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Corepressor Required for Adenovirus E1B 55,000-molecular-weight Protein Repression of Basal Transcription

Overview
Journal Mol Cell Biol
Specialty Cell Biology
Date 1999 Apr 17
PMID 10207064
Citations 27
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Abstract

Adenovirus E1B 55,000-molecular-weight protein (55K) binds to host cell p53, stabilizing it, greatly increasing its affinity for its cognate DNA-binding site, and converting it from a regulated activator to a constitutive repressor. Here we analyzed the mechanism of repression by the p53-E1B 55K complex. E1B 55K repression requires that 55K be tethered to the promoter by binding directly to DNA-bound p53. Transcription from an assembled, p53-activated preinitiation complex was not repressed by the subsequent addition of E1B 55K, suggesting that either sites of 55K interaction with p53 or targets of 55K in the preinitiation complex are blocked. Specific E1B 55K repression was observed in reactions lacking TFIIA and with recombinant TATA-binding protein in place of TFIID, conditions under which p53 does not activate transcription. Thus, E1B 55K does not simply inhibit a p53-specific activation mechanism but rather blocks basal transcription. As a consequence, E1B 55K may repress transcription from any promoter with an associated p53-binding site, no matter what other activators associate with the promoter. E1B 55K did not repress basal transcription in reactions with recombinant and highly purified general transcription factors and RNA polymerase II but rather required a corepressor that copurifies with the polymerase.

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References
1.
Sarnow P, Ho Y, Williams J, Levine A . Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells. Cell. 1982; 28(2):387-94. DOI: 10.1016/0092-8674(82)90356-7. View

2.
Lillie J, Green M . Transcription activation by the adenovirus E1a protein. Nature. 1989; 338(6210):39-44. DOI: 10.1038/338039a0. View

3.
Thompson N, Aronson D, Burgess R . Purification of eukaryotic RNA polymerase II by immunoaffinity chromatography. Elution of active enzyme with protein stabilizing agents from a polyol-responsive monoclonal antibody. J Biol Chem. 1990; 265(12):7069-77. View

4.
Kao C, Yew P, Berk A . Domains required for in vitro association between the cellular p53 and the adenovirus 2 E1B 55K proteins. Virology. 1990; 179(2):806-14. DOI: 10.1016/0042-6822(90)90148-k. View

5.
Hengartner C, Thompson C, Zhang J, Chao D, Liao S, Koleske A . Association of an activator with an RNA polymerase II holoenzyme. Genes Dev. 1995; 9(8):897-910. DOI: 10.1101/gad.9.8.897. View