Wadsworth S C
Mol Cell Biol. 1982 Mar;2(3):286-92. doi: 10.1128/mcb.2.3.286-292.1982.
At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.
从与一个先前已证明定位于87A和87C热休克胀泡位点的克隆热休克基因杂交的mRNA中,合成了至少四种分子量为70,000至75,000(70 - 75K)的蛋白质。当在十二烷基硫酸钠 - 聚丙烯酰胺凝胶上进行分析时,这些体外合成的蛋白质与体内合成的热休克诱导蛋白无法区分。对在5分钟脉冲期间或连续标记期间体内合成的这组蛋白质的模式进行比较表明,72 - 75K的蛋白质可能不是主要70K热休克蛋白的动力学前体。用V8蛋白酶产生的部分消化产物表明,70 - 75K的热休克蛋白密切相关,但它们之间存在明显差异。从Kc细胞系和黑腹果蝇俄勒冈R品系的热休克蛋白获得的部分消化模式非常相似。对70 - 75K热休克蛋白合成模式的遗传分析表明,编码三种72 - 75K热休克蛋白中至少两种的基因位于主要的87A和87C胀泡位点之外。