ArticleThe Journal of biological chemistry2010
The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 162 citations in OpenAlex.
- Computational Evaluation of Novel PARP-1 Inhibitors for Breast Cancer: Docking, Molecular Dynamics, MM/GBSA, DFT and ADMET Calculations.Pharmaceuticals (Basel, Switzerland) · 2026Article
- NADCell reports · 2026Article
- PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation.Nature communications · 2026Article
- The zinc finger domains of PARP-1 are selectively and potently inhibited by the Au(I)-based drugs sodium aurothiomalate and aurothioglucose.FEBS letters · 2025Article
- Review
- A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation.Molecular cell · 2025Article
- PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells.Cell death & disease · 2024Article
- AKT-dependent nuclear localization of EPRS1 activates PARP1 in breast cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- PARP trapping is governed by the PARP inhibitor dissociation rate constant.Cell chemical biology · 2024Article
- PARP-ish: Gaps in Molecular Understanding and Clinical Trials Targeting PARP Exacerbate Racial Disparities in Prostate Cancer.Cancer research · 2024Review
- PARP14 correlates with GBM proliferation and poor prognosis by elevating expression of SAMD/SAMD9L.Irish journal of medical science · 2024Article
- Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1.Scientific reports · 2024Article
- A computational model of the DNA damage-induced IKK/ NF-κB pathway reveals a critical dependence on irradiation dose and PARP-1.iScience · 2023Article
- The expanding universe of PARP1-mediated molecular and therapeutic mechanisms.Molecular cell · 2022Review
- Article
- Truncated PARP1 mediates ADP-ribosylation of RNA polymerase III for apoptosis.Cell discovery · 2022Article
- Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022Review
- HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.Nature communications · 2021Article
- Mechanisms of Nucleosome Reorganization by PARP1.International journal of molecular sciences · 2021Article
- Role of PARP in TNBC: Mechanism of Inhibition, Clinical Applications, and Resistance.Biomedicines · 2021Review
24 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
PARP-1 is involved in multiple cellular processes, including transcription, DNA repair, and apoptosis. PARP-1 attaches ADP-ribose units to target proteins, including itself as a post-translational modification that can change the biochemical properties of target proteins and mediate recruitment of proteins to sites of poly(ADP-ribose) synthesis. Independent of its catalytic activity, PARP-1 binds to chromatin and promotes compaction affecting RNA polymerase II transcription. PARP-1 has a modular structure composed of six independent domains. Two homologous zinc fingers, Zn1 and Zn2, form the DNA-binding module. Zn1-Zn2 binding to DNA breaks triggers catalytic activity. Recently, we have identified a third zinc binding domain in PARP-1, the Zn3 domain, which is essential for DNA-dependent PARP-1 activity. The crystal structure of the Zn3 domain revealed a novel zinc-ribbon fold and a homodimeric Zn3 structure that formed in the crystal lattice. Structure-guided mutagenesis was used here to investigate the roles of these two features of the Zn3 domain. Our results indicate that the zinc-ribbon fold of the Zn3 domain mediates an interdomain contact crucial to assembly of the DNA-activated conformation of PARP-1. In contrast, residues located at the Zn3 dimer interface are not required for DNA-dependent activation but rather make important contributions to the chromatin compaction activity of PARP-1. Thus, the Zn3 domain has dual roles in regulating the functions of PARP-1.
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