ArticleMolecular and cellular biology2007
The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
88 citing papers in PubMed, 140 citations in OpenAlex.
- PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026Article
- Review
- Nucleoplasmic Lamin A/C controls replication fork restart upon stress by modulating local H3K9me3 and ADP-ribosylation levels.Nature communications · 2025Article
- PARP1 as an Epigenetic Modulator: Implications for the Regulation of Host-Viral Dynamics.Pathogens (Basel, Switzerland) · 2024Review
- Therapeutic targeting of PARP with immunotherapy in acute myeloid leukemia.Frontiers in pharmacology · 2024Review
- Review
- PARP1 modulates METTL3 promoter chromatin accessibility and associated LPAR5 RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- PARP3 Affects Nucleosome Compaction Regulation.International journal of molecular sciences · 2023Article
- Cooperative targeting of PARP-1 domains to regulate metabolic and developmental genes.Frontiers in endocrinology · 2023Article
- Review
- Identification of a novel GR-ARID1a-P53BP1 protein complex involved in DNA damage repair and cell cycle regulation.Oncogene · 2022Article
- Human PARP1 Facilitates Transcription through a Nucleosome and Histone Displacement by Pol II In Vitro.International journal of molecular sciences · 2022Article
- The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer.Molecular cell · 2021Article
- XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair.Nature cell biology · 2021Article
- Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single-molecule measurements reveal that PARP1 condenses DNA by loop stabilization.Science advances · 2021Article
- Differential immunomodulatory effect of PARP inhibition in BRCA1 deficient and competent tumor cells.Biochemical pharmacology · 2021Article
- Mitochondrial NADMolecular cell · 2021Article
- Decoding the rosetta stone of mitonuclear communication.Pharmacological research · 2020Review
- Poly(ADP-ribose) Polymerase 1 (PARP1) restrains MyoD-dependent gene expression during muscle differentiation.Scientific reports · 2020Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We explored the mechanisms of chromatin compaction and transcriptional regulation by poly(ADP-ribose) polymerase 1 (PARP-1), a nucleosome-binding protein with an NAD(+)-dependent enzymatic activity. By using atomic force microscopy and a complementary set of biochemical assays with reconstituted chromatin, we showed that PARP-1 promotes the localized compaction of chromatin into supranucleosomal structures in a manner independent of the amino-terminal tails of core histones. In addition, we defined the domains of PARP-1 required for nucleosome binding, chromatin compaction, and transcriptional repression. Our results indicate that the DNA binding domain (DBD) of PARP-1 is necessary and sufficient for binding to nucleosomes, yet the DBD alone is unable to promote chromatin compaction and only partially represses RNA polymerase II-dependent transcription in an in vitro assay with chromatin templates (approximately 50% of the repression observed with wild-type PARP-1). Furthermore, our results show that the catalytic domain of PARP-1, which does not bind nucleosomes on its own, cooperates with the DBD to promote chromatin compaction and efficient transcriptional repression in a manner independent of its enzymatic activity. Collectively, our results have revealed a novel function for the catalytic domain in chromatin compaction. In addition, they show that the DBD and catalytic domain cooperate to regulate chromatin structure and chromatin-dependent transcription, providing mechanistic insights into how these domains contribute to the chromatin-dependent functions of PARP-1.
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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.