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

Sarah Burney, Nathalie Hoang, Michael Caruso, Elizabeth A. Dudkin, Margaret Ahmad, Jean Pierre Bouly

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1427-1433
Number of pages7
JournalFEBS Letters
Volume583
Issue number9
DOIs
StatePublished - May 6 2009

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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