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

doi:10.1016/j.febslet.2009.03.040

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

Penn State Brandywine

Research output: Contribution to journal › Article › peer-review

38 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 language	English (US)
Pages (from-to)	1427-1433
Number of pages	7
Journal	FEBS Letters
Volume	583
Issue number	9
DOIs	https://doi.org/10.1016/j.febslet.2009.03.040
State	Published - May 6 2009

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2009.03.040

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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.",

author = "Sarah Burney and Nathalie Hoang and Michael Caruso and Dudkin, {Elizabeth A.} and Margaret Ahmad and Bouly, {Jean Pierre}",

note = "Funding Information: We are indebted to Rachel Carol for critical reading of the manuscript and helpful discussion. This work was funded by the US National Science Foundation (Award No. 0343737) to Margaret Ahmad. Nathalie Hoang was funded by an ACI/BCMS doctoral fellowship from the French ministry of research.",

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T1 - Conformational change induced by ATP binding correlates with enhanced biological function of Arabidopsis cryptochrome

AU - Burney, Sarah

AU - Hoang, Nathalie

AU - Caruso, Michael

AU - Dudkin, Elizabeth A.

AU - Ahmad, Margaret

AU - Bouly, Jean Pierre

N1 - Funding Information: We are indebted to Rachel Carol for critical reading of the manuscript and helpful discussion. This work was funded by the US National Science Foundation (Award No. 0343737) to Margaret Ahmad. Nathalie Hoang was funded by an ACI/BCMS doctoral fellowship from the French ministry of research.

PY - 2009/5/6

Y1 - 2009/5/6

N2 - 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.

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

Abstract

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