Histone H3 and H4 N-Terminal Tails in Nucleosome Arrays at Cellular Concentrations Probed by Magic Angle Spinning NMR Spectroscopy.
J Am Chem Soc. 2013 Oct 2;
Authors: Gao M, Nadaud PS, Bernier MW, North JA, Hammel PC, Poirier MG, Jaroniec CP
Abstract
Chromatin is a supramolecular assembly of DNA and histone proteins, organized into nucleosome repeat units. The dynamics of chromatin organization regulates DNA accessibility to eukaryotic transcription and DNA repair complexes. However, the structural and dynamic properties of chromatin at high concentrations characteristic of the cellular environment (> ~200 mg/ml) are largely unexplored at the molecular level. Here, we apply magic angle spinning nuclear magnetic resonance to directly probe the dynamic histone protein regions in 13C,15N-enriched recombinant nucleosome arrays at cellular chromatin concentrations and conditions designed to emulate distinct states of DNA condensation, with focus on the flexible H3 and H4 N-terminal tails which mediate chromatin compaction. 2D 1H-13C and 1H-15N spectra reveal numerous correlations for H3 and H4 backbone and side-chain atoms, enabling identification of specific residues making up the dynamically disordered N-terminal tail domains. Remarkably, we find that both the H3 and H4 N-terminal tails are overall dynamic even in a highly condensed state. This significant conformational flexibility of the histone tails suggests that they remain available for protein binding in compact chromatin states to enable regulation of heterochromatin. Furthermore, our study provides a foundation for quantitative structural and dynamic investigations of chromatin at physiological concentrations.
PMID: 24088044 [PubMed - as supplied by publisher]
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Acc Chem Res. 2013 Feb 13;
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Abstract
In living organisms, biological molecules often organize into multicomponent complexes. Such assemblies consist of various proteins and carry out essential functions, ranging from cell division, transport, and energy transduction to catalysis, signaling, and viral...
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Abstract
G protein-coupled receptors (GPCRs) represent the largest family of membrane receptors and mediate a diversity of cellular processes. These receptors have a common seven-transmembrane helix structure, yet have evolved...
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Biochim Biophys Acta. 2011 Aug 3;
Authors: Gustavsson M, Traaseth NJ, Veglia G
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments....
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08-16-2011 01:19 PM
Solid-state photo-CIDNP effect observed in phototropin LOV1-C57S by (13)C magic-angle spinning NMR spectroscopy.
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Histone H3 and H4 N-Terminal Tails in Nucleosome Arrays at Cellular Concentrations Probed by Magic Angle Spinning NMR Spectroscopy.
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