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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Interaction of PC4 with melted DNA inhibits transcription.

PC4 is a nuclear DNA-binding protein that stimulates activator-dependent class II gene transcription in vitro. Recent biochemical and X-ray analyses have revealed a unique structure within the C-terminal domain of PC4 that binds tightly to unpaired double-stranded (ds)DNA. The cellular function of this evolutionarily conserved dimeric DNA-binding fold is unknown. Here we demonstrate that PC4 represses transcription through this motif. Interaction with melted promoters is not required for activator-dependent transcription in vitro. The inhibitory activity is attenuated on bona fide promoters by (i) transcription factor TFIIH and (ii) phosphorylation of PC4. PC4 remains a potent inhibitor of transcription in regions containing unpaired ds DNA, in single-stranded DNA that can fold into two antiparallel strands, and on DNA ends. Our observations are consistent with a novel inhibitory function of PC4.[1]


  1. Interaction of PC4 with melted DNA inhibits transcription. Werten, S., Stelzer, G., Goppelt, A., Langen, F.M., Gros, P., Timmers, H.T., Van der Vliet, P.C., Meisterernst, M. EMBO J. (1998) [Pubmed]
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