Institute for Physiological Chemistry and Pathobiochemistry, Johannes Gutenberg University, Medical School, Mainz, Germany.
FEBS J. 2010 Mar;277(5):1182-201. doi: 10.1111/j.1742-4658.2009.07552.x. Epub 2010 Feb 1.
Based on the light-reactive behavior of siliceous sponges, their intriguing quartz glass-based spicular system and the existence of a light-generating luciferase [Müller WEG et al. (2009) Cell Mol Life Sci 66, 537-552], a protein potentially involved in light reception has been identified, cloned and recombinantly expressed from the demosponge Suberites domuncula. Its sequence displays two domains characteristic of cryptochrome, the N-terminal photolyase-related region and the C-terminal FAD-binding domain. The expression level of S. domuncula cryptochrome depends on animal's exposure to light and is highest in tissue regions rich in siliceous spicules; in the dark, no cryptochrome transcripts/translational products are seen. From the experimental data, it is proposed that sponges might employ a luciferase-like protein, the spicular system and a cryptochrome as the light source, optical waveguide and photosensor, respectively.
基于硅质海绵的光反应行为、其引人入胜的石英玻璃基骨针系统以及存在发光酶[Müller WEG 等人。(2009)细胞分子生命科学 66, 537-552],已经从寻常海绵 Suberites domuncula 中鉴定、克隆并重组表达了一种可能参与光接收的蛋白质。其序列显示出两个特征为隐色体的结构域,即 N 端光解酶相关区域和 C 端 FAD 结合结构域。S. domuncula 隐色体的表达水平取决于动物对光的暴露程度,在富含硅质骨针的组织区域中表达水平最高;在黑暗中,没有隐色体转录本/翻译产物。根据实验数据,提出海绵可能利用一种类似于荧光素酶的蛋白、骨针系统和隐色体分别作为光源、光导波和光传感器。