Peter Weil
Faculty Member
Last active: 11/4/2015

The transcriptional repressor activator protein Rap1p is a direct regulator of TATA-binding protein.

Bendjennat M, Weil PA
J Biol Chem. 2008 283 (13): 8699-710

PMID: 18195009 · PMCID: PMC2417159 · DOI:10.1074/jbc.M709436200

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.

MeSH Terms (15)

DNA, Fungal Gene Expression Regulation, Fungal Models, Molecular Nucleic Acid Conformation Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary RNA, Messenger Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins TATA-Box Binding Protein Telomere-Binding Proteins Transcription, Genetic Transcription Factors Up-Regulation

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