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PMID: 11437367 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions of DNA damage.

Biochemical and biophysical research communications ·Vol. 285 ·No. 1 ·2001-07-06 ·Pages 27-31

Oei SL, Shi Y

Abstract

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.

MeSH Terms
Base Sequence DNA Damage DNA Primers DNA-Binding Proteins/metabolism Erythroid-Specific DNA-Binding Factors HeLa Cells Humans Poly(ADP-ribose) Polymerases/metabolism Precipitin Tests Transcription Factors/metabolism YY1 Transcription Factor
Chemicals
DNA Primers DNA-Binding Proteins Erythroid-Specific DNA-Binding Factors Transcription Factors YY1 Transcription Factor YY1 protein, human Poly(ADP-ribose) Polymerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Oei S L
Institut für Biochemie, Freie Universität Berlin, Thielallee 63, Berlin, 14195, Federal Republic of Germany. Lity@chemie.fu-berlin.de
Shi Y
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
2001-07-06
Pages
27-31
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIGMS NIH HHS · GM53874 · United States
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