ArticleThe Journal of biological chemistry2012
HMGN1 protein regulates poly(ADP-ribose) polymerase-1 (PARP-1) self-PARylation in mouse fibroblasts.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- GPCR systems coordinate cellular resilience against aging-associated stress.Frontiers in molecular biosciences · 2026Review
- Progression of monoclonal gammopathy of undetermined significance to multiple myeloma is associated with enhanced translational quality control and overall loss of surface antigens.Journal of translational medicine · 2024Article
- Comprehensive proteogenomic characterization of early duodenal cancer reveals the carcinogenesis tracks of different subtypes.Nature communications · 2023Article
- Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.Computational and structural biotechnology journal · 2023Review
- HMGB3 promotes PARP inhibitor resistance through interacting with PARP1 in ovarian cancer.Cell death & disease · 2022Article
- The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity.Frontiers in cell and developmental biology · 2022Article
- The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021Review
- Article
- Human HMGN1 and HMGN2 are not required for transcription-coupled DNA repair.Scientific reports · 2020Article
- Biological Functions of HMGN Chromosomal Proteins.International journal of molecular sciences · 2020Review
- Altered transcriptional regulatory proteins in glioblastoma and YBX1 as a potential regulator of tumor invasion.Scientific reports · 2019Article
- Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins.Nucleic acids research · 2019Review
- NADPNature communications · 2019Article
- HMGA2 as a functional antagonist of PARP1 inhibitors in tumor cells.Molecular oncology · 2019Article
- The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors.Oncotarget · 2018Article
- XRCC1 phosphorylation affects aprataxin recruitment and DNA deadenylation activity.DNA repair · 2018Article
- XRCC1-mediated repair of strand breaks independent of PNKP binding.DNA repair · 2017Article
- Role of the oxidized form of XRCC1 in protection against extreme oxidative stress.Free radical biology & medicine · 2017Article
- Article
- Sam68 Is Required for DNA Damage Responses via Regulating Poly(ADP-ribosyl)ation.PLoS biology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
In mammalian cells, the nucleosome-binding protein HMGN1 (high mobility group N1) affects the structure and function of chromatin and plays a role in repair of damaged DNA. HMGN1 affects the interaction of DNA repair factors with chromatin and their access to damaged DNA; however, not all of the repair factors affected have been identified. Here, we report that HMGN1 affects the self-poly(ADP-ribosyl)ation (i.e., PARylation) of poly(ADP-ribose) polymerase-1 (PARP-1), a multifunctional and abundant nuclear enzyme known to recognize DNA lesions and promote chromatin remodeling, DNA repair, and other nucleic acid transactions. The catalytic activity of PARP-1 is activated by DNA with a strand break, and this results in self-PARylation and PARylation of other chromatin proteins. Using cells obtained from Hmgn1(-/-) and Hmgn1(+/+) littermate mice, we find that in untreated cells, loss of HMGN1 protein reduces PARP-1 self-PARylation. A similar result was obtained after MMS treatment of these cells. In imaging experiments after low energy laser-induced DNA damage, less PARylation at lesion sites was observed in Hmgn1(-/-) than in Hmgn1(+/+) cells. The HMGN1 regulation of PARP-1 activity could be mediated by direct protein-protein interaction as HMGN1 and PARP-1 were found to interact in binding assays. Purified HMGN1 was able to stimulate self-PARylation of purified PARP-1, and in experiments with cell extracts, self-PARylation was greater in Hmgn1(+/+) than in Hmgn1(-/-) extract. The results suggest a regulatory role for HMGN1 in PARP-1 activation.
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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.