Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (347K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (22)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Süsse, S.
Right arrow Articles by Wiesmüller, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Süsse, S.
Right arrow Articles by Wiesmüller, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 2 February 2004

Nucleic Acids Research, 2004, Vol. 32, No. 2 669-680
© 2004 Oxford University Press

Poly(ADP-ribose) polymerase (PARP-1) and p53 independently function in regulating double-strand break repair in primate cells

Silke Süsse1,2, Claus-Jürgen Scholz1, Alexander Bürkle3 and Lisa Wiesmüller*,1,2

1 Universitätsfrauenklinik, Prittwitzstrasse 43, D-89075 Ulm, 2 Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, Martinistraße 52, D-20251 Hamburg and 3 Molecular Toxicology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany

*To whom correspondence should be addressed. Tel: +49 731 500 27640; Fax: +49 731 500 26674; Email: lisa.wiesmueller{at}medizin.uni-ulm.de

PARP-1 is rapidly activated by DNA strand breaks, which finally leads to the modulation of multiple protein activities in DNA replication, DNA repair and checkpoint control. PARP-1 may be involved in homologous recombination, and poly(ADP-ribosyl)ation of p53 represents one possible mechanism that activates p53 as a recombination surveillance factor. Here, we examined the influence of PARP-1 on homology-directed double-strand break (DSB) repair by use of a fluorescence- and I-SceI- meganuclease-based assay with either episomal or chromosomally integrated DNA substrates. Surprisingly, the transient expression of both full-length PARP-1 and of a dominant negative mutant, retaining the DNA-binding but lacking the catalytic domain, down-regulated DSB repair in a dose-dependent manner. This effect was seen regardless of p53 status, however, with enhanced inhibition in the presence of wild-type p53. Taken together, our data reveal that PARP-1 overexpression counteracts DSB repair independently of its enzymatic activity and of poly(ADP-ribosyl)ation of p53 in particular, but synergizes with p53 in suppressing chromosomal rearrangements.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
M. Wang, W. Wu, W. Wu, B. Rosidi, L. Zhang, H. Wang, and G. Iliakis
PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways
Nucleic Acids Res., December 4, 2006; 34(21): 6170 - 6182.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
C. Baumann, G. S. Boehden, A. Burkle, and L. Wiesmuller
Poly(ADP-RIBOSE) polymerase-1 (Parp-1) antagonizes topoisomerase I-dependent recombination stimulation by P53
Nucleic Acids Res., February 9, 2006; 34(3): 1036 - 1049.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
H. Wang, B. Rosidi, R. Perrault, M. Wang, L. Zhang, F. Windhofer, and G. Iliakis
DNA Ligase III as a Candidate Component of Backup Pathways of Nonhomologous End Joining
Cancer Res., May 15, 2005; 65(10): 4020 - 4030.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.