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Biophys J
2015 Oct 20;1098:1676-85. doi: 10.1016/j.bpj.2015.07.004.
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Nucleosome Core Particle Disassembly and Assembly Kinetics Studied Using Single-Molecule Fluorescence.
Hazan NP
,
Tomov TE
,
Tsukanov R
,
Liber M
,
Berger Y
,
Masoud R
,
Toth K
,
Langowski J
,
Nir E
.
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The stability of the nucleosome core particle (NCP) is believed to play a major role in regulation of gene expression. To understand the mechanisms that influence NCP stability, we studied stability and dissociation and association kinetics under different histone protein (NCP) and NaCl concentrations using single-pair Förster resonance energy transfer and alternating laser excitation techniques. The method enables distinction between folded, unfolded, and intermediate NCP states and enables measurements at picomolar to nanomolar NCP concentrations where dissociation and association reactions can be directly observed. We reproduced the previously observed nonmonotonic dependence of NCP stability on NaCl concentration, and we suggest that this rather unexpected behavior is a result of interplay between repulsive and attractive forces within positively charged histones and between the histones and the negatively charged DNA. Higher NaCl concentrations decrease the attractive force between the histone proteins and the DNA but also stabilize H2A/H2B histone dimers, and possibly (H3/H4)2 tetramers. An intermediate state in which one DNA arm is unwrapped, previously observed at high NaCl concentrations, is also explained by this salt-induced stabilization. The strong dependence of NCP stability on ion and histone concentrations, and possibly on other charged macromolecules, may play a role in chromosomal morphology.
Akey,
Histone chaperones and nucleosome assembly.
2003, Pubmed
Akey,
Histone chaperones and nucleosome assembly.
2003,
Pubmed
Andrews,
The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions.
2010,
Pubmed
,
Xenbase
Biswas,
Role of histone tails in structural stability of the nucleosome.
2011,
Pubmed
Böhm,
Nucleosome accessibility governed by the dimer/tetramer interface.
2011,
Pubmed
Bönisch,
H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilization.
2012,
Pubmed
Claudet,
Histone octamer instability under single molecule experiment conditions.
2005,
Pubmed
Dyer,
Reconstitution of nucleosome core particles from recombinant histones and DNA.
2004,
Pubmed
Erler,
The role of histone tails in the nucleosome: a computational study.
2014,
Pubmed
Gansen,
Nucleosome disassembly intermediates characterized by single-molecule FRET.
2009,
Pubmed
Gansen,
Closing the gap between single molecule and bulk FRET analysis of nucleosomes.
2013,
Pubmed
Gansen,
Single-pair fluorescence resonance energy transfer of nucleosomes in free diffusion: optimizing stability and resolution of subpopulations.
2007,
Pubmed
Gansen,
Structural variability of nucleosomes detected by single-pair Förster resonance energy transfer: histone acetylation, sequence variation, and salt effects.
2009,
Pubmed
,
Xenbase
Gloss,
The effect of salts on the stability of the H2A-H2B histone dimer.
2002,
Pubmed
,
Xenbase
Gottesfeld,
Energetics and affinity of the histone octamer for defined DNA sequences.
2001,
Pubmed
Hoch,
Protein-protein Förster resonance energy transfer analysis of nucleosome core particles containing H2A and H2A.Z.
2007,
Pubmed
,
Xenbase
Karantza,
Thermodynamic studies of the core histones: pH and ionic strength effects on the stability of the (H3-H4)/(H3-H4)2 system.
1996,
Pubmed
Karantza,
Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability.
1995,
Pubmed
Karantza,
Thermodynamic studies of the core histones: stability of the octamer subunits is not altered by removal of their terminal domains.
2001,
Pubmed
Kelbauskas,
Sequence-dependent variations associated with H2A/H2B depletion of nucleosomes.
2008,
Pubmed
Koopmans,
Single-pair FRET microscopy reveals mononucleosome dynamics.
2007,
Pubmed
Koopmans,
spFRET using alternating excitation and FCS reveals progressive DNA unwrapping in nucleosomes.
2009,
Pubmed
Koopmans,
Nucleosome immobilization strategies for single-pair FRET microscopy.
2008,
Pubmed
Li,
Nucleosomes facilitate their own invasion.
2004,
Pubmed
,
Xenbase
Li,
Rapid spontaneous accessibility of nucleosomal DNA.
2005,
Pubmed
Lovullo,
A fluorescence resonance energy transfer-based probe to monitor nucleosome structure.
2005,
Pubmed
Luo,
Single molecule fluorescence methodologies for investigating transcription factor binding kinetics to nucleosomes and DNA.
2014,
Pubmed
,
Xenbase
Masoud,
Studying the structural dynamics of bipedal DNA motors with single-molecule fluorescence spectroscopy.
2012,
Pubmed
Nir,
Shot-noise limited single-molecule FRET histograms: comparison between theory and experiments.
2006,
Pubmed
Olins,
Spheroid chromatin units (v bodies).
1974,
Pubmed
Oohara,
Spectroscopic studies on histone-DNA interactions. II. Three transitions in nucleosomes resolved by salt-titration.
1987,
Pubmed
Park,
A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome.
2004,
Pubmed
,
Xenbase
Potoyan,
Regulation of the H4 tail binding and folding landscapes via Lys-16 acetylation.
2012,
Pubmed
Thåström,
Histone-DNA binding free energy cannot be measured in dilution-driven dissociation experiments.
2004,
Pubmed
,
Xenbase
Tomov,
Disentangling subpopulations in single-molecule FRET and ALEX experiments with photon distribution analysis.
2012,
Pubmed
Tomschik,
Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer.
2005,
Pubmed
Tomschik,
Nucleosome dynamics as studied by single-pair fluorescence resonance energy transfer: a reevaluation.
2009,
Pubmed
Tóth,
Histone- and DNA sequence-dependent stability of nucleosomes studied by single-pair FRET.
2013,
Pubmed
,
Xenbase
Tsukanov,
Detailed study of DNA hairpin dynamics using single-molecule fluorescence assisted by DNA origami.
2013,
Pubmed
Tsukanov,
Conformational dynamics of DNA hairpins at millisecond resolution obtained from analysis of single-molecule FRET histograms.
2013,
Pubmed
White,
Defined structural changes occur in a nucleosome upon Amt1 transcription factor binding.
2004,
Pubmed
,
Xenbase
Workman,
Alteration of nucleosome structure as a mechanism of transcriptional regulation.
1998,
Pubmed
Yager,
Dynamics and equilibria of nucleosomes at elevated ionic strength.
1984,
Pubmed
Yager,
Salt-induced release of DNA from nucleosome core particles.
1989,
Pubmed
Zlatanova,
The nucleosome family: dynamic and growing.
2009,
Pubmed
