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  • Title: Interaction of PC4 with melted DNA inhibits transcription.
    Author: Werten S, Stelzer G, Goppelt A, Langen FM, Gros P, Timmers HT, Van der Vliet PC, Meisterernst M.
    Journal: EMBO J; 1998 Sep 01; 17(17):5103-11. PubMed ID: 9724646.
    Abstract:
    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.
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