ArticleProceedings of the National Academy of Sciences of the United States of America2019
Hit and run versus long-term activation of PARP-1 by its different domains fine-tunes nuclear processes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 96 citations in OpenAlex.
- PARP1 and PARylation facilitate transcription-coupled DNA repair by stabilizing the CSB-RNAPII complex.Nucleic acids research · 2025Article
- PARP1 and PARG Are the Draft Horses for Polycomb-Trithorax Chromatin Regulator Machinery.Biomolecules · 2025Article
- Article
- Disordered Protein Tail Is Wagging Poly(ADP-ribosyl)ation.International journal of molecular sciences · 2025Article
- Single nucleosome imaging reveals principles of transient multiscale chromatin reorganization triggered by histone ADP-ribosylation at DNA lesions.Nature communications · 2025Article
- Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1.Biomolecules · 2024Article
- Adaptive genetic mechanisms in mammalian Parp1 locus.G3 (Bethesda, Md.) · 2024Article
- Transcriptional regulation mechanism of PARP1 and its application in disease treatment.Epigenetics & chromatin · 2024Review
- ATM and 53BP1 regulate alternative end joining-mediated V(D)J recombination.Science advances · 2024Article
- PARP-ish: Gaps in Molecular Understanding and Clinical Trials Targeting PARP Exacerbate Racial Disparities in Prostate Cancer.Cancer research · 2024Review
- PARG Protein Regulation Roles inInternational journal of molecular sciences · 2024Article
- Article
- Article
- PARP-1 is a transcriptional rheostat of metabolic and bivalent genes during development.Life science alliance · 2024Article
- Poly(ADP-ribosyl)ating enzymes coordinate changes in the expression of metabolic genes with developmental progression.Scientific reports · 2023Article
- Exploring the interplay between PARP1 and circRNA biogenesis and function.Wiley interdisciplinary reviews. RNA · 2023Review
- PARP1 modulates METTL3 promoter chromatin accessibility and associated LPAR5 RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- Review
- PARPs and ADP-Ribosylation in Chronic Inflammation: A Focus on Macrophages.Pathogens (Basel, Switzerland) · 2023Review
- Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling.Nature communications · 2023Article
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(ADP-ribose) polymerase 1 (PARP-1) is a multidomain multifunctional nuclear enzyme involved in the regulation of the chromatin structure and transcription. PARP-1 consists of three functional domains: the N-terminal DNA-binding domain (DBD) containing three zinc fingers, the automodification domain (A), and the C-terminal domain, which includes the protein interacting WGR domain (W) and the catalytic (Cat) subdomain responsible for the poly(ADP ribosyl)ating reaction. The mechanisms coordinating the functions of these domains and determining the positioning of PARP-1 in chromatin remain unknown. Using multiple deletional isoforms of PARP-1, lacking one or another of its three domains, as well as consisting of only one of those domains, we demonstrate that different functions of PARP-1 are coordinated by interactions among these domains and their targets. Interaction between the DBD and damaged DNA leads to a short-term binding and activation of PARP-1. This "hit and run" activation of PARP-1 initiates the DNA repair pathway at a specific point. The long-term chromatin loosening required to sustain transcription takes place when the C-terminal domain of PARP-1 binds to chromatin by interacting with histone H4 in the nucleosome. This long-term activation of PARP-1 results in a continuous accumulation of pADPr, which maintains chromatin in the loosened state around a certain locus so that the transcription machinery has continuous access to DNA. Cooperation between the DBD and C-terminal domain occurs in response to heat shock (HS), allowing PARP-1 to scan chromatin for specific binding sites.
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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.