ArticleJournal of nucleic acids2010
Divalent metal- and high mobility group N protein-dependent nucleosome stability and conformation.
Article in Journal of nucleic acids, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Selective binding of divalent cations reshapes nucleosome mechanics and unlocks histone tail dynamics.Communications biology · 2026Article
- Central gene transcriptional regulatory networks shaping monocyte development in bone marrow.Frontiers in immunology · 2022Article
- PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome.Nature communications · 2019Article
- Specific association of teratogen and toxicant metals in hair of newborns with congenital birth defects or developmentally premature birth in a cohort of couples with documented parental exposure to military attacks: observational study at Al Shifa Hospital, Gaza, Palestine.International journal of environmental research and public health · 2014Observational
- Nucleosome structural changes induced by binding of non-histone chromosomal proteins HMGN1 and HMGN2.FEBS open bio · 2013Article
- Nucleosomal occupancy and CGG repeat expansion: a comparative analysis of triplet repeat region from mouse and human fragile X mental retardation gene 1.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
High mobility group N proteins (HMGNs) bind specifically to the nucleosome core and act as chromatin unfolding and activating factors. Using an all-Xenopus system, we found that HMGN1 and HMGN2 binding to nucleosomes results in distinct ion-dependent conformation and stability. HMGN2 association with nucleosome core particle or nucleosomal array in the presence of divalent metal triggers a reversible transition to a species with much reduced electrophoretic mobility, consistent with a less compact state of the nucleosome. Residues outside of the nucleosome binding domain are required for the activity, which is also displayed by an HMGN1 truncation product lacking part of the regulatory domain. In addition, thermal denaturation assays show that the presence of 1 mM Mg(2+)> or Ca(2+) gives a reduction in nucleosome core terminus stability, which is further substantially diminished by the binding of HMGN2 or truncated HMGN1. Our findings emphasize the importance of divalent metals in nucleosome dynamics and suggest that the differential biological activities of HMGNs in chromatin activation may involve different conformational alterations and modulation of nucleosome core stability.
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Registered trials
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