TY - JOUR
T1 - Na+and K+Ions Differently Affect Nucleosome Structure, Stability, and Interactions with Proteins
AU - Andreeva, Tatyana V.
AU - Maluchenko, Natalya V.
AU - Sivkina, Anastasiia L.
AU - Chertkov, Oleg V.
AU - Valieva, Maria E.
AU - Kotova, Elena Y.
AU - Kirpichnikov, Mikhail P.
AU - Studitsky, Vasily M.
AU - Feofanov, Alexey V.
N1 - Publisher Copyright:
Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of the Microscopy Society of America.
PY - 2022/2/6
Y1 - 2022/2/6
N2 - 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.
AB - 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.
KW - FACT
KW - RNA polymerase II
KW - nucleosome
KW - poly(ADP-ribose) polymerase 1
KW - potassium ion
KW - sodium ion
KW - structure
KW - Chromatin
KW - DNA
KW - Ions
KW - Nucleosomes
UR - http://www.scopus.com/inward/record.url?scp=85120742594&partnerID=8YFLogxK
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=purepublist2023&SrcAuth=WosAPI&KeyUT=WOS:000757458900022&DestLinkType=FullRecord&DestApp=WOS
U2 - 10.1017/S1431927621013751
DO - 10.1017/S1431927621013751
M3 - Article
C2 - 35177143
SN - 1431-9276
VL - 28
SP - 243
EP - 253
JO - Microscopy and Microanalysis
JF - Microscopy and Microanalysis
IS - 1
ER -