Reversibility of Structural Rearrangements in Mononucleosomes Induced by Ionic Strength

Feofanov, Аlexey V.; Андреева, Т. В.; Studitsky, Vasily M.; Kirpichnikov, Mikhaǐl P.

doi:10.3103/s0096392518030070

Cited by 4 publications

(3 citation statements)

References 15 publications

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“…4с). Our previous studies show that the structural changes occurring in nucleosomes during short (10 min) exposure to 700 mM KCl are fully reversible (Feofanov et al, 2018). Therefore, at KCl concentration of less than 700 mM, most of the observed structural changes are restricted by DNA uncoiling from histone octamer, which involves from 13 to 35 bp of nucleosome positioning sequence, and proceed without loss of core histones.…”

Section: Resultsmentioning

confidence: 97%

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

et al. 2021

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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.

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Section: Resultsmentioning

confidence: 97%

“…Only 70 and 50% of nucleosomes restore their initial structure after the short exposure to 1.0 and 1.3M KCl, respectively (Feofanov et al, 2018). At these concentrations, DNA uncoiling involves more than 35 bp and results in the dissociation of core histones, which is essentially irreversible at low ( ca .…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2021

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“…The single-particle Förster resonance energy transfer (spFRET) measurements were performed in the buffer (10 mM Tris-HCl pH 8.0, 0.5 mM EDTA) containing 0.15 M KCl as described in [ 27 ]. For the time course analysis at higher ionic strength, nucleosomes were diluted to a concentration of 1 nM in the buffer with 0.5 M KCl and measured by spFRET microscopy during the time periods of 0–7.5, 7.5–15, and 15–22.5 min after dilution [ 27 , 48 ].…”

Section: Methodsmentioning

confidence: 99%

N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro

Chang

Feofanov

Lyubitelev

et al. 2022

Cells

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Histone N-terminal tails and their post-translational modifications affect various biological processes, often in a context-specific manner; the underlying mechanisms are poorly studied. Here, the role of individual N-terminal tails of histones H2A/H2B during transcription through chromatin was analyzed in vitro. spFRET data suggest that the tail of histone H2B (but not of histone H2A) affects nucleosome stability. Accordingly, deletion of the H2B tail (amino acids 1–31, but not 1–26) causes a partial relief of the nucleosomal barrier to transcribing RNA polymerase II (Pol II), likely facilitating uncoiling of DNA from the histone octamer during transcription. Taken together, the data suggest that residues 27–31 of histone H2B stabilize DNA–histone interactions at the DNA region localized ~25 bp in the nucleosome and thus interfere with Pol II progression through the region localized 11–15 bp in the nucleosome. This function of histone H2B requires the presence of the histone H2A N-tail that mediates formation of nucleosome–nucleosome dimers; however, nucleosome dimerization per se plays only a minimal role during transcription. Histone chaperone FACT facilitates transcription through all analyzed nucleosome variants, suggesting that H2A/H2B tails minimally interact with FACT during transcription; therefore, an alternative FACT-interacting domain(s) is likely involved in this process.

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Our Journal–2020: What and How We Publish

Kirpichnikov

Моргунова

Хохлов

2020

Moscow Univ. Biol.Sci. Bull.

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Краткий обзор, посвященный последним изменениям в редакционной политике и содержании журнала «Вестник Московского университета. Серия 16. Биология» с особым акцентом на ситуацию с его англоязычной версией -«Moscow University Biological Sciences Bulletin». Описываются текущая стратегия рассмотрения редколлегией поступающих рукописей, их отклонения, рецензирования и редактирования, а также распределения работ по новым рубрикам издания. Рассматриваются требования к языку статей, составлению списков литературы и статистическому анализу полученных авторами данных. Приводятся как информация о росте наукометрических показателей журнала за последние годы, так и список баз данных, в которых издание индексируется в настоящее время. Отмечаются различия в интересе к опубликованным статьям между зарубежными и отечественными читателями. Приводятся данные о количестве скачиваний наиболее популярных статей с интернет-сайта издательства Springer Nature. Анализируются тематики статей, опубликованных в журнале в 2017-2019 гг. Подчеркивается приоритетность для редколлегии обзоров, затрагивающих как фундаментальные, так и прикладные аспекты исследований в области биологии, биомедицины и биотехнологии.

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Reversibility of Structural Rearrangements in Mononucleosomes Induced by Ionic Strength

Cited by 4 publications

References 15 publications

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

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

N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro

Our Journal–2020: What and How We Publish

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Reversibility of Structural Rearrangements in Mononucleosomes Induced by Ionic Strength

Cited by 4 publications

References 15 publications

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

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

N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro

Our Journal–2020: What and How We Publish

Contact Info

Product

Resources

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

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