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首页> 外文期刊>Molecular and Cellular Biology >Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila.
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Structure and expression of two temperature-specific surface proteins in the ciliated protozoan Tetrahymena thermophila.

机译：纤毛原生动物四氢乙酰硫唑中两个温度特异性表面蛋白的结构和表达。

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The presence of specific proteins (known as immobilization antigens) on the surface of the ciliated protozoan Tetrahymena thermophila is under environmental regulation. There are five different classes (serotypes) of surface proteins which appear on the cell surface when T. thermophila is cultured under different conditions of temperature or incubation medium; three of these are temperature dependent. The appearance of these proteins on the cell surface is mutually exclusive. We used polyclonal antibodies raised against 30 degrees C (designated SerH3)- and 40 degrees C (designated SerT)-specific surface antigens to study their structure and expression. We showed that these surface proteins contain at least one disulfide bridge. On sodium dodecyl sulfate-denaturing polyacrylamide gels, the nonreduced 30 degrees C- and 40 degrees C-specific surface proteins migrated with molecular sizes of 69 and 36 kilodaltons, respectively. The reduced forms of the proteins migrated with molecular sizes of 58 and 30 kilodaltons, respectively. The synthesis of the surface proteins responded rapidly and with a time course similar to that of the incubation temperature. The synthesis of each surface protein was greatly reduced within 1 h and undetectable by 2 h after a shift to the temperature at which the protein is not expressed. Surface protein synthesis resumed by the end of 1 h after a shift to the temperature at which the protein is expressed. The temperature-dependent induction of these surface proteins appears to be dependent on the synthesis of new mRNA, as indicated by a sensitivity to actinomycin D. Surface protein syntheses were mutually exclusive except at a transition temperature. At 35 degrees C both surface proteins were synthesized by a cell population. These data support the potential of this system as a model for the study of the effects of environmental factors on the genetic regulation of cell surface proteins.
机译：在丝状原生动物Tetrahymena Heatholia的表面上存在特定蛋白质（称为固定抗原）的存在是在环境调节下进行的。当在不同的温度或培养培养基的不同条件下培养T.VircophiRA时，在细胞表面上出现五种不同的表面蛋白（血清型）。其中三个是温度依赖性。这些蛋白质在细胞表面上的外观是互斥的。我们使用针对30摄氏度（指定的SerH3）的多克隆抗体 - 和40℃（指定的Sert）特异性表面抗原，以研究其结构和表达。我们表明这些表面蛋白质含有至少一种二硫桥。在十二烷基硫酸钠 - 变性聚丙烯酰胺凝胶上，分别具有69和36千杆子的分子尺寸的30℃和40摄氏度的C-和40摄氏度的表面蛋白。蛋白质的减少形式分别以分子尺寸的58和30千伏多谷迁移。表面蛋白的合成迅速响应，并且具有与孵育温度类似的时间过程。在1小时内，每种表面蛋白的合成大大降低，并且在向未表达蛋白质的温度后2小时内未检测到。在向表达蛋白质的温度后1小时结束，表面蛋白质合成恢复。这些表面蛋白的温度依赖性诱导似乎取决于新mRNA的合成，如通过对放线霉素D的敏感性所示。表面蛋白合成除了在过渡温度下相互排他性。在35摄氏度下，通过细胞群合化两种表面蛋白质。这些数据支持该系统的潜力作为研究环境因素对细胞表面蛋白遗传调节的影响的模型。

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