Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair
| Autor: | John B. Leppard, Zachary B. Mackey, Alan E. Tomkinson, Zhiwan Dong |
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| Rok vydání: | 2003 |
| Předmět: |
Time Factors
DNA Ligases DNA Repair Poly ADP ribose polymerase DNA polymerase II Recombinant Fusion Proteins Immunoblotting Biology Xenopus Proteins Mass Spectrometry XRCC1 DNA Ligase ATP Two-Hybrid System Techniques Deoxyribonuclease I Humans Poly-ADP-Ribose Binding Proteins Molecular Biology Glutathione Transferase chemistry.chemical_classification Cell Nucleus DNA ligase DNA clamp Okazaki fragments Cell Biology Surface Plasmon Resonance Molecular biology Precipitin Tests DNA Dynamics and Chromosome Structure Protein Structure Tertiary DNA-Binding Proteins X-ray Repair Cross Complementing Protein 1 chemistry biology.protein Poly(ADP-ribose) Polymerases DNA polymerase mu Nucleotide excision repair DNA Damage HeLa Cells Plasmids Subcellular Fractions |
| Zdroj: | Molecular and cellular biology. 23(16) |
| ISSN: | 0270-7306 |
| Popis: | The repair of DNA single-strand breaks in mammalian cells is mediated by poly(ADP-ribose) polymerase 1 (PARP-1), DNA ligase IIIalpha, and XRCC1. Since these proteins are not found in lower eukaryotes, this DNA repair pathway plays a unique role in maintaining genome stability in more complex organisms. XRCC1 not only forms a stable complex with DNA ligase IIIalpha but also interacts with several other DNA repair factors. Here we have used affinity chromatography to identify proteins that associate with DNA ligase III. PARP-1 binds directly to an N-terminal region of DNA ligase III immediately adjacent to its zinc finger. In further studies, we have shown that DNA ligase III also binds directly to poly(ADP-ribose) and preferentially associates with poly(ADP-ribosyl)ated PARP-1 in vitro and in vivo. Our biochemical studies have revealed that the zinc finger of DNA ligase III increases DNA joining in the presence of either poly(ADP-ribosyl)ated PARP-1 or poly(ADP-ribose). This provides a mechanism for the recruitment of the DNA ligase IIIalpha-XRCC1 complex to in vivo DNA single-strand breaks and suggests that the zinc finger of DNA ligase III enables this complex and associated repair factors to locate the strand break in the presence of the negatively charged poly(ADP-ribose) polymer. |
| Databáze: | OpenAIRE |
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