Na+ and K+ Ions Differently Affect Nucleosome Structure, Stability, and Interactions with Proteins.
Microsc Microanal, 2022/02;28(1):243-253.
Andreeva TV[1], Maluchenko NV[1], Sivkina AL[1], Chertkov OV[1], Valieva ME[1], Kotova EY[2], Kirpichnikov MP[1, 3], Studitsky VM[1, 2], Feofanov AV[1, 3]
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PMID: 35177143DOI: 10.1017/S1431927621013751
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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: FACT; RNA polymerase II; nucleosome; poly(ADP-ribose) polymerase 1; potassium ion; sodium ion; structure
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