ArticleThe Biochemical journal2012
The chromatin-binding protein HMGN3 stimulates histone acetylation and transcription across the Glyt1 gene.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
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- Transcriptional regulation of solute carrier family 6 member 9 gene.Molecular biology reports · 2025Article
- H3K14: A histone site closely related to diseases.Journal of Cancer · 2025Review
- DNA G-Quadruplexes Contribute to CTCF Recruitment.International journal of molecular sciences · 2021Article
- Biological Functions of HMGN Chromosomal Proteins.International journal of molecular sciences · 2020Review
- Maintenance of active chromatin states by HMGN2 is required for stem cell identity in a pluripotent stem cell model.Epigenetics & chromatin · 2019Article
- A Genome Model to Explain Major Features of Neurodevelopmental Disorders in Newborns.Biomedical informatics insights · 2019Article
- Article
- Cap-independent translation by DAP5 controls cell fate decisions in human embryonic stem cells.Genes & development · 2016Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- E2F1 coregulates cell cycle genes and chromatin components during the transition of oligodendrocyte progenitors from proliferation to differentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Glycine transporters as novel therapeutic targets in schizophrenia, alcohol dependence and pain.Nature reviews. Drug discovery · 2013Review
- ATF4-dependent regulation of the JMJD3 gene during amino acid deprivation can be rescued in Atf4-deficient cells by inhibition of deacetylation.The Journal of biological chemistry · 2012Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
HMGNs are nucleosome-binding proteins that alter the pattern of histone modifications and modulate the binding of linker histones to chromatin. The HMGN3 family member exists as two splice forms, HMGN3a which is full-length and HMGN3b which lacks the C-terminal RD (regulatory domain). In the present study, we have used the Glyt1 (glycine transporter 1) gene as a model system to investigate where HMGN proteins are bound across the locus in vivo, and to study how the two HMGN3 splice variants affect histone modifications and gene expression. We demonstrate that HMGN1, HMGN2, HMGN3a and HMGN3b are bound across the Glyt1 gene locus and surrounding regions, and are not enriched more highly at the promoter or putative enhancer. We conclude that the peaks of H3K4me3 (trimethylated Lys(4) of histone H3) and H3K9ac (acetylated Lys(9) of histone H3) at the active Glyt1a promoter do not play a major role in recruiting HMGN proteins. HMGN3a/b binding leads to increased H3K14 (Lys(14) of histone H3) acetylation and stimulates Glyt1a expression, but does not alter the levels of H3K4me3 or H3K9ac enrichment. Acetylation assays show that HMGN3a stimulates the ability of PCAF [p300/CREB (cAMP-response-element-binding protein)-binding protein-associated factor] to acetylate nucleosomal H3 in vitro, whereas HMGN3b does not. We propose a model where HMGN3a/b-stimulated H3K14 acetylation across the bodies of large genes such as Glyt1 can lead to more efficient transcription elongation and increased mRNA production.
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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.