Parker C S, Topol J
Cell. 1984 May;37(1):273-83. doi: 10.1016/0092-8674(84)90323-4.
A Drosophila RNA polymerase II transcription factor that is specific for at least one of the heat-shock genes has been isolated (designated HSTF for heat-shock transcription factor). This factor is required for active transcription of an hsp 70 gene in addition to RNA polymerase II and another general transcription factor, the A factor. Footprint analysis of the HSTF on the hsp 70 gene reveals that it binds specifically to a 55 bp region upstream from the TATA box. Both coding and noncoding DNA strands are completely protected from DNAase I cleavage by the HSTF . HSTF binding occurs in the apparent absence of RNA polymerase II. The HSTF is present in both heat-shocked and nonshocked cells, although it is more transcriptionally active when isolated from heat-shocked cells. The previously described B factor (an RNA polymerase II transcription factor that binds to the TATA box), isolated from nonshocked cells, is significantly reduced in both binding and transcriptional activity in heat-shocked cells. The potential role of the HSTF and the B factor in the activation of heat-shock gene transcription is discussed.
一种对至少一种热休克基因具有特异性的果蝇RNA聚合酶II转录因子已被分离出来（命名为热休克转录因子HSTF）。除了RNA聚合酶II和另一种通用转录因子A因子外，该因子对于hsp 70基因的活性转录也是必需的。对hsp 70基因上的HSTF进行足迹分析表明，它特异性地结合在TATA框上游55 bp的区域。编码和非编码DNA链都完全受到HSTF的保护，不被DNA酶I切割。HSTF的结合在明显没有RNA聚合酶II的情况下发生。HSTF存在于热休克细胞和未热休克细胞中，尽管从热休克细胞中分离出来时它具有更高的转录活性。先前描述的B因子（一种与TATA框结合的RNA聚合酶II转录因子），从未热休克细胞中分离出来，在热休克细胞中的结合和转录活性均显著降低。文中讨论了HSTF和B因子在热休克基因转录激活中的潜在作用。
