Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy. / Sun, Wenjun; Lebedenko, Olga O.; Salguero, Nicole Gonzalez; Shannon, Matthew D.; Zandian, Mohamad; Poirier, Michael G.; Skrynnikov, Nikolai R.; Jaroniec, Christopher P.
в: Journal of the American Chemical Society, Том 145, № 46, 22.11.2023, стр. 25478-25485.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy
AU - Sun, Wenjun
AU - Lebedenko, Olga O.
AU - Salguero, Nicole Gonzalez
AU - Shannon, Matthew D.
AU - Zandian, Mohamad
AU - Poirier, Michael G.
AU - Skrynnikov, Nikolai R.
AU - Jaroniec, Christopher P.
N1 - Publisher: American Chemical Society
PY - 2023/11/22
Y1 - 2023/11/22
N2 - The fundamental repeat unit of chromatin, the nucleosome, consists of approximately 147 base pairs of double-stranded DNA and a histone protein octamer containing two copies each of histones H2A, H2B, H3, and H4. Each histone possesses a dynamically disordered N-terminal tail domain, and it is well-established that the tails of histones H3 and H4 play key roles in chromatin compaction and regulation. Here we investigate the conformational ensemble and interactions of the H4 tail in nucleosomes by means of solution NMR measurements of paramagnetic relaxation enhancements (PREs) in recombinant samples reconstituted with 15N-enriched H4 and nitroxide spin-label tagged H3. The experimental PREs, which report on the proximities of individual H4 tail residues to the different H3 spin-label sites, are interpreted by using microsecond time-scale molecular dynamics simulations of the nucleosome core particle. Collectively, these data enable improved localization of histone H4 tails in nucleosomes and support the notion that H4 tails engage in a fuzzy complex interaction with nucleosomal DNA.
AB - The fundamental repeat unit of chromatin, the nucleosome, consists of approximately 147 base pairs of double-stranded DNA and a histone protein octamer containing two copies each of histones H2A, H2B, H3, and H4. Each histone possesses a dynamically disordered N-terminal tail domain, and it is well-established that the tails of histones H3 and H4 play key roles in chromatin compaction and regulation. Here we investigate the conformational ensemble and interactions of the H4 tail in nucleosomes by means of solution NMR measurements of paramagnetic relaxation enhancements (PREs) in recombinant samples reconstituted with 15N-enriched H4 and nitroxide spin-label tagged H3. The experimental PREs, which report on the proximities of individual H4 tail residues to the different H3 spin-label sites, are interpreted by using microsecond time-scale molecular dynamics simulations of the nucleosome core particle. Collectively, these data enable improved localization of histone H4 tails in nucleosomes and support the notion that H4 tails engage in a fuzzy complex interaction with nucleosomal DNA.
KW - Chromatin
KW - DNA/chemistry
KW - Histones/chemistry
KW - Magnetic Resonance Spectroscopy
KW - Nucleic Acid Conformation
KW - Nucleosomes
UR - https://www.mendeley.com/catalogue/6d214cb8-953d-3fb3-a7a8-29c6060c4acd/
U2 - 10.1021/jacs.3c10340
DO - 10.1021/jacs.3c10340
M3 - Article
C2 - 37943892
VL - 145
SP - 25478
EP - 25485
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 46
ER -
ID: 114036633