Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
复制标题
DOI：
10.1126/science.285.5426.406
复制
发表时间：
1999-07-16
期刊：
影响因子：
56.9
通讯作者：
Bauer, CE
中科院分区：
文献类型：
--
作者：
Jiang, ZY;Swem, LR;Bauer, CE
在紫色光合细菌Rhodspirillum centenum中发现了一种光敏色素样蛋白PPR，PPR含有一个光活性黄蛋白(PYP)氨基末端结构域、一个与光敏色素相似的中心结构域和一个羧基末端组氨酸激活区。重建实验表明，PPR共价结合了蓝光吸收发色团对羟基肉桂酸，并且它的光循环在光谱上类似于PYP，但在动力学上慢于PYP。PPR还调节查尔酮合成酶基因的表达，以响应蓝光，并在体外被蓝光抑制自动磷酸化。系统发育分析表明，该菌可能是蓝藻和植物光敏色素的祖先。
A phytochrome-like protein called Ppr was discovered in the purple photosynthetic bacterium Rhodospirillum centenum, Ppr has a photoactive yellow protein (PYP) amino-terminal domain, a central domain with similarity to phytochrome, and a carboxyl-terminal histidine kinase domain. Reconstitution experiments demonstrate that Ppr covalently attaches the blue light-absorbing chromophore p-hydroxycinnamic acid and that it has a photocycle that is spectrally similar to, but kinetically slower than, that of PYP. Ppr also regulates chalcone synthase gene expression in response to blue light with autophosphorylation inhibited in vitro by blue light. Phylogenetic analysis demonstrates that R. centenum Ppr may be ancestral to cyanobacterial and plant phytochromes.