ArticleThe Journal of biological chemistry2011
Double-stranded DNA binding domain of poly(ADP-ribose) polymerase-1 and molecular insight into the regulation of its activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 60 citations in OpenAlex.
- Overcoming Resistance to PARP Inhibitors in BRCA-Mutated Cancers: Mechanisms and Therapeutic Strategies.Journal of Cancer · 2026Review
- Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains.Nucleic acids research · 2025Article
- Non-coding Y RNA fragments in a complex with YBX1 modulate PARP1 residency at DNA double strand breaks.Nucleic acids research · 2025Article
- Targeting DNA damage sensors for cancer therapy.DNA repair · 2025Review
- NEMO is essential for directing the kinases IKKα and ATM to the sites of DNA damage.Science signaling · 2025Article
- RECQL4 requires PARP1 for recruitment to DNA damage, and PARG dePARylation facilitates its associated role in end joining.Experimental & molecular medicine · 2025Article
- Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1.Scientific reports · 2024Article
- Mitochondrial Factors in the Cell Nucleus.International journal of molecular sciences · 2023Review
- LncFALEC recruits ART5/PARP1 and promotes castration-resistant prostate cancer through enhancing PARP1-meditated self PARylation.Cellular oncology (Dordrecht, Netherlands) · 2023Article
- Long non‑coding RNAs in multiple myeloma (Review).International journal of oncology · 2023Review
- Poly(ADP-ribose) in Condensates: The PARtnership of Phase Separation and Site-Specific Interactions.International journal of molecular sciences · 2022Review
- A sePARate phase? Poly(ADP-ribose) versus RNA in the organization of biomolecular condensates.Nucleic acids research · 2022Review
- The expanding universe of PARP1-mediated molecular and therapeutic mechanisms.Molecular cell · 2022Review
- PARP-1 Is a Potential Marker of Retinal Photooxidation and a Key Signal Regulator in Retinal Light Injury.Oxidative medicine and cellular longevity · 2022Review
- Comprehensive analyses identify RIPOR2 as a genomic instability-associated immune prognostic biomarker in cervical cancer.Frontiers in immunology · 2022Article
- The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer.Molecular cell · 2021Article
- Inhibition of PARP1 Dampens Pseudorabies Virus Infection through DNA Damage-Induced Antiviral Innate Immunity.Journal of virology · 2021Article
- The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021Review
- G-Quadruplex loops regulate PARP-1 enzymatic activation.Nucleic acids research · 2021Article
- Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds.Nucleic acids research · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Poly(ADP-ribose) polymerase-1 (PARP-1) modifies various proteins, including itself, with ADP-ribose polymers (automodification). Polymer synthesis is triggered by binding of its zinc finger 1 (Zn1) and 2 (Zn2) to DNA breaks and is followed by inactivation through automodification. The multiple functional domains of PARP-1 appear to regulate activation and automodification-mediated inactivation of PARP-1. However, the roles of these domains in activation-inactivation processes are not well understood. Our results suggest that Zn1, Zn2, and a domain identified in this study, the double-stranded DNA binding (DsDB) domain, are involved in DNA break-dependent activation of PARP-1. We found that binding of the DsDB domain to double-stranded DNA and DNA break recognition by Zn1 and Zn2, whose actual binding targets are likely to be single-stranded DNA, lead to the activation of PARP-1. In turn, the displacement of single- and double-stranded DNA from Zn2 and the DsDB domain caused by ADP-ribose polymer synthesis results in the dissociation of PARP-1 from DNA breaks and thus its inactivation. We also found that the WGR domain is one of the domains involved in the RNA-dependent activation of PARP-1. Furthermore, because zinc finger 3 (Zn3) has the ability to bind to single-stranded RNA, it may have an indirect role in RNA-dependent activation. PARP-1 functional domains, which are involved in oligonucleic acid binding, therefore coordinately regulate PARP-1 activity depending on the status of the neighboring oligonucleic acids. Based on these results, we proposed a model for the regulation of PARP-1 activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.