scholarly journals Structural and biochemical analyses of monoubiquitinated human histones H2B and H4

Open Biology ◽  
2016 ◽  
Vol 6 (6) ◽  
pp. 160090 ◽  
Author(s):  
Shinichi Machida ◽  
Satoshi Sekine ◽  
Yuuki Nishiyama ◽  
Naoki Horikoshi ◽  
Hitoshi Kurumizaka
Keyword(s):  
Histone H4 ◽  
Core Particle ◽  
Post Translational Modification ◽  
Nucleosome Core Particle ◽  
Active Chromatin ◽  
Histone H2b ◽  
Nucleosome Core ◽  
Nucleosome Structure ◽  
Biochemical Analyses ◽  
Nucleosome Stability

Monoubiquitination is a major histone post-translational modification. In humans, the histone H2B K120 and histone H4 K31 residues are monoubiquitinated and may form transcriptionally active chromatin. In this study, we reconstituted nucleosomes containing H2B monoubiquitinated at position 120 (H2Bub 120 ) and/or H4 monoubiquitinated at position 31 (H4ub 31 ). We found that the H2Bub 120 and H4ub 31 monoubiquitinations differently affect nucleosome stability: the H2Bub 120 monoubiquitination enhances the H2A–H2B association with the nucleosome, while the H4ub 31 monoubiquitination decreases the H3–H4 stability in the nucleosome, when compared with the unmodified nucleosome. The H2Bub 120 and H4ub 31 monoubiquitinations both antagonize the Mg 2+ -dependent compaction of a poly-nucleosome, suggesting that these monoubiquitinations maintain more relaxed conformations of chromatin. In the crystal structure, the H2Bub 120 and H4ub 31 monoubiquitinations do not change the structure of the nucleosome core particle and the ubiquitin molecules were flexibly disordered in the H2Bub 120 /H4ub 31 nucleosome structure. These results revealed the differences and similarities of the H2Bub 120 and H4ub 31 monoubiquitinations at the mono- and poly-nucleosome levels and provide novel information to clarify the roles of monoubiquitination in chromatin.

scholarly journals The human telomeric nucleosome displays distinct structural and dynamic properties

2019 ◽  
Author(s):  
Aghil Soman ◽  
Chong Wai Liew ◽  
Hsiang Ling Teo ◽  
Nikolay V. Berezhnoy ◽  
Vincent Olieric ◽  
...  
Keyword(s):  
Molecular Level ◽  
Dynamic Properties ◽  
Dynamic Structure ◽  
Genomic Integrity ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Telomeric Dna ◽  
Nucleosome Core ◽  
Nucleosome Structure

ABSTRACTTelomeres protect the ends of our chromosomes and are key to maintaining genomic integrity during cell division and differentiation. However, our knowledge of telomeric chromatin and nucleosome structure at the molecular level is limited. Here, we aimed to define the structure, dynamics as well as properties in solution of the human telomeric nucleosome. We first determined the 2.2 Å crystal structure of a human telomeric nucleosome core particle (NCP) containing 145 bp DNA, which revealed the same helical path for the DNA as well as symmetric stretching in both halves of the NCP as that of the 145 bp ‘601’ NCP. In solution, the telomeric nucleosome exhibited a less stable and a markedly more dynamic structure compared to NCPs containing DNA positioning sequences. These observations provide molecular insights into how telomeric DNA forms nucleosomes and chromatin and advance our understanding of the unique biological role of telomeres.

scholarly journals Beyond the Xi

2005 ◽  
Vol 280 (16) ◽  
pp. 16437-16445 ◽  
Author(s):  
D. Wade Abbott ◽  
Brian P. Chadwick ◽  
Anita A. Thambirajah ◽  
Juan Ausió
Keyword(s):  
Gel Electrophoresis ◽  
Salt Precipitation ◽  
Core Particle ◽  
Post Translational Modification ◽  
Nucleosome Core Particle ◽  
Two Dimensional Gel Electrophoresis ◽  
X Chromosomes ◽  
Nucleosome Core ◽  
Nuclear Processes

