Please use this identifier to cite or link to this item:
Title: Solid-state NMR 13C, 15N assignments of human histone H3 in the nucleosome core particle
Authors: Shi, Xiangyan
Prasanna, Chinmayi
Pervushin, Konstantin
Nordenskiöld, Lars
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Shi, X., Prasanna, C., Pervushin, K., & Nordenskiöld, L. (2020). Solid-state NMR 13C, 15N assignments of human histone H3 in the nucleosome core particle. Biomolecular NMR assignments, 14(1), 99–104.
Project: MOE2018-T2-1-112
Journal: Biomolecular NMR Assignments
Abstract: Nucleosome core particle (NCP), the basic unit of chromatin in eukaryotic cells, consists of ~ 147 bp DNA wrapped around a histone octamer (HO) formed by two H2A–H2B dimers and one (H3–H4)2 tetramer. Histones undergo various post-translational modifications (PTMs), which regulates genomic activities in different cellular phases. High-resolution structures have been solved for many nucleosomes primarily including NCPs. However, the atomic-resolution structures of nucleosome arrays and chromatin fiber, as well as the dynamics of nucleosomes remain poorly understood. Solid-state NMR (SSNMR) is one of the premier techniques to answer these questions. In this study, we present the 13C and 15N chemical shifts assignments for the globular domain of human histone H3 (hH3) using multidimensional SSNMR experiments. The obtained spectra are of outstanding resolution and the assignments are nearly 100% complete for the backbone 13C and 15N spins of R42–G132 and ~ 80% when taking into account the side chains. The secondary structure derived from the chemical shifts agrees with the previously reported X-ray crystal structure. The reported chemical shifts can be carried over to future SSNMR studies of structure and dynamics of hH3 in NCPs, nucleosome array, chromatin fibers and nucleosome-protein complexes.
ISSN: 1874-270X
DOI: 10.1007/s12104-020-09927-w
Rights: © 2020 Springer. This is a post-peer-review, pre-copyedit version of an article published in Biomolecular NMR Assignments. The final authenticated version is available online at:
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
Manuscript_Biomolecular NMR Assignments_DRNTU.pdf3.34 MBAdobe PDFView/Open

Citations 20

Updated on Jul 8, 2022

Citations 20

Updated on Jul 6, 2022

Page view(s)

Updated on Aug 7, 2022


Updated on Aug 7, 2022

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.