Faculty Opinions recommendation of Structure of RCC1 chromatin factor bound to the nucleosome core particle.

2010 ◽  
Author(s):  
Yixian Zheng
Keyword(s):  
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

The Crystal Structure of the Nucleosome Core Particle by Contrast Variation

1984 ◽  
pp. 105-117
Author(s):  
Graham A. Bentley ◽  
John T. Finch ◽  
Anita Lewit-Bentley ◽  
Michel Roth
Keyword(s):  
Crystal Structure ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Contrast Variation ◽  
Nucleosome Core

scholarly journals Primary organization of nucleosome core particle of chromatin: sequence of histone arrangement along DNA.

1978 ◽  
Vol 75 (9) ◽  
pp. 4184-4188 ◽  
Author(s):  
A. D. Mirzabekov ◽  
V. V. Shick ◽  
A. V. Belyavsky ◽  
S. G. Bavykin
Keyword(s):  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core ◽  
Primary Organization

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 A Systematic Study of Nucleosome Core Particle and Nucleosome-Nucleosome Stacking Structure

2018 ◽  
Vol 114 (3) ◽  
pp. 254a
Author(s):  
Nikolay Korolev ◽  
Alexander P. Lyubartsev ◽  
Lars Nordenskiöld
Keyword(s):  
Systematic Study ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core ◽  
Stacking Structure
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