ArticleMolecular and cellular biology2001
Mitotic phosphorylation prevents the binding of HMGN proteins to chromatin.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 75 citations in OpenAlex.
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.Genes & development · 2025Article
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.bioRxiv : the preprint server for biology · 2025Article
- Review
- Shaking up the silence: consequences of HMGN1 antagonizing PRC2 in the Down syndrome brain.Epigenetics & chromatin · 2022Review
- H3K27ac nucleosomes facilitate HMGN localization at regulatory sites to modulate chromatin binding of transcription factors.Communications biology · 2022Article
- Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2-nucleosome association.RSC chemical biology · 2021Article
- Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications.RSC chemical biology · 2021Article
- Trisomy of a Down Syndrome Critical Region Globally Amplifies Transcription via HMGN1 Overexpression.Cell reports · 2018Article
- Interplay between H1 and HMGN epigenetically regulates OLIG1&2 expression and oligodendrocyte differentiation.Nucleic acids research · 2017Article
- Serine ADP-Ribosylation Depends on HPF1.Molecular cell · 2017Article
- Real-time monitoring of PtaHMGB activity in poplar transactivation assays.Plant methods · 2017Article
- Nucleosome structure and function.Chemical reviews · 2015Review
- Evolution of high mobility group nucleosome-binding proteins and its implications for vertebrate chromatin specialization.Molecular biology and evolution · 2015Article
- DEK over-expression promotes mitotic defects and micronucleus formation.Cell cycle (Georgetown, Tex.) · 2015Article
- High mobility group nucleosomal binding domain 2 (HMGN2) SUMOylation by the SUMO E3 ligase PIAS1 decreases the binding affinity to nucleosome core particles.The Journal of biological chemistry · 2014Article
- The chromatin architectural proteins HMGD1 and H1 bind reciprocally and have opposite effects on chromatin structure and gene regulation.BMC genomics · 2014Article
- The role of the nucleosome acidic patch in modulating higher order chromatin structure.Journal of the Royal Society, Interface · 2013Review
- The HMGN family of chromatin-binding proteins: dynamic modulators of epigenetic processes.Biochimica et biophysica acta · 2012Review
- The nucleosome binding protein HMGN1 interacts with PCNA and facilitates its binding to chromatin.Molecular and cellular biology · 2012Article
- High-mobility group nucleosome-binding protein 1 acts as an alarmin and is critical for lipopolysaccharide-induced immune responses.The Journal of experimental medicine · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Condensation of the chromatin fiber and transcriptional inhibition during mitosis is associated with the redistribution of many DNA- and chromatin-binding proteins, including members of the high-mobility-group N (HMGN) family. Here we study the mechanism governing the organization of HMGN proteins in mitosis. Using site-specific antibodies and quantitative gel analysis with proteins extracted from synchronized HeLa cells, we demonstrate that, during mitosis, the conserved serine residues in the nucleosomal binding domain (NBD) of this protein family are highly and specifically phosphorylated. Nucleosome mobility shift assays with both in vitro-phosphorylated proteins and with point mutants bearing negative charges in the NBD demonstrate that the negative charge abolishes the ability of the proteins to bind to nucleosomes. Fluorescence loss of photobleaching demonstrates that, in living cells, the negative charge in the NBD increases the intranuclear mobility of the protein and significantly decreases the relative time that it is bound to chromatin. Expression of wild-type and mutant proteins in HmgN1(-/-) cells indicates that the negatively charged protein is not bound to chromosomes. We conclude that during mitosis the NBD of HMGN proteins is highly phosphorylated and that this modification regulates the interaction of the proteins with chromatin.
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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.