Cleavage and proteasome-mediated degradation of the basal transcription factor TFIIA

Torill Høiby, Dimitra J. Mitsiou, Huiqing Zhou, Hediye Erdjument-Bromage, Paul Tempst, Hendrik G. Stunnenberg

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

21 Citaten (Scopus)


The transcription factor TFIIA is encoded by two genes, TFIIAαβ and TFIIAγ. In higher eukaryotes, the TFIIAαβ is translated as a precursor and undergoes proteolytic cleavage; the regulation and biological implications of the cleavage have remained elusive. We determined by Edman degradation that the TFIIAβ subunit starts at Asp 278. We found that a cleavage recognition site (CRS), a string of amino acids QVDG at positions -6 to -3 from Asp 278, is essential for cleavage. Mutations in the CRS that prevent cleavage significantly prolong the half-life of TFIIA. Consistently, the cleaved TFIIA is a substrate for the ubiquitin pathway and proteasome-mediated degradation. We show that mutations in the putative phosphorylation sites of TFIIAβ greatly affect degradation of the β-subunit. We propose that cleavage and subsequent degradation fine-tune the amount of TFIIA in the cell and consequently the level of transcription.

Originele taal-2Engels
Pagina's (van-tot)3083-3091
Aantal pagina's9
TijdschriftEMBO Journal
Nummer van het tijdschrift15
StatusGepubliceerd - 4 aug. 2004
Extern gepubliceerdJa


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