Conformational change induced by ATP binding correlates with enhanced biological function of Arabidopsis cryptochrome |
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Authors: | Sarah Burney Michael Caruso Margaret Ahmad Jean-Pierre Bouly |
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Affiliation: | a Université Paris 6, CNRS - UMR 7180, PCMP, F-75005 Paris, France b Penn State University, Media, PA, USA |
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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. |
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Keywords: | Cryptochrome Photolyase Blue light Photoreceptor ATP Arabidopsis thaliana |
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