Literature DB >> 15637587

Modulation of DNMT1 activity by ADP-ribose polymers.

Anna Reale1, Giovanna De Matteis, Giada Galleazzi, Michele Zampieri, Paola Caiafa.   

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.

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Year:  2005        PMID： 15637587     DOI： 10.1038/sj.onc.1208005

Source DB:  PubMed          Journal:  Oncogene        ISSN： 0950-9232            Impact factor:   9.867


  60 in total

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