Conformational change induced by ATP binding correlates with enhanced biological function of Arabidopsis cryptochrome

FEBS Lett. 2009 May 6;583(9):1427-33. doi: 10.1016/j.febslet.2009.03.040. Epub 2009 Mar 25.

Abstract

Cryptochromes are widely distributed blue light photoreceptors involved in numerous signaling functions in plants and animals. Both plant and animal-type cryptochromes are found to bind ATP and display intrinsic autokinase activity; however the functional significance of this activity remains a matter of speculation. Here we show in purified preparations of Arabidopsis cry1 that ATP binding induces conformational change independently of light and increases the amount and stability of light-induced flavin radical formation. Nucleotide binding may thereby provide a mechanism whereby light responsivity in organisms can be regulated through modulation of cryptochrome photoreceptor conformation.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins
  • Cryptochromes
  • Flavoproteins / chemistry
  • Flavoproteins / isolation & purification
  • Flavoproteins / metabolism*
  • Flavoproteins / physiology
  • Hydrolysis
  • Oxidation-Reduction
  • Photochemistry
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Spectrometry, Fluorescence
  • Trypsin / metabolism

Substances

  • Arabidopsis Proteins
  • CRY1 protein, Arabidopsis
  • Cryptochromes
  • Flavoproteins
  • Recombinant Proteins
  • Adenosine Triphosphate
  • Trypsin