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Na+ and K+ Ions Differently Affect Nucleosome Structure, Stability, and Interactions with Proteins

Published online by Cambridge University Press:  01 December 2021

Tatyana V. Andreeva ,
Natalya V. Maluchenko ,
Anastasiia L. Sivkina ,
Oleg V. Chertkov ,
Maria E. Valieva Open the ORCID record for Maria E. Valieva [Opens in a new window] ,
Elena Y. Kotova ,
Mikhail P. Kirpichnikov ,
Vasily M. Studitsky  and
Alexey V. Feofanov Open the ORCID record for Alexey V. Feofanov [Opens in a new window]
Tatyana V. Andreeva
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia
Natalya V. Maluchenko
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia
Anastasiia L. Sivkina
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia
Oleg V. Chertkov
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia
Maria E. Valieva
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia
Elena Y. Kotova
Affiliation:
Fox Chase Cancer Center, Philadelphia, PA 19111-2497, USA
Mikhail P. Kirpichnikov
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia
Vasily M. Studitsky
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia Fox Chase Cancer Center, Philadelphia, PA 19111-2497, USA
Alexey V. Feofanov*
Affiliation:
Biology Faculty, Lomonosov Moscow State University, Moscow 119234, Russia Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia
*
*Corresponding author: Alexey V. Feofanov, E-mail: [email protected]
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Abstract

Inorganic ions are essential factors stabilizing nucleosome structure; however, many aspects of their effects on DNA transactions in chromatin remain unknown. Here, differential effects of K+ and Na+ on the nucleosome structure, stability, and interactions with protein complex FACT (FAcilitates Chromatin Transcription), poly(ADP-ribose) polymerase 1, and RNA polymerase II were studied using primarily single-particle Förster resonance energy transfer microscopy. The maximal stabilizing effect of K+ on a nucleosome structure was observed at ca. 80–150 mM, and it decreased slightly at 40 mM and considerably at >300 mM. The stabilizing effect of Na+ is noticeably lower than that of K+ and progressively decreases at ion concentrations higher than 40 mM. At 150 mM, Na+ ions support more efficient reorganization of nucleosome structure by poly(ADP-ribose) polymerase 1 and ATP-independent uncoiling of nucleosomal DNA by FACT as compared with K+ ions. In contrast, transcription through a nucleosome is nearly insensitive to K+ or Na+ environment. Taken together, the data indicate that K+ environment is more preserving for chromatin structure during various nucleosome transactions than Na+ environment.

Keywords

FACTnucleosomepoly(ADP-ribose) polymerase 1potassium ionRNA polymerase IIsodium ionstructure
Type
Biological Applications
Information
Microscopy and Microanalysis , Volume 28 , Issue 1 , February 2022 , pp. 243 - 253
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Copyright
Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of the Microscopy Society of America

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