Reference: Bendjennat M and Weil PA (2008) The transcriptional repressor activator protein Rap1p is a direct regulator of TATA-binding protein. J Biol Chem 283(13):8699-710

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Abstract


Essentially all nuclear eukaryotic gene transcription depends upon the function of the transcription factor TATA-binding protein (TBP). Here we show that the abundant, multifunctional DNA binding transcription factor repressor activator protein Rap1p interacts directly with TBP. TBP-Rap1p binding occurs efficiently in vivo at physiological expression levels, and in vitro analyses confirm that this is a direct interaction. The DNA binding domains of the two proteins mediate interaction between TBP and Rap1p. TBP-Rap1p complex formation inhibits TBP binding to TATA promoter DNA. Alterations in either Rap1p or TBP levels modulate mRNA gene transcription in vivo. We propose that Rap1p represents a heretofore unrecognized regulator of TBP.

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Journal Article | Research Support, N.I.H., Extramural
Authors
Bendjennat M, Weil PA
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