Structure and Function of Plant Photoreceptors

被引:400
作者
Moeglich, Andreas [1 ]
Yang, Xiaojing [1 ]
Ayers, Rebecca A. [1 ]
Moffat, Keith [1 ,2 ]
机构
[1] Univ Chicago, Dept Biochem & Mol Biol, Inst Biophys Dynam, Chicago, IL 60637 USA
[2] Univ Chicago, Consortium Adv Radiat Sources CARS, Chicago, IL 60637 USA
来源
ANNUAL REVIEW OF PLANT BIOLOGY, VOL 61 | 2010年 / 61卷
关键词
cryptochrome; light-oxygen-voltage; photochemistry; phytochrome; rhodopsin; signal transduction; BLUE-LIGHT RECEPTOR; CHROMOPHORE-BINDING DOMAIN; PHOTOACTIVE YELLOW PROTEIN; INDUCED PROTON RELEASE; SIGNAL-TRANSDUCTION; IN-VIVO; ARABIDOPSIS-THALIANA; CRYSTAL-STRUCTURE; LOV2; DOMAIN; PHYTOCHROME;
D O I
10.1146/annurev-arplant-042809-112259
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Signaling photoreceptors use the information contained in the absorption of a photon to modulate biological activity in plants and a wide range of organisms. The fundamental and as yet imperfectly answered question is, how is this achieved at the molecular level? We adopt the perspective of biophysicists interested in light-dependent signal transduction in nature and the three-dimensional structures that underpin signaling. Six classes of photoreceptors are known: light-oxygen-voltage (LOV) sensors, xanthopsins, phytochromes, blue-light sensors using flavin adenine dinucleotide (BLUF), cryptochromes, and rhodopsins. All are water-soluble proteins except rhodopsins, which are integral membrane proteins; all are based on a modular architecture except cryptochromes and rhodopsins; and each displays a distinct, light-dependent chemical process based on the photochemistry of their nonprotein chromophore, such as isomerization about a double bond (xanthopsins, phytochromes, and rhodopsins), formation or rupture of a covalent bond (LOV sensors), or electron transfer (BLUF sensors and cryptochromes).
引用
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页码:21 / 47
页数:27
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