Interaction of PC4 with melted DNA inhibits transcription.

نویسندگان

  • S Werten
  • G Stelzer
  • A Goppelt
  • F M Langen
  • P Gros
  • H T Timmers
  • P C Van der Vliet
  • M Meisterernst
چکیده

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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عنوان ژورنال:
  • The EMBO journal

دوره 17 17  شماره 

صفحات  -

تاریخ انتشار 1998