Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue J Mol Biol Année : 1989

Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA

Résumé

Poly(ADP-ribose)polymerase is a chromatin-associated enzyme of eukaryotic cell nuclei that catalyses the covalent attachment of ADP-ribose units from NAD+ to various nuclear acceptor proteins. This post-translational modification has been postulated to influence several chromatin functions, particularly those where nicking and rejoining of DNA occur. Poly(ADP-ribosyl)ation reactions are strictly dependent upon the presence of interruptions on DNA. We have recently demonstrated that the DNA-binding domain of the protein containing two putative "zinc-fingers" binds DNA in a zinc-dependent manner. The basis for the recognition of the DNA strand breaks by this enzyme, and more precisely, its 29,000 Mr N-terminal part, which contains the metal binding sites, needed to be clarified. DNA probes harbouring a single strand interruption at a defined position were constructed from synthetic oligonucleotides. DNase I protection studies show that poly(ADP-ribose)polymerase specifically binds to a DNA single-strand break by its metal-binding domain depending upon the presence of Zn(II). These results support the idea that the enzyme participates to the maintenance of DNA integrity in eukaryotes.

Dates et versions

hal-02371462 , version 1 (19-11-2019)

Identifiants

Citer

J Menissier-de Murcia, M Molinete, G Gradwohl, F Simonin, G De Murcia. Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA. J Mol Biol, 1989, 210 (1), pp.229-33. ⟨10.1016/0022-2836(89)90302-1⟩. ⟨hal-02371462⟩

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