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

Tatyana V. Andreeva, Natalya V. Maluchenko, Anastasiia L. Sivkina, Oleg V. Chertkov, Maria E. Valieva, Elena Y. Kotova, Mikhail P. Kirpichnikov, Vasily M. Studitsky, Alexey V. Feofanov

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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.

Original languageEnglish
Pages (from-to)243-253
Number of pages11
JournalMicroscopy and Microanalysis
Volume28
Issue number1
DOIs
StatePublished - Feb 6 2022

Keywords

  • FACT
  • RNA polymerase II
  • nucleosome
  • poly(ADP-ribose) polymerase 1
  • potassium ion
  • sodium ion
  • structure
  • Chromatin
  • DNA
  • Ions
  • Nucleosomes

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