Svejstrup J Q, Feaver W J, LaPointe J, Kornberg R D
Department of Cell Biology, Stanford University School of Medicine, California 94305.
J Biol Chem. 1994 Nov 11;269(45):28044-8.
An RNA polymerase transcription factor IIH holoenzyme (holoTFIIH) has been resolved to near homogeneity from Saccharomyces cerevisiae. HoloTFIIH comprises the five-subunit core transcription factor described previously (Feaver, W. J., Svejstrup, J. Q., Bardwell, A. J., Bardwell, L., Buratowski, S., Gulyas, K. D., Donahue, T. F., Friedberg, E. C. and Kornberg, R. D. (1993) Cell 75, 1379-1387) and in addition, SSL2 and three further, as yet unidentified, polypeptides. HoloTFIIH possesses C-terminal repeat domain kinase activity and, together with other pure yeast transcription proteins, enables RNA polymerase II transcription in a fully defined system. By contrast, core TFIIH is inert in both C-terminal repeat domain kinase and reconstituted transcription assays.
一种RNA聚合酶转录因子IIH全酶(holoTFIIH)已从酿酒酵母中分离至近乎纯一的状态。HoloTFIIH包含先前所述的五亚基核心转录因子(Feaver, W. J., Svejstrup, J. Q., Bardwell, A. J., Bardwell, L., Buratowski, S., Gulyas, K. D., Donahue, T. F., Friedberg, E. C.和Kornberg, R. D.(1993年)《细胞》75卷,1379 - 1387页),此外,还有SSL2以及另外三种尚未鉴定的多肽。HoloTFIIH具有C末端重复结构域激酶活性,并且与其他纯酵母转录蛋白一起,能够在一个完全明确的系统中实现RNA聚合酶II转录。相比之下,核心TFIIH在C末端重复结构域激酶和重组转录试验中均无活性。