ArticleGenes & development2006
The histone variant mH2A1.1 interferes with transcription by down-regulating PARP-1 enzymatic activity.
Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed, 172 citations in OpenAlex.
- Opposing Patterns of the Histone Variant MacroH2A1.1 in Fmr1 Knockout and BTBR T+ Itpr3tf/J Mouse Models of Autism Spectrum Disorder.Molecular neurobiology · 2026Article
- MacroH2A-Mediated Gene Repression through Nucleosome Compaction and Remodeling Inhibition.bioRxiv : the preprint server for biology · 2026Article
- Loss of histone macroH2A1.1 causes kidney abnormalities secondary to a change in nutrient metabolization.Science advances · 2025Article
- Heat Stress-Mediated Multi-Organ Injury: Pathophysiology and Treatment Strategies.Comprehensive Physiology · 2025Review
- HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025Review
- Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024Review
- Identification of a novel DNA oxidative damage repair pathway, requiring the ubiquitination of the histone variant macroH2A1.1.BMC biology · 2024Article
- Transcriptional regulation mechanism of PARP1 and its application in disease treatment.Epigenetics & chromatin · 2024Review
- H2A.Z is involved in premature aging and DSB repair initiation in muscle fibers.Nucleic acids research · 2024Article
- MBD4 loss results in global reactivation of promoters and retroelements with low methylated CpG density.Journal of experimental & clinical cancer research : CR · 2023Article
- Combinatorial targeting of a specific EMT/MET network by macroH2A variants safeguards mesenchymal identity.PloS one · 2023Article
- Review
- The pathogenesis and therapeutic strategies of heat stroke-induced liver injury.Critical care (London, England) · 2022Review
- The high mobility group protein HMG20A cooperates with the histone reader PHF14 to modulate TGFβ and Hippo pathways.Nucleic acids research · 2022Article
- The histone variant macroH2A1.1 regulates RNA polymerase II-paused genes within defined chromatin interaction landscapes.Journal of cell science · 2022Article
- Unconventional metabolites in chromatin regulation.Bioscience reports · 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
- Evolution of a histone variant involved in compartmental regulation of NAD metabolism.Nature structural & molecular biology · 2021Article
- Solid tumours hijack the histone variant network.Nature reviews. Cancer · 2021Review
- Histone variants in skeletal myogenesis.Epigenetics · 2021Review
50 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
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone variant mH2A is believed to be involved in transcriptional repression, but how it exerts its function remains elusive. By using chromatin immunoprecipitation and tandem affinity immunopurification of the mH2A1.1 nucleosome complex, we identified numerous genes with promoters containing mH2A1.1 nucleosomes. In particular, the promoters of the inducible Hsp70.1 and Hsp70.2 genes, but not that of the constitutively expressed Hsp70.8, were highly enriched in mH2A1.1. PARP-1 was identified as a part of the mH2A1.1 nucleosome complex and was found to be associated with the Hsp70.1 promoter. A specific interaction between mH2A1.1 and PARP-1 was demonstrated and found to be associated with inactivation of PARP-1 enzymatic activity. Heat shock released both mH2A1.1 and PARP-1 from the Hsp70.1 promoter and activated PARP-1 automodification activity. The data we present point to a novel mechanism for control of Hsp70.1 gene transcription. mH2A1.1 recruits PARP-1 to the promoter, thereby inactivating it. Upon heat shock, the Hsp70.1 promoter-bound PARP-1 is released to activate transcription through ADP-ribosylation of other Hsp70.1 promoter-bound proteins.
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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.