Role of phycoerythrin in marine picoplankton Synechococcus spp.
Role of phycoerythrin in marine picoplankton Synechococcus spp.
复制标题
藻红蛋白在海洋超微型浮游生物聚球藻中的作用。
DOI：
10.1126/science.3097824
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Glazer,AN
中科院分区：
文献类型：
--
作者：
Yeh,SW;Ong,LJ;Glazer,AN
光合单细胞蓝藻聚藻球菌最近才被认为是海洋微浮游生物群落（细胞直径为0.2至2.0微米）的重要成员，也是海洋初级生产力的重要贡献者(1)。这些蓝藻细菌的一个特别显著的特征是它们的橘红色，这是它们细胞内含有高水平的光合辅助藻胆蛋白藻红蛋白（PE）的结果。对许多蓝藻和红藻的研究表明，在合适的条件下，藻胆蛋白可以作为一种称为藻胆异构体的大型光收集复合物的组成部分被分离出来(2)。此外，完整蓝藻和红藻细胞的大量时间分辨发射数据表明，几乎所有的藻胆蛋白都包含在这些复合物中(3)。Wyman等人(4)得出结论，这种概括似乎不适用于在硝酸盐不是生长限制因素的培养基中培养的海洋蓝藻。Wyman等人(4)测量了在50%甘油（假定能将PE向藻蓝蛋白的能量转移解偶）和完整细胞中聚珠球菌球菌WH7803（也称为DC2）细胞的相对PE荧光发射，计算出在富氮培养基中培养的细胞中，多达40%的PE以游离蛋白的形式存在，并得出PE在聚珠球菌中具有两种不同功能的结论
Photosynthetic unicellular cyanobacteria Synechococcus spp. were recognized only re-cently as prominent members of the oceanic picoplankton community (cells of diameter 0.2 to 2.0, um) and as significant contribu-tors to primary productivity in the sea (1). A particularly noticeable feature of these cyan-obacteria is their orange-red color, a conse-quence of the high level of the photosynthetic accessory phycobiliprotein phycoerythrin (PE) contained within their cells. Studies of numerous cyanobacteria and red algae have shown that the phycobiliproteins can be isolated under suitable conditions as components ofa large light-harvesting com-plex called the phycobilisome (2). More-over, substantial time-resolved emission data on intact cyanobacterial and red algal cells indicate that virtually all ofthe phycobiliprotein is contained within these complex-es (3). Wyman et al.(4) conclude that this generalization does not appear to hold for marine cyanobacteria cultured in a medium in which nitrate was not a limiting factor for growth. From measurements of relative PE fluorescence emission of cells of Synechococ-cus WH7803 (also known as DC2) in 50% glycerol (assumed to uncouple the energy transfer from PE to phycocyanin) and of intact cells, Wyman et al.(4) calculate that as much as 40% of the PE in cells cultured in nitrogen-sufficient media is present as free protein and conclude that PE serves two functionally distinct roles in Synechococcus