Chromatin unfolding and activation by HMGN**The nomenclature of the HMG protein superfamily has been recently revised (see Ref. 12 and http://www.informatics.jax.org/mgihome/nomen/genefamilies/hmgfamily.shtml). chromosomal proteins

Bustin, Michael

doi:10.1016/s0968-0004(01)01855-2

Cited by 162 publications

(32 citation statements)

References 55 publications

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“…4), stabilizes the position of the nucleosomes at these TSS—an unexpected finding, since HMGN proteins stabilize the structure of isolated nucleosomes (48) and loss of the protein would therefore be expected to sensitize the released nucleosomes to further digestion. Several mechanisms could account for the effects of HMGN1 on nucleosome positioning and stability.…”

Section: Discussionmentioning

confidence: 98%

HMGN1 Modulates Nucleosome Occupancy and DNase I Hypersensitivity at the CpG Island Promoters of Embryonic Stem Cells

Deng

Zhu

Zhang

et al. 2013

Molecular and Cellular Biology

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Chromatin structure plays a key role in regulating gene expression and embryonic differentiation; however, the factors that determine the organization of chromatin around regulatory sites are not fully known. Here we show that HMGN1, a nucleosome-binding protein ubiquitously expressed in vertebrate cells, preferentially binds to CpG island-containing promoters and affects the organization of nucleosomes, DNase I hypersensitivity, and the transcriptional profile of mouse embryonic stem cells and neural progenitors. Loss of HMGN1 alters the organization of an unstable nucleosome at transcription start sites, reduces the number of DNase I-hypersensitive sites genome wide, and decreases the number of nestin-positive neural progenitors in the subventricular zone (SVZ) region of mouse brain. Thus, architectural chromatin-binding proteins affect the transcription profile and chromatin structure during embryonic stem cell differentiation.

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Section: Discussionmentioning

confidence: 98%

HMGN1 Modulates Nucleosome Occupancy and DNase I Hypersensitivity at the CpG Island Promoters of Embryonic Stem Cells

Deng

Zhu

Zhang

et al. 2013

Molecular and Cellular Biology

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“…HMGN1 and HMGN2, the major variants of the HMGN protein family (40), compete for nucleosome binding sites and have similar effects on chromatin structure (9,12). HMGN1 was shown to be highly expressed throughout all mouse preimplantation stages (8).…”

Section: Resultsmentioning

confidence: 99%

Interplay between H1 and HMGN epigenetically regulates OLIG1&2 expression and oligodendrocyte differentiation

Deng

Postnikov

Zhang

et al. 2016

Nucleic Acids Research

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An interplay between the nucleosome binding proteins H1 and HMGN is known to affect chromatin dynamics, but the biological significance of this interplay is still not clear. We find that during embryonic stem cell differentiation loss of HMGNs leads to down regulation of genes involved in neural differentiation, and that the transcription factor OLIG2 is a central node in the affected pathway. Loss of HMGNs affects the expression of OLIG2 as well as that of OLIG1, two transcription factors that are crucial for oligodendrocyte lineage specification and nerve myelination. Loss of HMGNs increases the chromatin binding of histone H1, thereby recruiting the histone methyltransferase EZH2 and elevating H3K27me3 levels, thus conferring a repressive epigenetic signature at Olig1&2 sites. Embryonic stem cells lacking HMGNs show reduced ability to differentiate towards the oligodendrocyte lineage, and mice lacking HMGNs show reduced oligodendrocyte count and decreased spinal cord myelination, and display related neurological phenotypes. Thus, the presence of HMGN proteins is required for proper expression of neural differentiation genes during embryonic stem cell differentiation. Specifically, we demonstrate that the dynamic interplay between HMGNs and H1 in chromatin epigenetically regulates the expression of OLIG1&2, thereby affecting oligodendrocyte development and myelination, and mouse behavior.

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“…The nucleosome binding domain contains the invariant octapeptide RRSARLSA which serves as the signature motif of this protein family [3, 20]. As elaborated below, this octapeptide serves as the anchoring point of HMGNs on the nucleosome [20].…”

Section: Hmg Proteinsmentioning

confidence: 99%

Functional interplay between histone H1 and HMG proteins in chromatin

Postnikov

Bustin

2016

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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The dynamic interaction of nucleosome binding proteins with their chromatin targets is an important element in regulating the structure and function of chromatin. Histone H1 variants and High Mobility Group (HMG) proteins are ubiquitously expressed in all vertebrate cells, bind dynamically to chromatin, and are known to affect chromatin condensation and the ability of regulatory factors to access their genomic binding sites. Here, we review the studies that focus on the interactions between H1 and HMGs and highlight the functional consequences of the interplay between these architectural chromatin binding proteins. H1 and HMG proteins are mobile molecules that bind to nucleosomes as members of a dynamic protein network. All HMGs compete with H1 for chromatin binding sites, in a dose dependent fashion, but each HMG family has specific effects on the interaction of H1 with chromatin. The interplay between H1 and HMGs affects chromatin organization and plays a role in epigenetic regulation.

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Chromatin unfolding and activation by HMGN**The nomenclature of the HMG protein superfamily has been recently revised (see Ref. 12 and http://www.informatics.jax.org/mgihome/nomen/genefamilies/hmgfamily.shtml). chromosomal proteins

Cited by 162 publications

References 55 publications

HMGN1 Modulates Nucleosome Occupancy and DNase I Hypersensitivity at the CpG Island Promoters of Embryonic Stem Cells

HMGN1 Modulates Nucleosome Occupancy and DNase I Hypersensitivity at the CpG Island Promoters of Embryonic Stem Cells

Interplay between H1 and HMGN epigenetically regulates OLIG1&2 expression and oligodendrocyte differentiation

Functional interplay between histone H1 and HMG proteins in chromatin

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