DP-1 - A CELL-CYCLE-REGULATED AND PHOSPHORYLATED COMPONENT OF TRANSCRIPTION FACTOR DRTF1/E2F WHICH IS FUNCTIONALLY IMPORTANT FOR RECOGNITION BY PRB AND THE ADENOVIRUS E4-ORF-6/7 PROTEIN
DP-1 - A CELL-CYCLE-REGULATED AND PHOSPHORYLATED COMPONENT OF TRANSCRIPTION FACTOR DRTF1/E2F WHICH IS FUNCTIONALLY IMPORTANT FOR RECOGNITION BY PRB AND THE ADENOVIRUS E4-ORF-6/7 PROTEIN
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DOI：
10.1002/j.1460-2075.1994.tb06609.x
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发表时间：
1994-07-01
期刊：
影响因子：
11.4
通讯作者：
LATHANGUE, NB
中科院分区：
文献类型：
--
作者：
BANDARA, LR;LAM, EWF;LATHANGUE, NB
细胞转录因子DRTF 1/E2 F通过与细胞增殖的重要调节因子的周期性相互作用将细胞周期事件与转录装置整合。两个序列特异性DNA结合蛋白DP-1和E2 F-1是DRTF 1/E2 F的组分，它们在DP-1/E2 F-1异二聚体中协同相互作用。在这里，我们表明，DP-1是一个非常常见的，可能是普遍的，在3 T3细胞中的DRTF 1/E2 F的组成部分，因为它存在于所有形式的DNA结合活性，发生在细胞周期的进展。此外，磷酸化的DP-1多肽在细胞周期期间经历磷酸化依赖性迁移率变化，表明其磷酸化水平在细胞周期进展期间受到调节。DP-1中的C-末端区域可以与pRb相互作用，在DP-1/E2 F-1异二聚体的情况下，其有助于pRb结合的效率。DP-1/E2 F-1异二聚体与5型腺病毒E4 orf 6/7蛋白特异性相互作用，产生DNA结合活性，其以类似于腺病毒感染期间E4 orf 6/7对DRTF 1/E2 F的调节的方式协同结合两个适当定位的E2 F位点并通过其转录激活。我们得出结论，DP-1是一个常见的和细胞周期调节的DRTF 1/E2 F的组成部分，并在DP-1/E2 F-1异二聚体，它是由pRb和E4 orf 6/7蛋白识别功能重要。
The cellular transcription factor DRTF1/E2F integrates cell cycle events with the transcription apparatus through its cyclical interactions with important regulators of cellular proliferation. Two sequence-specific DNA binding proteins, DP-1 and E2F-1, are components of DRTF1/E2F which synergistically interact in a DP-1/E2F-1 heterodimer. Here, we show that DP-1 is a very frequent, possibly universal, component of DRTF1/E2F in 3T3 cells since it is present in all forms of the DNA binding activity that occur during cell cycle progression. Furthermore, the DP-1 polypeptide, which is phosphorylated, undergoes a phosphorylation-dependent mobility shift during the cell cycle suggesting that its level of phosphorylation is regulated during cell cycle progression. A C-terminal region in DP-1 can interact with pRb which, in the context of the DP-1/E2F-1 heterodimer, contributes to the efficiency of pRb binding. The DP-1/E2F-1 heterodimer specifically interacts with the adenovirus type 5 E4 orf 6/7 protein, to produce a DNA binding activity which binds co-operatively to, and transcriptionally activates through, two appropriately positioned E2F sites in a manner which resembles the regulation of DRTF1/E2F by E4 orf 6/7 during adenovirus infection. We conclude that DP-1 is a frequent and cell cycle-regulated component of DRTF1/E2F, and that in the DP-1/E2F-1 heterodimer it is functionally important for recognition by pRb and the E4 orf 6/7 protein.