in animal brains and as receptors controlling photomorphogenesis in response to blue or ultraviolet (UV-A) light in plants. Cryptochromes are probably the evolutionary descendents of DNA photolyases, which are light-activated DNA-repair enzymes, and are classified into three groups -- plant cryptochromes, animal cryptochromes, and CRY-DASH proteins. Cryptochromes and photolyases have similar three-dimensional structures, characterized by an alpha/beta domain and a helical domain. The structure also includes a chromophore, flavin adenine dinucleotide (FAD). The FAD-access cavity of the helical domain is the catalytic site of photolyases, and it is predicted also to be important in the mechanism of cryptochromes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Arabidopsis Proteins
  • Circadian Rhythm / physiology*
  • Cryptochromes
  • Drosophila / genetics
  • Drosophila / metabolism
  • Evolution, Molecular
  • Flavoproteins / chemistry
  • Flavoproteins / genetics
  • Flavoproteins / physiology*
  • Mammals / genetics
  • Mammals / metabolism
  • Models, Biological
  • Models, Molecular
  • Multigene Family
  • Photoreceptor Cells / chemistry
  • Photoreceptor Cells / physiology*
  • Phylogeny
  • Protein Structure, Tertiary

Substances

  • Arabidopsis Proteins
  • CRY1 protein, Arabidopsis
  • Cryptochromes
  • Flavoproteins