Regulated synthesis of phycobilisome components.
Regulated synthesis of phycobilisome components.
复制标题
藻胆体成分的调节合成。
DOI：
10.1111/j.1751-1097.1986.tb05543.x
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发表时间：
1986
影响因子：
3.3
通讯作者：
Conley,PB
中科院分区：
文献类型：
--
作者：
Grossman,AR;Lemaux,PG;Conley,PB
在某些真核藻类和原核蓝藻中的主要捕光触角是称为藻胆体的大分子复合物（甘特，1981; Glazer，1977，1982，1985; Glazer等人，1983年）。虽然在功能上类似于高等植物的捕光叶绿素蛋白复合物，但这些水溶性结构附着在光合膜上，而不是嵌入其中。藻胆体由两个结构域组成：靠近光合膜的核心和从核心辐射出的杆。在许多蓝细菌中发现的典型的半球形藻胆体结构如图1所示。在过去的十年中，光谱学（参见甘特，1981; Glazer，1982，1985）、免疫学（参见甘特，1981）、生物化学（Yamanaka等人，1980; Redlinger和甘特，1981; Yamanaka和Glazer，1981; Yamanaka等人，1982; Gingrich等人，1982; Lundell和Glazer，1983 a，B）和X射线晶体学分析（Riimbeli等人，1985; Schirmer等人，1985; Schirmer等人，1986）已经得到了其结构的详细图片（关于藻胆体结构的综述参见Glazer等人，1983）和能量转移途径的某些方面（Glazer等人，1985; Glazer，1985）。藻胆体由发色（85%）和非发色（ISYO）多肽组成（Tandeau de马尔萨克和Cohen-Bazire，1977）。根据它们的光谱特性，发色蛋白或藻胆蛋白被分为三大类：别藻蓝蛋白（AP）、藻蓝蛋白（PC）和藻红蛋白（PE）。藻红蓝蛋白，第四种藻胆蛋白，有时取代PE的光捕获复合物。藻胆蛋白的基本结构单元是含有两个不同亚基（a和p）的单体。在核心中，AP（λ，650 nm）的单体聚集成三聚体，根据它们在藻胆体中的位置，三聚体与胆蛋白亚基和接头多肽的命名是根据Glazer（1985）组装的。对于胆蛋白，亚基由类型（a或p）和组（AP、PC或PE）表示。例如，alpha-PC表示为apt。连接子以其分子量（MW）（上标）和在藻胆体中的位置（下标）表示（其中C=核心，R=杆状结构）。ItC=杆状核连接，CM=核-类囊体膜连接）。例如，锚蛋白表示为L; t！H.
The major light-harvesting antennae in certain eukaryotic algae and prokaryotic cyanobacteria are macromolecular complexes called phycobilisomes (Gantt, 1981; Glazer, 1977, 1982, 1985; Glazer et al., 1983). Although functionally analogous to the light-harvesting chlorophyll-protein complexes of higher plants, these water-soluble structures are attached to but not embedded in the photosynthetic membranes. The phycobilisome is composed of two structural domains: the core which is proximal to the photosynthetic membranes and the rods which radiate from the core. A typical hemidiscoidal phycobilisome structure, found in many cyanobacteria, is presented in Fig. 1. Over the past decade spectral (see Gantt, 1981; Glazer, 1982, 1985) immunological (see Gantt, 1981), biochemical (Yamanaka et al., 1980; Redlinger and Gantt, 1981; Yamanaka and Glazer, 1981; Yamanaka et al., 1982; Gingrich et a/., 1982; Lundelll and Glazer, 1983a, b) and X-ray crystallographic analyses (Riimbeli et al., 1985; Schirmer et al., 1985; Schirmer et at., 1986) of this complex have resulted in a detailed picture of its architecture (for review on phycobilisome structure see Glazer et al., 1983) and some aspects of the pathway of energy transfer (Glazer et a/., 1985; Glazer, 1985). The phycobilisome is composed of chromophoric (85%) and nonchromophoric (ISYO) polypeptides (Tandeau de Marsac and Cohen-Bazire, 1977). Based on their spectral characteristics the chromophoric proteins, or phycobiliproteins, have been classified into three major groups, allophycocyanin (AP), phycocyanin (PC), and phycoerythrin (PE). Phycoerythrocyanin, a fourth phycobiliprotein species, sometimes replaces PE in the light-harvesting complex. The basic phycobiliprotein building block is a monomer containing two dissimilar subunits (a and p). In the core, monomers of AP (A,,, 650 nm) aggregate into trimers which, depending upon their position in the phycobilisome are assembled with'Nomenclature for biliprotein subunits and linker polypeptides is after Glazer (1985). For the biliproteins, the subunits are denoted by type (a or p) and groups (AP, PC or PE). For example, alpha-PC is denoted apt. The linkers are denoted by their molecular weight (MW)(superscript) and location in the phycobilisome (subscript)(where C= core, R= rod substucture. ItC= rod core junction, CM= core-thylakoid membrane jaunction). For example, the anchor protein is denoted L; t! h.