E2F was originally identified as a transcription factor mediating the transcription of adenovirus E2 gene. It is a heterodimer composed of two structurally related subunits, termed E2F and DP. E2F is encoded by at least five genes, E2F-1 through E2F-5, and DP is encoded by at least two genes, DP-1 and DP-2. All these genes (E2F-1 through E2F-5, DP-1 and DP-2) have been considered as members of the E2F gene family because they have a number of common structural and functional characteristics. Among those members of the E2F family, E2F-1 was the first E2F gene cloned and characterized. The E2F-1 protein has been shown to interact with RB both in vitro and in vivo. Although the E2F proteins can function as transcription factors by themselves, they should be considered as RB-mediators as well because almost every functional response of RB protein(s) requires the presence of E2F protein(s).
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Clear and colorless frozen liquid solution
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Adenovirus infection activates the E2F transcription factor, in part through the formation of a heteromeric protein complex involving a 19 kd E4 gene product that then allows cooperative and stable promoter binding. We now find that cellular factors are complexed
An expression vector was modified to permit the rapid synthesis of purified, 32P-labeled, glutathione S-transferase (GST)-retinoblastoma (RB) fusion proteins. The products were used to screen lambda gt11 expression libraries, from which we cloned a cDNA encoding a polypeptide (RBAP-1) capable
The retinoblastoma protein (pRB) plays an important role in the control of cell proliferation, apparently by binding to and regulating cellular transcription factors such as E2F. Here we describe the characterization of a cDNA clone that encodes a protein with
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