MacroH2A (mH2A) is a histone variant that is enriched in the inactivated X-chromosomes of mammalian females. To characterize the role of this protein in other nuclear processes we isolated chromatin particles from chicken liver, a vertebrate system that does not undergo X-inactivation. Chromatin digestion and fractionation studies determined that mH2A is evenly distributed at several levels of chromatin structure and stabilizes the nucleosome core particle in solution. However, at the level of the chromatosome, selective salt precipitation showed the existence of a mutually exclusive relationship between mH2A and H1, which may reveal functional redundancy between these proteins. Two-dimensional gel electrophoresis demonstrated the presence of one major population of mH2A containing nucleosomes, which may become ADP-ribosylated. This report provides new clues into how mH2A distribution and a previously unidentified post-translational modification may help regulate the repression of autosomal chromatin.

scholarly journals The human telomeric nucleosome displays distinct structural and dynamic properties

2020 ◽  
Vol 48 (10) ◽  
pp. 5383-5396 ◽  
Author(s):  
Aghil Soman ◽  
Chong Wai Liew ◽  
Hsiang Ling Teo ◽  
Nikolay V Berezhnoy ◽  
Vincent Olieric ◽  
...  
Keyword(s):  
Molecular Level ◽  
Dynamic Properties ◽  
Dynamic Structure ◽  
Genomic Integrity ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Telomeric Dna ◽  
Nucleosome Core ◽  
Nucleosome Structure

Abstract Telomeres protect the ends of our chromosomes and are key to maintaining genomic integrity during cell division and differentiation. However, our knowledge of telomeric chromatin and nucleosome structure at the molecular level is limited. Here, we aimed to define the structure, dynamics as well as properties in solution of the human telomeric nucleosome. We first determined the 2.2 Å crystal structure of a human telomeric nucleosome core particle (NCP) containing 145 bp DNA, which revealed the same helical path for the DNA as well as symmetric stretching in both halves of the NCP as that of the 145 bp ‘601’ NCP. In solution, the telomeric nucleosome exhibited a less stable and a markedly more dynamic structure compared to NCPs containing DNA positioning sequences. These observations provide molecular insights into how telomeric DNA forms nucleosomes and chromatin and advance our understanding of the unique biological role of telomeres.

scholarly journals Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Masatoshi Wakamori ◽  
Yoshifumi Fujii ◽  
Noriyuki Suka ◽  
Mikako Shirouzu ◽  
Kensaku Sakamoto ◽  
...  
Keyword(s):  
Histone H4 ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core

scholarly journals Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions

2001 ◽  
Vol 20 (18) ◽  
pp. 5207-5218 ◽  
Author(s):  
Cindy L. White ◽  
Robert K. Suto ◽  
Karolin Luger
Keyword(s):  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core

Helical repeat of DNA in the nucleosome core particle

2000 ◽  
Vol 28 (4) ◽  
pp. 373-376 ◽  
Author(s):  
R. Negri ◽  
M. Buttinelli ◽  
G. Panetta ◽  
V. De Arcangelis ◽  
E. Di Mauro ◽  
...  
Keyword(s):  
Dna Sequences ◽  
Linker Histone ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Apparent Paradox ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
High Affinity Site ◽  
Hydroxyl Radical Cleavage ◽  
Radical Cleavage

Although the crystal structure of nucleosome core particle is essentially symmetrical in the vicinity of the dyad, the linker histone binds asymmetrically in this region to select a single high-affinity site from potentially two equivalent sites. To try to resolve this apparent paradox we mapped to base-pair resolution the dyads and rotational settings of nucleosome core particles reassembled on synthetic tandemly repeating 20 bp DNA sequences. In agreement with previous observations, we observed (1) that the helical repeat on each side of the dyad cluster is 10 bp maintaining register with the sequence repeat and (2) that this register changes by 2 bp in the vicinity of the dyad. The additional 2 bp required to effect the change in the rotational settings is accommodated by an adjustment immediately adjacent to the dyad. At the dyad the hydroxyl radical cleavage is asymmetric and we suggest that the inferred structural asymmetry could direct the binding of the linker histone to a single preferred site.

scholarly journals 3.9 Å structure of the nucleosome core particle determined by phase-plate cryo-EM

2016 ◽  
Vol 44 (17) ◽  
pp. 8013-8019 ◽  
Author(s):  
Eugene Y.D. Chua ◽  
Vinod K. Vogirala ◽  
Oviya Inian ◽  
Andrew S.W. Wong ◽  
Lars Nordenskiöld ◽  
...  
Keyword(s):  
Phase Plate ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core
Sign in / Sign up

Export Citation Format

Share Document