果蝇中组蛋白H2b作为热休克蛋白的鉴定。
Identification of histone H2b as a heat-shock protein in Drosophila.
作者信息
Sanders M M
出版信息
J Cell Biol. 1981 Nov;91(2 Pt 1):579-83. doi: 10.1083/jcb.91.2.579.
Total cell polypeptides synthesized, in cultured Drosophila cells under control (25 degrees C) and heat-shock (37 degrees C) conditions have been compared in two different two-dimensional polyacrylamide gel electrophoresis systems which, together, resolve polypeptides having a wide range of isoelectric points, including the most basic polypeptides of the cell. The electrophoresis of basic proteins showed that the most prominent basic polypeptide synthesized in heat shock comigrated with histone H2b. This heat-shock polypeptide was identified as histone H2b by two criteria: (a) it comigrated with authentic histone H2b in Triton-urea-acetic acid acrylamide gel electrophoresis after solubilization from nuclei with acid; and (b) partial proteolysis peptide maps of the basic heat-shock protein and histone H2b were identical. The synthesis of histone H2b was induced threefold in heat shock, whereas synthesis of the other histones was reduced from two- to tenfold. The noncoordinate synthesis of histones in Drosophila in heat shock provides an interesting system in which to investigate transcriptional and translational controls of histone synthesis as well as assembly of histones into chromatin.
在两种不同的二维聚丙烯酰胺凝胶电泳系统中，对处于对照（25摄氏度）和热休克（37摄氏度）条件下培养的果蝇细胞中合成的总细胞多肽进行了比较。这两种系统共同分离出具有广泛等电点的多肽，包括细胞中最碱性的多肽。碱性蛋白质的电泳显示，热休克中合成的最突出的碱性多肽与组蛋白H2b迁移率相同。通过两个标准将这种热休克多肽鉴定为组蛋白H2b：（a）在用酸从细胞核中溶解后，在Triton - 尿素 - 乙酸丙烯酰胺凝胶电泳中，它与真实的组蛋白H2b迁移率相同；（b）碱性热休克蛋白和组蛋白H2b的部分蛋白酶解肽图相同。在热休克中，组蛋白H2b的合成增加了两倍，而其他组蛋白的合成则减少了两到十倍。果蝇在热休克中组蛋白的非协同合成提供了一个有趣的系统，可用于研究组蛋白合成的转录和翻译控制以及组蛋白组装到染色质中的过程。
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