title: Conformational change induced by ATP binding correlates with enhanced biological function of Arabidopsis cryptochrome.
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.
authors.affiliation: Université Paris 6, CNRS-UMR 7180, PCMP, F-75005 Paris, France.
authors.forename: Sarah
authors.initials: S
authors.lastname: Burney
authors.forename: Nathalie
authors.initials: N
authors.lastname: Hoang
authors.forename: Michael
authors.initials: M
authors.lastname: Caruso
authors.forename: Elizabeth A
authors.initials: EA
authors.lastname: Dudkin
authors.forename: Margaret
authors.initials: M
authors.lastname: Ahmad
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Bouly