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- Title
Modulation of DNMT1 activity by ADP-ribose polymers.
- Authors
Reale, Anna; de Matteis, Giovanna; Galleazzi, Giada; Zampieri, Michele; Caiafa, Paola
- Abstract
We provided evidence that competitive inhibition of poly(ADP-ribose) polymerases in mammalian cells treated with 3-aminobenzamide causes DNA hypermethylation in the genome and anomalous hypermethylation of CpG islands. The molecular mechanism(s) connecting poly(ADP-ribosyl)ation with DNA methylation is still unknown. Here we show that DNMT1 is able to bind long and branched ADP-ribose polymers in a noncovalent way. Binding of poly ADP-ribose on DNMT1 inhibits DNA methyltransferase activity. Co-immunoprecipitation reactions indicate that PARP1 and DNMT1 are associated in vivo and that in this complex PARP1 is present in its ADP-ribosylated isoform. We suggest that this complex is catalytically inefficient in DNA methylation.Oncogene (2005) 24, 13-19. doi:10.1038/sj.onc.1208005
- Subjects
RIBOSE; POLYMERS; GENOMES; METHYLATION; DNA; CELLS
- Publication
Oncogene, 2005, Vol 24, Issue 1, p13
- ISSN
0950-9232
- Publication type
Article
- DOI
10.1038/sj.onc.1208005