ArticleProtein science : a publication of the Protein Society2002
An inducible helix-Gly-Gly-helix motif in the N-terminal domain of histone H1e: a CD and NMR study.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 34 citations in OpenAlex.
- Linker Histones: The Multiple Binding Modes of the Enigmatic 5th Histone.Biomolecules · 2026Review
- Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2.Scientific reports · 2021Article
- Protein disorder-to-order transition enhances the nucleosome-binding affinity of H1.Nucleic acids research · 2020Article
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- Complex Evolutionary History of the Mammalian Histone H1.1-H1.5 Gene Family.Molecular biology and evolution · 2017Article
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
- Multimerization of Drosophila sperm protein Mst77F causes a unique condensed chromatin structure.Nucleic acids research · 2015Article
- What is the role of histone H1 heterogeneity? A functional model emerges from a 50 year mystery.AIMS biophysics · 2015Article
- N- and C-terminal domains determine differential nucleosomal binding geometry and affinity of linker histone isotypes H1(0) and H1c.The Journal of biological chemistry · 2012Article
- Genetic analysis of phage Mu Mor protein amino acids involved in DNA minor groove binding and conformational changes.The Journal of biological chemistry · 2011Article
- Structure of the H1 C-terminal domain and function in chromatin condensation.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2011Review
- Linker histone H1 is present in centromeric chromatin of living human cells next to inner kinetochore proteins.Nucleic acids research · 2009Article
- Projected [(1)H, (15)N]-HMQC-[ (1)H, (1)H]-NOESY for large molecular systems: application to a 121 kDa protein-DNA complex.Journal of biomolecular NMR · 2008Article
- Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain.Nucleic acids research · 2004Article
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5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Knowledge of the structural properties of linker histones is important to the understanding of their role in higher-order chromatin structure and gene regulation. Here we study the conformational properties of the peptide Ac-EKTPVKKKARKAAGGAKRKTSG-NH(2) (NE-1) by circular dichroism and (1)H-NMR. This peptide corresponds to the positively charged region of the N-terminal domain, adjacent to the globular domain, of mouse histone H1e (residues 15-36). This is the most abundant H1 subtype in many kinds of mammalian somatic cells. NE-1 is mainly unstructured in aqueous solution, but in the presence of the secondary-structure stabilizer trifluoroethanol (TFE) it acquires an alpha-helical structure. In 90% TFE solution the alpha-helical population is approximately 40%. In these conditions, NE-1 is structured in two alpha-helices that comprise almost all the peptide, namely, from Thr17 to Ala27 and from Gly29 to Thr34. Both helical regions are highly amphipathic, with the basic residues on one face of the helix and the apolar ones on the other. The two helical elements are separated by a Gly-Gly motif. Gly-Gly motifs at equivalent positions are found in many vertebrate H1 subtypes. Structure calculations show that the Gly-Gly motif behaves as a flexible linker between the helical regions. The wide range of relative orientations of the helical axes allowed by the Gly-Gly motif may facilitate the tracking of the phosphate backbone by the helical elements or the simultaneous binding of two nonconsecutive DNA segments in chromatin.
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