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

被引：33

作者：

Burney, Sarah

Hoang, Nathalie

Caruso, Michael ^{[2
]}

Dudkin, Elizabeth A. ^{[2
]}

Ahmad, Margaret ^{[2
]}

Bouly, Jean-Pierre ^{[1
]}

机构：

[1] Univ Paris 06, CNRS, UR5, PCMP,UMR 7180, F-75005 Paris, France

[2] Penn State Univ, Media, PA USA

来源：

FEBS LETTERS | 2009年 / 583卷 / 09期

基金：

美国国家科学基金会;

关键词：

Cryptochrome; Photolyase; Blue light; Photoreceptor; ATP; Arabidopsis thaliana; BLUE-LIGHT PHOTORECEPTOR; INDUCED ELECTRON-TRANSFER; SIGNAL-TRANSDUCTION; IN-VIVO; AUTOPHOSPHORYLATION; PHOSPHORYLATION; PROTEIN; DOMAIN; STATE;

D O I：

10.1016/j.febslet.2009.03.040

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1427 / 1433

页数：7

共 22 条

[1] DETERMINING STABILITY OF PROTEINS FROM GUANIDINIUM CHLORIDE TRANSITION CURVES [J].