ArticlePloS one2013
Structural plasticity in human heterochromatin protein 1β.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Conformational diversity of human HP1α.Protein science : a publication of the Protein Society · 2024Article
- Interplay between charge distribution and DNA in shaping HP1 paralog phase separation and localization.eLife · 2024Article
- Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein.Chemical science · 2022Article
- On the stability and layered organization of protein-DNA condensates.Biophysical journal · 2022Article
- Consistent Force Field Captures Homologue-Resolved HP1 Phase Separation.Journal of chemical theory and computation · 2021Article
- Reorientational Dynamics of Amyloid-β from NMR Spin Relaxation and Molecular Simulation.The journal of physical chemistry letters · 2019Article
- Disruption of an RNA-binding hinge region abolishes LHP1-mediated epigenetic repression.Genes & development · 2017Article
- Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin.Nature communications · 2016Article
- Evidence supporting a critical contribution of intrinsically disordered regions to the biochemical behavior of full-length human HP1γ.Journal of molecular modeling · 2016Article
- Histones: at the crossroads of peptide and protein chemistry.Chemical reviews · 2015Review
- Disruption of both nesprin 1 and desmin results in nuclear anchorage defects and fibrosis in skeletal muscle.Human molecular genetics · 2014Article
- Mechanisms of functional promiscuity by HP1 proteins.Trends in cell biology · 2014Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As essential components of the molecular machine assembling heterochromatin in eukaryotes, HP1 (Heterochromatin Protein 1) proteins are key regulators of genome function. While several high-resolution structures of the two globular regions of HP1, chromo and chromoshadow domains, in their free form or in complex with recognition-motif peptides are available, less is known about the conformational behavior of the full-length protein. Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1β (hHP1β) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners. In addition, the binding pockets within the chromo and chromoshadow domains experience internal dynamics that can be useful for the versatile recognition of different binding partners. In particular, we provide evidence for the presence of a distinct structural propensity in free hHP1β that prepares a binding-competent interface for the formation of the intermolecular β-sheet with methylated histone H3. The structural plasticity of hHP1β supports its ability to bind and connect a wide variety of binding partners in epigenetic processes.
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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.