Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions of DNA damage.
Under conditions of severe DNA damage the nuclear enzyme poly(ADP-ribose) polymerase 1 (PARP-1) is activated, catalyzing the modification of proteins by forming and attaching to them poly(ADP-ribose) chains. A specific physical interaction between PARP-1 and transcription factor Yin Yang 1 (YY1) in vitro was shown previously, which had important consequences for the activities of both proteins. It is demonstrated here that YY1 and PARP-1 form complexes in vivo. YY1 was transiently poly(ADP-ribosyl)ated immediately after genotoxic treatment of HeLa cells. The narrow time frame of the modification coincides with that known for the activation of PARP-1 under these conditions. This immediate modification correlated with a decreased affinity of YY1 to its cognate DNA binding sites.
Oei
S L
SL
Institut für Biochemie, Freie Universität Berlin, Thielallee 63, Berlin, 14195, Federal Republic of Germany. Lity@chemie.fu-berlin.de
Shi
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D001483:Base Sequence; D004249:DNA Damage; D017931:DNA Primers; D004268:DNA-Binding Proteins / Q000378:metabolism*; D050981:Erythroid-Specific DNA-Binding Factors; D006367:HeLa Cells; D006801:Humans; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011233:Precipitin Tests; D014157:Transcription Factors / Q000378:metabolism*; D050986:YY1 Transcription Factor
D017931:DNA Primers; D004268:DNA-Binding Proteins; D050981:Erythroid-Specific DNA-Binding Factors; D014157:Transcription Factors; D050986:YY1 Transcription Factor; C494698:YY1 protein, human; D011065:Poly(ADP-ribose) Polymerases