Rappaport J, Reinberg D, Zandomeni R, Weinmann R
J Biol Chem. 1987 Apr 15;262(11):5227-32.
SII was purified from calf thymus tissue to apparent homogeneity by a rapid procedure. The 38-kDa protein stimulated RNA synthesis by purified calf thymus RNA polymerase II 4-fold. The calf thymus SII had similar chromatographic properties and molecular size and cross-reacted immunologically with antibodies to mouse SII (Sekimizu, K., Nakanishi, Y., Mizuno, D., and Natori, S. (1979) Biochemistry 18, 1582-1588). We have substituted the purified calf thymus SII for the partially purified HeLa transcription factor IIS fraction in a HeLa (human) transcription system reconstituted with purified factors and RNA polymerase II. The purified protein stimulated specific transcription from the adenovirus 2 major late promoter by increasing the efficiency of the elongation reaction.
通过一种快速方法从小牛胸腺组织中纯化出SII，使其达到表观均一性。这种38 kDa的蛋白质能将纯化的小牛胸腺RNA聚合酶II的RNA合成活性提高4倍。小牛胸腺SII具有相似的色谱特性和分子大小，并且能与抗小鼠SII的抗体发生免疫交叉反应（关水，K.，中西，Y.，水野，D.，和名取，S.（1979年）《生物化学》18，1582 - 1588）。在一个用纯化因子和RNA聚合酶II重建的HeLa（人）转录系统中，我们用纯化的小牛胸腺SII替代了部分纯化的HeLa转录因子IIS组分。该纯化蛋白通过提高延伸反应的效率，刺激了腺病毒2主要晚期启动子的特异性转录。
