酪氨酸磷酸化的Stat1和Stat2加上一种48 kDa的蛋白质在形成干扰素刺激基因因子3时均与DNA接触。

Qureshi S A, Salditt-Georgieff M, Darnell J E

Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021, USA.

Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):3829-33. doi: 10.1073/pnas.92.9.3829.

Interferon alpha induction of transcription operates through interferon-stimulated-gene factor 3 (ISGF), a transcription factor two components of which are members of the newly characterized Stat family of transcription factors. Interferon alpha induces tyrosine phosphorylation of Stat1 and Stat2 proteins that associate and, together with a 48-kDa protein, form ISGF3. Evidence is presented that a heterodimer of Stat1 and Stat2 is present in ISGF3 and that Stat1 and the 48-kDa protein make precise contact, while Stat2 makes general contact, with the interferon-stimulated response element, the binding site of the ISGF3.

α干扰素诱导的转录作用是通过干扰素刺激基因因子3（ISGF）来实现的，该转录因子的两个组成部分是新鉴定的转录因子Stat家族的成员。α干扰素诱导Stat1和Stat2蛋白的酪氨酸磷酸化，这些蛋白相互结合，并与一种48 kDa的蛋白一起形成ISGF3。有证据表明，ISGF3中存在Stat1和Stat2的异二聚体，Stat1和48 kDa的蛋白与干扰素刺激反应元件（ISGF3的结合位点）进行精确接触，而Stat2则进行一般性接触。