Salt-induced conformation and interaction changes of nucleosome core particles
- PMID: 11751321
- PMCID: PMC1302474
- DOI: 10.1016/S0006-3495(02)75399-X
Salt-induced conformation and interaction changes of nucleosome core particles
Abstract
Small angle x-ray scattering was used to follow changes in the conformation and interactions of nucleosome core particles (NCP) as a function of the monovalent salt concentration C(s). The maximal extension (D(max)) of the NCP (145 +/- 3-bp DNA) increases from 137 +/- 5 A to 165 +/- 5 A when C(s) rises from 10 to 50 mM and remains constant with further increases of C(s) up to 200 mM. In view of the very weak increase of the R(g) value in the same C(s) range, we attribute this D(max) variation to tail extension, a proposal confirmed by simulations of the entire I(q) curves, considering an ideal solution of particles with tails either condensed or extended. This tail extension is observed at higher salt values when particles contain longer DNA fragments (165 +/- 10 bp). The maximal extension of the tails always coincides with the screening of repulsive interactions between particles. The second virial coefficient becomes smaller than the hard sphere virial coefficient and eventually becomes negative (net attractive interactions) for NCP(145). Addition of salt simultaneously screens Coulombic repulsive interactions between NCP and Coulombic attractive interactions between tails and DNA inside the NCP. We discuss how the coupling of these two phenomena may be of biological relevance.
Similar articles
-
H2A and H2B tails are essential to properly reconstitute nucleosome core particles.Eur Biophys J. 2007 Nov;36(8):1083-94. doi: 10.1007/s00249-007-0212-9. Epub 2007 Sep 19. Eur Biophys J. 2007. PMID: 17882413
-
Role of histone tails in the conformation and interactions of nucleosome core particles.Biochemistry. 2004 Apr 27;43(16):4773-80. doi: 10.1021/bi036210g. Biochemistry. 2004. PMID: 15096046
-
Computer modeling reveals that modifications of the histone tail charges define salt-dependent interaction of the nucleosome core particles.Biophys J. 2009 Mar 18;96(6):2082-94. doi: 10.1016/j.bpj.2008.10.073. Biophys J. 2009. PMID: 19289035 Free PMC article.
-
Computer modeling demonstrates that electrostatic attraction of nucleosomal DNA is mediated by histone tails.Biophys J. 2006 Jun 15;90(12):4305-16. doi: 10.1529/biophysj.105.080226. Epub 2006 Mar 24. Biophys J. 2006. PMID: 16565063 Free PMC article.
-
Cation-induced polyelectrolyte-polyelectrolyte attraction in solutions of DNA and nucleosome core particles.Adv Colloid Interface Sci. 2010 Jul 12;158(1-2):32-47. doi: 10.1016/j.cis.2009.08.002. Epub 2009 Aug 26. Adv Colloid Interface Sci. 2010. PMID: 19758583 Review.
Cited by
-
EGFP-tagged core and linker histones diffuse via distinct mechanisms within living cells.Biophys J. 2006 Sep 15;91(6):2326-36. doi: 10.1529/biophysj.105.079343. Epub 2006 Jun 30. Biophys J. 2006. PMID: 16815908 Free PMC article.
-
Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2-nucleosome complexes.Nucleic Acids Res. 2011 May;39(10):4122-35. doi: 10.1093/nar/gkr005. Epub 2011 Jan 29. Nucleic Acids Res. 2011. PMID: 21278419 Free PMC article.
-
H2A and H2B tails are essential to properly reconstitute nucleosome core particles.Eur Biophys J. 2007 Nov;36(8):1083-94. doi: 10.1007/s00249-007-0212-9. Epub 2007 Sep 19. Eur Biophys J. 2007. PMID: 17882413
-
Nucleosome shape dictates chromatin fiber structure.Biophys J. 2009 Feb;96(3):777-84. doi: 10.1016/j.bpj.2008.09.055. Biophys J. 2009. PMID: 19186120 Free PMC article.
-
Solution scattering and FRET studies on nucleosomes reveal DNA unwrapping effects of H3 and H4 tail removal.PLoS One. 2013 Nov 12;8(11):e78587. doi: 10.1371/journal.pone.0078587. eCollection 2013. PLoS One. 2013. PMID: 24265699 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources