Literature DB >> 22227197

The effect of salt on oligocation-induced chromatin condensation.

Nikolay Korolev1, Yongqian Zhao, Abdollah Allahverdi, Khee Dong Eom, James P Tam, Lars Nordenskiöld.   

Abstract

Condensation of model chromatin in the form of fully saturated 12-mer nucleosome arrays, induced by addition of cationic ligands (ε-oligolysines with charge varied from +4 to +11), was studied in a range of KCl concentrations (10-500mM) using light scattering and precipitation assay titrations. The dependence of EC(50) (ligand concentration at the midpoint of the array condensation) on C(KCl) displays two regimes, a salt-independent at low C(KCl) and a salt-dependent at higher salt concentrations. In the salt-dependent regime EC(50) rises sharply with increase of C(KCl). Increase of ligand charge shifts the transition from the salt-independent to salt-dependent regime to higher salt. In the nucleosome array system, due to the partial neutralization of the DNA charge by histones, a lower oligocation concentration is needed to provoke condensation in the salt-independent regime compared to the related case of DNA condensation by the same cation. In the physiological range of salt concentrations (C(KCl)=50-300mM), K(+) ions assist array condensation by shifting EC(50) of the ε-oligolysines to lower values. At higher C(KCl), K(+) competes with the cationic ligands, which leads to increase of EC(50). Values of salt-dependent dissociation constant for the ε-oligolysine-nucleosome array interaction were obtained, by fitting to a general equation developed earlier for DNA, describing the dependence of EC(50) on dissociation constant, salt and polyelectrolyte concentrations.
Copyright © 2011 Elsevier Inc. All rights reserved.

Entities:  

Mesh:

Substances:

Year:  2011        PMID: 22227197     DOI: 10.1016/j.bbrc.2011.12.112

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  7 in total

1.  Opposing roles of H3- and H4-acetylation in the regulation of nucleosome structure––a FRET study.

Authors:  Alexander Gansen; Katalin Tóth; Nathalie Schwarz; Jörg Langowski
Journal:  Nucleic Acids Res       Date:  2015-02-18       Impact factor: 16.971

2.  The Influence of Ionic Environment and Histone Tails on Columnar Order of Nucleosome Core Particles.

Authors:  Nikolay V Berezhnoy; Ying Liu; Abdollah Allahverdi; Renliang Yang; Chun-Jen Su; Chuan-Fa Liu; Nikolay Korolev; Lars Nordenskiöld
Journal:  Biophys J       Date:  2016-04-26       Impact factor: 4.033

3.  An advanced coarse-grained nucleosome core particle model for computer simulations of nucleosome-nucleosome interactions under varying ionic conditions.

Authors:  Yanping Fan; Nikolay Korolev; Alexander P Lyubartsev; Lars Nordenskiöld
Journal:  PLoS One       Date:  2013-02-13       Impact factor: 3.240

4.  Chromatin compaction under mixed salt conditions: opposite effects of sodium and potassium ions on nucleosome array folding.

Authors:  Abdollah Allahverdi; Qinming Chen; Nikolay Korolev; Lars Nordenskiöld
Journal:  Sci Rep       Date:  2015-02-17       Impact factor: 4.379

5.  Atomic force microscopy of chromatin arrays reveal non-monotonic salt dependence of array compaction in solution.

Authors:  Katarzyna M Krzemien; Maximilian Beckers; Salina Quack; Jens Michaelis
Journal:  PLoS One       Date:  2017-03-15       Impact factor: 3.240

6.  Global histone protein surface accessibility in yeast indicates a uniformly loosely packed genome with canonical nucleosomes.

Authors:  Luke T Marr; Josefina Ocampo; David J Clark; Jeffrey J Hayes
Journal:  Epigenetics Chromatin       Date:  2021-01-11       Impact factor: 4.954

7.  Reconstituted TAD-size chromatin fibers feature heterogeneous nucleosome clusters.

Authors:  Nikolay Korolev; Anatoly Zinchenko; Aghil Soman; Qinming Chen; Sook Yi Wong; Nikolay V Berezhnoy; Rajib Basak; Johan R C van der Maarel; John van Noort; Lars Nordenskiöld
Journal:  Sci Rep       Date:  2022-09-16       Impact factor: 4.996

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.